# refs

id: PMID:37164017
data:
  {"abstract":"Most eukaryotes respire oxygen, using it to generate biomass and energy. However, a few organisms have lost the capacity to respire. Understanding how they manage biomass and energy production may illuminate the critical points at which respiration feeds into central carbon metabolism and explain possible routes to its optimization. Here, we use two related fission yeasts, Schizosaccharomyces pombe and Schizosaccharomyces japonicus, as a comparative model system. We show that although S. japonicus does not respire oxygen, unlike S. pombe, it is capable of efficient NADH oxidation, amino acid synthesis, and ATP generation. We probe possible optimization strategies through the use of stable isotope tracing metabolomics, mass isotopologue distribution analysis, genetics, and physiological experiments. S. japonicus appears to have optimized cytosolic NADH oxidation via glycerol-3-phosphate synthesis. It runs a fully bifurcated TCA pathway, sustaining amino acid production. Finally, we propose that it has optimized glycolysis to maintain high ATP/ADP ratio, in part by using the pentose phosphate pathway as a glycolytic shunt, reducing allosteric inhibition of glycolysis and supporting biomass generation. By comparing two related organisms with vastly different metabolic strategies, our work highlights the versatility and plasticity of central carbon metabolism in eukaryotes, illuminating critical adaptations supporting the preferential use of glycolysis over oxidative phosphorylation.","alleles_by_uniquename":{"SJAG_00409:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00409","name":"gpd1delta","uniquename":"SJAG_00409:allele-1"},"SJAG_00601:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00601","name":"rip1delta","uniquename":"SJAG_00601:allele-1"},"SJAG_01355:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01355","name":"cox6delta","uniquename":"SJAG_01355:allele-1"},"SJAG_01753:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01753","name":"mdh1delta","uniquename":"SJAG_01753:allele-1"},"SJAG_02796:allele-1":{"allele_type":"amino_acid_mutation","description":"A343T","gene_uniquename":"SJAG_02796","name":"pyk1-A343T","uniquename":"SJAG_02796:allele-1"},"SJAG_03920:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03920","name":"sdh3delta","uniquename":"SJAG_03920:allele-1"},"SJAG_04843:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04843","name":"fum1delta","uniquename":"SJAG_04843:allele-1"}},"annotation_curators":[{"annotation_count":20,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2023-05-18","authors":"Alam S, Gu Y, Reichert P, Bähler J, Oliferenko S","authors_abbrev":"Alam S et al.","canto_added_date":"2023-05-12 00:40:04","canto_annotation_status":"APPROVED","canto_approved_date":"2024-07-03 11:37:10","canto_approver_orcid":"0000-0001-6330-7526","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2023-05-18 12:11:54","canto_session_key":"94bcbfb72cf94809","canto_session_submitted_date":"2023-05-18 12:11:43","canto_triage_status":"Curatable","citation":"Curr Biol 2023 Apr 30;","cv_annotations":{"single_locus_phenotype":[{"annotations":[115468],"is_not":false,"summary":null,"term":"FYPO:0007363"},{"annotations":[115466],"is_not":false,"summary":null,"term":"FYPO:0000026"},{"annotations":[115465],"is_not":false,"summary":null,"term":"FYPO:0001355"},{"annotations":[115467],"is_not":false,"summary":null,"term":"FYPO:0001489"},{"annotations":[115469],"is_not":false,"summary":null,"term":"FYPO:0004165"},{"annotations":[115463,115464],"is_not":false,"summary":null,"term":"FYPO:0007790"},{"annotations":[115457,115460],"is_not":false,"summary":null,"term":"FYPO:0000760"},{"annotations":[115459,115462],"is_not":false,"summary":null,"term":"FYPO:0000579"},{"annotations":[115458,115461],"is_not":false,"summary":null,"term":"FYPO:0000590"},{"annotations":[115454,115455,115456],"is_not":false,"summary":null,"term":"FYPO:0001357"},{"annotations":[115453],"is_not":false,"summary":null,"term":"FYPO:0001234"},{"annotations":[115470,115471,115472],"is_not":false,"summary":null,"term":"FYPO:0002058"}]},"doi":"10.1016/j.cub.2023.04.046","gene_count":7,"genes_by_uniquename":{"SJAG_00409":null,"SJAG_00601":null,"SJAG_01355":null,"SJAG_01753":null,"SJAG_02796":null,"SJAG_03920":null,"SJAG_04843":null},"genotypes_by_uniquename":{"cox6delta":{"display_name":"cox6delta","display_uniquename":"cox6delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01355:allele-1","expression":"Null"}]}]},"fum1delta":{"display_name":"fum1delta","display_uniquename":"fum1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04843:allele-1","expression":"Null"}]}]},"gpd1delta":{"display_name":"gpd1delta","display_uniquename":"gpd1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00409:allele-1","expression":"Null"}]}]},"mdh1delta":{"display_name":"mdh1delta","display_uniquename":"mdh1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01753:allele-1","expression":"Null"}]}]},"pyk1-A343T-A343T-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"pyk1-A343T(aa)","display_uniquename":"pyk1-A343T-A343T-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02796:allele-1","expression":"Not assayed or wild type"}]}]},"rip1delta":{"display_name":"rip1delta","display_uniquename":"rip1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00601:allele-1","expression":"Null"}]}]},"sdh3delta":{"display_name":"sdh3delta","display_uniquename":"sdh3delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03920:allele-1","expression":"Null"}]}]}},"ltp_gene_count":7,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-05-10","pubmed_publication_date":"30 Apr 2023","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000015":null,"FYECO:0000126":null,"FYECO:0000137":null,"FYPO:0000026":null,"FYPO:0000579":null,"FYPO:0000590":null,"FYPO:0000760":null,"FYPO:0001234":null,"FYPO:0001355":null,"FYPO:0001357":null,"FYPO:0001489":null,"FYPO:0002058":null,"FYPO:0004165":null,"FYPO:0007363":null,"FYPO:0007790":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null},"title":"Optimization of energy production and central carbon metabolism in a non-respiring eukaryote.","uniquename":"PMID:37164017"}


id: PMID:34198697
data:
  {"abstract":"Mitogen activated protein kinase (MAPK) signaling pathways execute essential functions in eukaryotic organisms by transducing extracellular stimuli into adaptive cellular responses. In the fission yeast model  Schizosaccharomyces pombe  the cell integrity pathway (CIP) and its core effector, MAPK Pmk1, play a key role during regulation of cell integrity, cytokinesis, and ionic homeostasis.  Schizosaccharomyces japonicus , another fission yeast species, shows remarkable differences with respect to  S. pombe , including a robust yeast to hyphae dimorphism in response to environmental changes. We show that the CIP MAPK module architecture and its upstream regulators, PKC orthologs Pck1 and Pck2, are conserved in both fission yeast species. However, some of  S. pombe 's CIP-related functions, such as cytokinetic control and response to glucose availability, are regulated differently in  S. japonicus.  Moreover, Pck1 and Pck2 antagonistically regulate  S. japonicus  hyphal differentiation through fine-tuning of Pmk1 activity. Chimeric MAPK-swapping experiments revealed that  S. japonicus  Pmk1 is fully functional in  S. pombe , whereas  S. pombe  Pmk1 shows a limited ability to execute CIP functions and promote  S. japonicus  mycelial development. Our findings also suggest that a modified N-lobe domain secondary structure within  S. japonicus  Pmk1 has a major influence on the CIP signaling features of this evolutionarily diverged fission yeast.","alleles_by_uniquename":{"SJAG_00610:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00610","name":"pck2delta","uniquename":"SJAG_00610:allele-1"},"SJAG_01787:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01787","name":"pck1delta","uniquename":"SJAG_01787:allele-1"},"SJAG_02592:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02592","name":"sty1delta","uniquename":"SJAG_02592:allele-1"},"SJAG_04551:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04551","name":"pmk1delta","uniquename":"SJAG_04551:allele-1"},"SJAG_04551:allele-2":{"allele_type":"amino_acid_insertion","description":"82-NITCIYDLDIIINPYNFNEVYIYEE-105","gene_uniquename":"SJAG_04551","name":"Pmk1Sj(ins82-105)","uniquename":"SJAG_04551:allele-2"},"SJAG_04551:allele-3":{"allele_type":"other","description":"Pmk1 from S. pombe","gene_uniquename":"SJAG_04551","name":"Pmk1Sp","uniquename":"SJAG_04551:allele-3"},"SJAG_04551:allele-4":{"allele_type":"partial_amino_acid_deletion","description":"Pmk1 from S. pombe with deleted residues 82-105","gene_uniquename":"SJAG_04551","name":"Pmk1Sp(delta82-105)","uniquename":"SJAG_04551:allele-4"}},"annotation_curators":[{"annotation_count":34,"community_curator":true,"file_name":null,"file_type":null,"name":"Elisa Gomez Gil","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-09-14","authors":"Gómez-Gil E, Franco A, Vázquez-Marín B, Prieto-Ruiz F, Pérez-Díaz A, Vicente-Soler J, Madrid M, Soto T, Cansado J","authors_abbrev":"Gómez-Gil E et al.","canto_added_date":"2021-09-14 16:45:58","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-14 21:32:21","canto_approver_orcid":"0000-0002-8138-6851","canto_curator_name":"Elisa Gomez Gil","canto_curator_role":"community","canto_first_approved_date":"2021-09-14 21:32:21","canto_session_key":"0ba747685c452996","canto_session_submitted_date":"2021-09-14 17:59:01","canto_triage_status":"Curatable","citation":"J Fungi (Basel) 2021 Jun 14;7(6)","cv_annotations":{"PSI-MOD":[{"annotations":[115384,115385,115386],"is_not":false,"summary":null,"term":"MOD:00696"}],"cellular_component":[{"annotations":[115383],"is_not":false,"summary":null,"term":"GO:0005737"},{"annotations":[115382],"is_not":false,"summary":null,"term":"GO:0005634"}],"multi_locus_phenotype":[{"annotations":[115400],"is_not":false,"summary":null,"term":"FYPO:0007780"}],"single_locus_phenotype":[{"annotations":[115398,115406],"is_not":false,"summary":null,"term":"FYPO:0002678"},{"annotations":[115405],"is_not":false,"summary":null,"term":"FYPO:0002033"},{"annotations":[115387,115399,115403,115408,115411],"is_not":false,"summary":null,"term":"FYPO:0007776"},{"annotations":[115388,115404,115409,115412],"is_not":false,"summary":null,"term":"FYPO:0007780"},{"annotations":[115397,115401],"is_not":false,"summary":null,"term":"FYPO:0001838"},{"annotations":[115392],"is_not":false,"summary":null,"term":"FYPO:0007775"},{"annotations":[115393],"is_not":false,"summary":null,"term":"FYPO:0007779"},{"annotations":[115394],"is_not":false,"summary":null,"term":"FYPO:0002680"},{"annotations":[115391],"is_not":false,"summary":null,"term":"FYPO:0001038"},{"annotations":[115379],"is_not":false,"summary":null,"term":"FYPO:0004295"},{"annotations":[115389],"is_not":false,"summary":null,"term":"FYPO:0005152"},{"annotations":[115381,115396,115402,115407,115410],"is_not":false,"summary":null,"term":"FYPO:0007521"},{"annotations":[115380,115395],"is_not":false,"summary":null,"term":"FYPO:0000079"},{"annotations":[115390],"is_not":false,"summary":null,"term":"FYPO:0007522"}]},"doi":"10.3390/jof7060482","gene_count":4,"genes_by_uniquename":{"SJAG_00610":null,"SJAG_01787":null,"SJAG_02592":null,"SJAG_04551":null},"genotypes_by_uniquename":{"Pmk1Sj(ins82-105)-82-NITCIYDLDIIINPYNFNEVYIYEE-105-amino_acid_insertion-expression-not_assayed_or_wild_type":{"display_name":"Pmk1Sj(ins82-105)(82-NITCIYDLDIIINPYNFNEVYIYEE-105)","display_uniquename":"Pmk1Sj(ins82-105)-82-NITCIYDLDIIINPYNFNEVYIYEE-105-amino_acid_insertion-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-2","expression":"Not assayed or wild type"}]}]},"Pmk1Sp(delta82-105)-Pmk1_from_S._pombe_with_deleted_residues_82-105-partial_amino_acid_deletion-expression-not_assayed_or_wild_type":{"display_name":"Pmk1Sp(delta82-105)(Pmk1 from S. pombe with deleted residues 82-105 Δaa)","display_uniquename":"Pmk1Sp(delta82-105)-Pmk1_from_S._pombe_with_deleted_residues_82-105-partial_amino_acid_deletion-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-4","expression":"Not assayed or wild type"}]}]},"Pmk1Sp-Pmk1_from_S._pombe-other-expression-not_assayed_or_wild_type":{"display_name":"Pmk1Sp(Pmk1 from S. pombe)","display_uniquename":"Pmk1Sp-Pmk1_from_S._pombe-other-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-3","expression":"Not assayed or wild type"}]}]},"pck1delta":{"display_name":"pck1delta","display_uniquename":"pck1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01787:allele-1","expression":"Null"}]}]},"pck1delta__pmk1delta":{"display_name":"pck1delta pmk1delta","display_uniquename":"pck1delta__pmk1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01787:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-1","expression":"Null"}]}]},"pck2delta":{"display_name":"pck2delta","display_uniquename":"pck2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00610:allele-1","expression":"Null"}]}]},"pmk1delta":{"display_name":"pmk1delta","display_uniquename":"pmk1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04551:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]}},"ltp_gene_count":4,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-07-02","pubmed_publication_date":"14 Jun 2021","terms_by_termid":{"FYECO:0000207":null,"FYECO:0000314":null,"FYPO:0000079":null,"FYPO:0001038":null,"FYPO:0001838":null,"FYPO:0002033":null,"FYPO:0002678":null,"FYPO:0002680":null,"FYPO:0004295":null,"FYPO:0005152":null,"FYPO:0007521":null,"FYPO:0007522":null,"FYPO:0007775":null,"FYPO:0007776":null,"FYPO:0007779":null,"FYPO:0007780":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"GO:0005634":null,"GO:0005737":null,"GO:0036460":null,"GO:0042149":null,"GO:0071475":null,"GO:0072690":null,"MOD:00696":null},"title":"Specific Functional Features of the Cell Integrity MAP Kinase Pathway in the Dimorphic Fission Yeast  Schizosaccharomyces japonicus .","uniquename":"PMID:34198697"}


id: PMID:36058798
data:
  {"abstract":"Schizosaccharomyces japonicus is a dimorphic yeast, transiting between unicellular and hyphal growth. The glycoproteins of fission yeast contain, in addition to mannose (Man), a large number of galactose (Gal) residues. Previously, we reported that the cell-surface O-glycans of S. japonicus comprise mainly tri-saccharides (Gal-Man-Man) as a main component, in contrast to the tetra-saccharides observed in other Schizosaccharomyces species. Here we have investigated the function of cell-surface Gal residues in S. japonicus. Because disruption of gms1 + , encoding the UDP-Gal transporter required for galactomannan synthesis, abolishes cell-surface galactosylation in Schizosaccharomyces pombe, we constructed a deletion mutant of the homologous gene in S. japonicus gms1Δ [gms1 (S.j)] and determined the N- and O-linked oligosaccharide structures present on the cell surface. Disruption of gms1 (S.j) resulted in a complete lack of Gal on the cell surface, indicating that Gms1 plays an essential role in supplying UDP-Gal from the cytoplasm to the Golgi lumen. Analytical microscopy of gms1Δ demonstrated that the lack of cell-surface Gal did not affect cell growth or morphology during vegetative growth. However, hyphal development was blocked in gms1Δ, even in the presence of the topoisomerase I inhibitor camptothecin, which is known to induce hyphal differentiation in wild-type S. japonicus. Collectively, these findings show that Gal-containing oligosaccharides are required for cell wall integrity during filamentous growth in S. japonicus.","alleles_by_uniquename":{"SJAG_04697:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04697","name":"gms1delta","uniquename":"SJAG_04697:allele-1"}},"annotation_curators":[{"annotation_count":6,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-12-01","authors":"Fukunaga T, Ohashi T, Tanaka Y, Yoshimatsu T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Fukunaga T et al.","canto_added_date":"2022-11-25 12:12:27","canto_annotation_status":"APPROVED","canto_approved_date":"2022-12-01 10:35:53","canto_approver_orcid":"0000-0002-8138-6851","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2022-12-01 10:35:53","canto_session_key":"465355706dc223a3","canto_session_submitted_date":"2022-11-25 12:49:07","canto_triage_status":"Curatable","citation":"J Biosci Bioeng 2022 Nov;134(5):384-392","cv_annotations":{"single_locus_phenotype":[{"annotations":[115547],"is_not":false,"summary":null,"term":"FYPO:0008029"},{"annotations":[115543],"is_not":false,"summary":null,"term":"FYPO:0000082"},{"annotations":[115546],"is_not":false,"summary":null,"term":"FYPO:0007776"},{"annotations":[115545],"is_not":false,"summary":null,"term":"FYPO:0007780"},{"annotations":[115542],"is_not":false,"summary":null,"term":"FYPO:0003727"},{"annotations":[115544],"is_not":false,"summary":null,"term":"FYPO:0000106"}]},"doi":"10.1016/j.jbiosc.2022.07.014","gene_count":1,"genes_by_uniquename":{"SJAG_04697":null},"genotypes_by_uniquename":{"gms1delta":{"display_name":"gms1delta","display_uniquename":"gms1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04697:allele-1","expression":"Null"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-09-04","pubmed_publication_date":"Nov 2022","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000005":null,"FYECO:0000126":null,"FYECO:0000137":null,"FYECO:0000314":null,"FYPO:0000082":null,"FYPO:0000106":null,"FYPO:0003727":null,"FYPO:0007776":null,"FYPO:0007780":null,"FYPO:0008029":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null},"title":"Galactosylation of cell-surface glycoprotein required for hyphal growth and cell wall integrity in Schizosaccharomyces japonicus.","uniquename":"PMID:36058798"}


id: PMID:2021084
data:
  {"abstract":"The genus Schizosaccharomyces comprises a small, somewhat heterogeneous group of yeast species which have in common a unique mode of vegetative reproduction by cross-wall formation without constriction as well as a certain degree of osmophilia, most strains having been isolated from habitats of high sugar concentration. This study evaluated inter- and intraspecific relationships utilizing nDNA/nDNA optical reassociation and by the analysis of physiological profiles of several strains of each species. Results demonstrate that the genus should be divided into three species: Schiz. japonicus, Schiz. octosporus and Schiz. pombe.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Vaughan Martini A","authors_abbrev":"Vaughan Martini A","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Yeast 1991 Jan;7(1):73-8","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1991","pubmed_entrez_date":"1991-01-01","pubmed_publication_date":"Jan 1991","terms_by_termid":{},"title":"Evaluation of phylogenetic relationships among fission yeast by nDNA/nDNA reassociation and conventional taxonomic criteria.","uniquename":"PMID:2021084"}


id: PMID:7612397
data:
  {"abstract":"The ultrastructure of isolated cell walls of Schizosaccharomyces pombe was studied by electron microscopy after treatment with the following purified enzymes: endo-beta-(1-->3)-glucanase, endo-beta-(-->6)-glucanase, and endo-alpha-(1-->3)-glucanase produced by Bacillus circulans; exo-beta-(1-->3)-glucanase and endo-beta-(1-->3)-glucanase produced by Schizosaccharomyces japonicus var. versatilis. The exo-beta-(1-->3)-glucanase had no detectable effect on the walls, but amorphous wall material was removed by action of the endo-beta-(1-->3)- and endo-beta-(1-->6)-glucanases of B. circulans to reveal a wall component consisting of densely interwoven microfibrils. The fibrils were hydrolyzed by treatment with the Schiz. japonicus endo-beta-(1-->3)-glucanase followed by B. circulans endo-alpha-(1-->3)-glucanase--suggesting that they were composed of -beta-(1-->3)-linked glucan and alpha-(1-->3)-linked glucan. The presence of a fibrillar component in untreated walls was evident after negative staining.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Kopecká M, Fleet GH, Phaff HJ","authors_abbrev":"Kopecká M et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Struct Biol 1995 Mar;114(2):140-52","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1995","pubmed_entrez_date":"1995-03-01","pubmed_publication_date":"Mar 1995","terms_by_termid":{},"title":"Ultrastructure of the cell wall of Schizosaccharomyces pombe following treatment with various glucanases.","uniquename":"PMID:7612397"}


id: PMID:33947067
data:
  {"abstract":"The fission yeast  Schizosaccharomyces japonicus , comprising  S. japonicus  var.  japonicus  and  S. japonicus  var.  versatilis  varieties, has unique characteristics such as striking hyphal growth not seen in other  Schizosaccharomyces  species; however, information on its diversity and evolution, in particular mating and sporulation, remains limited. Here we compared the growth and mating phenotypes of 17 wild strains of  S. japonicus , including eight  S. japonicus  var.  japonicus  strains newly isolated from an insect ( Drosophila ). Unlike existing wild strains isolated from fruits/plants, the strains isolated from  Drosophila  sporulated at high frequency even under nitrogen-abundant conditions. In addition, one of the strains from  Drosophila  was stained by iodine vapor, although the type strain of  S. japonicus  var.  japonicus  is not stained. Sequence analysis further showed that the nucleotide and amino acid sequences of pheromone-related genes have diversified among the eight strains from  Drosophila , suggesting crossing between  S. japonicus  cells of different genetic backgrounds occurs frequently in this insect. Much of yeast ecology remains unclear, but our findings suggest that insects such as  Drosophila  might be a good niche for mating and sporulation, and will provide a basis for the understanding of sporulation mechanisms via signal transduction, as well as the ecology and evolution of yeast.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Seike T, Sakata N, Matsuda F, Furusawa C","authors_abbrev":"Seike T et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Fungi (Basel) 2021 Apr 29;7(5)","cv_annotations":{},"doi":"10.3390/jof7050350","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-05-05","pubmed_publication_date":"29 Apr 2021","terms_by_termid":{},"title":"Elevated Sporulation Efficiency in Fission Yeast  Schizosaccharomyces japonicus  Strains Isolated from  Drosophila .","uniquename":"PMID:33947067"}


id: PMID:25942548
data:
  {"abstract":"New work shows the anillin-related protein Mid1 does not position the cytokinetic ring in the fission yeast Schizosaccharomyces japonicus, unlike its role in S. pombe. Further analysis suggests the conserved function of Mid1-like anillin proteins may be in scaffolding, not positioning, the cytokinetic ring. ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Moseley JB","authors_abbrev":"Moseley JB","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Curr Biol 2015 May 04;25(9):R364-6","cv_annotations":{},"doi":"10.1016/j.cub.2015.03.017","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-05-06","pubmed_publication_date":"04 May 2015","terms_by_termid":{},"title":"Cytokinesis: does Mid1 have an identity crisis?","uniquename":"PMID:25942548"}


id: GO_REF:0000059
data:
  {"abstract":"We have created a standard template for the definition of classes for the regulation of a molecular function. This includes the definitions for positive and negative regulation. The equivalence axiom templates are \"GO:0065007 and 'regulates' some X\" (regulation), \"GO:0065007 and 'negatively_regulates' some X\" (negative regulation), and \"GO:0065007 and 'positively_regulates' some X\" (positive regulation), where X is a molecular function.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of regulation in the Gene Ontology (molecular function) ","uniquename":"GO_REF:0000059"}


id: GO_REF:0000003
data:
  {"abstract":"Transitive assignment using Enzyme Commission identifiers. This method is used for any database entry, such as a protein record in UniProtKB or TrEMBL, that has had an Enzyme Commission number assigned. The corresponding GO term is determined using the EC cross-references in the GO molecular function ontology. Also see Hill et al., Genomics (2001) 74:121-128. The mapping file is available at http://www.geneontology.org/external2go/ec2go.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GOA curators, MGI curators","canto_curator_role":"JaponicusDB","cv_annotations":{"molecular_function":[{"annotations":[68434],"is_not":false,"summary":null,"term":"GO:0003925"},{"annotations":[68825],"is_not":false,"summary":null,"term":"GO:0044024"},{"annotations":[59027],"is_not":false,"summary":null,"term":"GO:0043864"},{"annotations":[65189],"is_not":false,"summary":null,"term":"GO:0052832"},{"annotations":[65190],"is_not":false,"summary":null,"term":"GO:0052833"},{"annotations":[67997],"is_not":false,"summary":null,"term":"GO:1990817"}]},"gene_count":5,"genes_by_uniquename":{"SJAG_01885":null,"SJAG_02383":null,"SJAG_02721":null,"SJAG_03739":null,"SJAG_04509":null},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{"GO:0003925":null,"GO:0043864":null,"GO:0044024":null,"GO:0052832":null,"GO:0052833":null,"GO:1990817":null},"title":"Gene Ontology annotation based on Enzyme Commission mapping","uniquename":"GO_REF:0000003"}


id: PMID:17870620
data:
  {"abstract":"In this work, we identify a family of putative adhesins in the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. The members of this family share a conserved tandem repeat related to those found in the Candida albicans Als family of adhesins. Unlike previously characterised adhesins that possess conserved ligand-binding domains at the N-terminus, this group of proteins carry ligand-binding domains at their C-termini. We demonstrate that one such domain--the uncharacterised GLEYA domain, is related to the lectin-like ligand-binding domain found in the Saccharomyces cerevisiae Flo proteins. Unlike the Flo and Als proteins, the fission yeast adhesins do not contain detectable glycosyl phosphatidyl inositol (GPI) membrane anchor signals to mediate their attachment to the cell wall, which may suggest a novel cell wall attachment mechanism. Further sequence analysis identified several putative adhesins in the sub-phylum of Pezizomycotina, where only a few adhesins have been described to date.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Linder T, Gustafsson CM","authors_abbrev":"Linder T et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Fungal Genet Biol 2008 Apr;45(4):485-97","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2008","pubmed_entrez_date":"2007-09-18","pubmed_publication_date":"Apr 2008","terms_by_termid":{},"title":"Molecular phylogenetics of ascomycotal adhesins--a novel family of putative cell-surface adhesive proteins in fission yeasts.","uniquename":"PMID:17870620"}


id: PMID:23786411
data:
  {"abstract":"Three types of mitosis, which are open, closed or semi-open mitosis, function in eukaryotic cells, respectively. The open mitosis involves breakage of the nuclear envelope before nuclear division, whereas the closed mitosis proceeds with an intact nuclear envelope. To understand the mechanism and significance of three types of mitotic division in eukaryotes, we investigated the process of semi-open mitosis, in which the nuclear envelope is only partially broken, in the fission yeast Schizosaccharomyces japonicus. In anaphase-promoting complex/cyclosome (APC/C) mutants of Sz. japonicus, the nuclear envelope remained relatively intact during anaphase, resulting in impaired semi-open mitosis. As a suppressor of apc2 mutant, a mutation of Oar2, which was a 3-oxoacyl-[acyl carrier protein] reductase, was obtained. The level of the Oar2, which had two destruction-box motifs recognized by APC/C, was increased in APC/C mutants. Furthermore, the defective semi-open mitosis observed in an apc2 mutant was restored by mutated oar2+. Based on these findings, we propose that APC/C regulates the dynamics of the nuclear envelope through degradation of Oar2 dependent on APC/C during the metaphase-to-anaphase transition of semi-open mitosis in Sz. japonicus.","alleles_by_uniquename":{"SJAG_01946:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01946","name":"cem1delta","uniquename":"SJAG_01946:allele-1"},"SJAG_01956:allele-1":{"allele_type":"amino_acid_mutation","description":"E405K ts","gene_uniquename":"SJAG_01956","name":"nuc2-1051","uniquename":"SJAG_01956:allele-1"},"SJAG_03198:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03198","name":"oar2delta","uniquename":"SJAG_03198:allele-1"},"SJAG_03198:allele-2":{"allele_type":"amino_acid_mutation","description":"Y189D cold sensitive","gene_uniquename":"SJAG_03198","name":"oar2-51","uniquename":"SJAG_03198:allele-2"},"SJAG_03198:allele-3":{"allele_type":"amino_acid_mutation","description":"R72A,L75A,R106A,L109A","gene_uniquename":"SJAG_03198","name":"oar2-dm12","synonyms":[{"name":"destruction box mutations","reference":"PMID:23786411","type":"exact"}],"uniquename":"SJAG_03198:allele-3"},"SJAG_03351:allele-1":{"allele_type":"amino_acid_mutation","description":"A186T ts","gene_uniquename":"SJAG_03351","name":"cut23-415","uniquename":"SJAG_03351:allele-1"},"SJAG_03575:allele-1":{"allele_type":"amino_acid_mutation","description":"E548K ts","gene_uniquename":"SJAG_03575","name":"apc2-361","uniquename":"SJAG_03575:allele-1"}},"annotation_curators":[{"annotation_count":22,"community_curator":true,"file_name":null,"file_type":null,"name":"Sho Okamoto","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-11-21","authors":"Aoki K, Shiwa Y, Takada H, Yoshikawa H, Niki H","authors_abbrev":"Aoki K et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2022-11-21 18:57:14","canto_approver_orcid":"0000-0002-8138-6851","canto_curator_name":"Sho Okamoto","canto_curator_role":"community","canto_first_approved_date":"2022-11-21 18:57:14","canto_session_key":"a0c3e1394f326db9","canto_session_submitted_date":"2022-11-21 18:57:00","canto_triage_status":"Curatable","citation":"Genes Cells 2013 Sep;18(9):733-52","cv_annotations":{"cellular_component":[{"annotations":[115355],"is_not":false,"summary":null,"term":"GO:0005730"}],"multi_locus_phenotype":[{"annotations":[115369,115370,115371,115373],"is_not":false,"summary":null,"term":"FYPO:0000674"}],"single_locus_phenotype":[{"annotations":[115356,115357,115358,115372],"is_not":false,"summary":null,"term":"FYPO:0000080"},{"annotations":[115365,115366,115367],"is_not":false,"summary":null,"term":"FYPO:0000618"},{"annotations":[115374,115375,115376],"is_not":false,"summary":null,"term":"FYPO:0001327"},{"annotations":[115362,115363,115364],"is_not":false,"summary":null,"term":"FYPO:0001387"},{"annotations":[115359,115360,115361],"is_not":false,"summary":null,"term":"FYPO:0000324"},{"annotations":[115368],"is_not":false,"summary":null,"term":"FYPO:0004683"}]},"doi":"10.1111/gtc.12072","gene_count":6,"genes_by_uniquename":{"SJAG_00259":null,"SJAG_01946":null,"SJAG_01956":null,"SJAG_03198":null,"SJAG_03351":null,"SJAG_03575":null},"genotypes_by_uniquename":{"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"apc2-361(E548K ts)","display_uniquename":"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03575:allele-1","expression":"Not assayed or wild type"}]}]},"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type__cem1delta":{"display_name":"apc2-361(E548K ts) cem1delta","display_uniquename":"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type__cem1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03575:allele-1","expression":"Not assayed or wild type"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_01946:allele-1","expression":"Null"}]}]},"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type__oar2-51-Y189D_cold_sensitive-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"apc2-361(E548K ts) oar2-51(Y189D cold sensitive)","display_uniquename":"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type__oar2-51-Y189D_cold_sensitive-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03575:allele-1","expression":"Not assayed or wild type"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03198:allele-2","expression":"Not assayed or wild type"}]}]},"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type__oar2-dm12-R72A,L75A,R106A,L109A-amino_acid_mutation-expression-overexpression":{"display_name":"apc2-361(E548K ts) oar2-dm12(R72A,L75A,R106A,L109A aa)[Overexpression]","display_uniquename":"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type__oar2-dm12-R72A,L75A,R106A,L109A-amino_acid_mutation-expression-overexpression","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03575:allele-1","expression":"Not assayed or wild type"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03198:allele-3","expression":"Overexpression"}]}]},"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type__oar2delta":{"display_name":"apc2-361(E548K ts) oar2delta","display_uniquename":"apc2-361-E548K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type__oar2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03575:allele-1","expression":"Not assayed or wild type"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03198:allele-1","expression":"Null"}]}]},"cem1delta":{"display_name":"cem1delta","display_uniquename":"cem1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01946:allele-1","expression":"Null"}]}]},"cut23-415-A186T_ts-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"cut23-415(A186T ts)","display_uniquename":"cut23-415-A186T_ts-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03351:allele-1","expression":"Not assayed or wild type"}]}]},"nuc2-1051-E405K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"nuc2-1051(E405K ts)","display_uniquename":"nuc2-1051-E405K_ts-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01956:allele-1","expression":"Not assayed or wild type"}]}]},"oar2-51-Y189D_cold_sensitive-amino_acid_mutation-expression-overexpression":{"display_name":"oar2-51(Y189D cold sensitive)[Overexpression]","display_uniquename":"oar2-51-Y189D_cold_sensitive-amino_acid_mutation-expression-overexpression","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03198:allele-2","expression":"Overexpression"}]}]},"oar2-dm12-R72A,L75A,R106A,L109A-amino_acid_mutation-expression-overexpression":{"display_name":"oar2-dm12(R72A,L75A,R106A,L109A aa)[Overexpression]","display_uniquename":"oar2-dm12-R72A,L75A,R106A,L109A-amino_acid_mutation-expression-overexpression","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03198:allele-3","expression":"Overexpression"}]}]},"oar2delta":{"display_name":"oar2delta","display_uniquename":"oar2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03198:allele-1","expression":"Null"}]}]}},"ltp_gene_count":6,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2013","pubmed_entrez_date":"2013-06-22","pubmed_publication_date":"Sep 2013","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000006":null,"FYECO:0000137":null,"FYPO:0000080":null,"FYPO:0000324":null,"FYPO:0000618":null,"FYPO:0000674":null,"FYPO:0001327":null,"FYPO:0001387":null,"FYPO:0004683":null,"FYPO_EXT:0000001":null,"GO:0005730":null},"title":"Regulation of nuclear envelope dynamics via APC/C is necessary for the progression of semi-open mitosis in Schizosaccharomyces japonicus.","uniquename":"PMID:23786411"}


id: PMID:27059155
data:
  {"abstract":"In the fission yeast Schizosaccharomyces pombe (Sp), Mid1/Dmf1 plays an important role in positioning the division site by inducing formation of the contractile ring (CR). Mid1, emanating from the nucleus located in the cell center, forms a dozen of nodes in the middle cell cortex ahead of mitosis, and actin filaments and myosin II accumulated at each node interact and assemble the CR in metaphase. Curiously, in another fission yeast S. japonicus (Sj), CR formation begins after nuclear segregation in late anaphase. Here, we investigated the role of S. japonicus Mid1 during mitosis to compare the molecular mechanisms that determine the cell division site in Schizosaccharomyces. Similar to Sp Mid1, Sj Mid1 often accumulated in the nucleus of interphase cells. Moreover, Sj Mid1 localized to cortical dots with myosin II in the future division site and formed a medial ring in mitotic cells. However, S. japonicus cells without Mid1 function still carried out symmetrical binary division. Therefore, the Mid1 dependency for positional control of the cell division site is possibly different between the two species. Meanwhile, we found that Sj Mid1 enhanced CR formation, in a manner possibly similar to that by Sp Mid1. ","alleles_by_uniquename":{"SJAG_01143:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01143","name":"mid1delta","uniquename":"SJAG_01143:allele-1"}},"annotation_curators":[{"annotation_count":3,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"},{"annotation_count":1,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-28","authors":"Yasuda T, Takaine M, Numata O, Nakano K","authors_abbrev":"Yasuda T et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-01 07:07:40","canto_approver_orcid":"0000-0001-6330-7526","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-28 11:44:06","canto_session_key":"f86427f99db0ccf7","canto_session_submitted_date":"2021-07-28 11:44:00","canto_triage_status":"Curatable","citation":"Genes Cells 2016 Jun;21(6):594-607","cv_annotations":{"biological_process":[{"annotations":[115144],"is_not":false,"summary":null,"term":"GO:1903475"}],"cellular_component":[{"annotations":[115141],"is_not":false,"summary":null,"term":"GO:0005826"},{"annotations":[115142],"is_not":false,"summary":null,"term":"GO:1990753"}],"single_locus_phenotype":[{"annotations":[115143],"is_not":false,"summary":null,"term":"FYPO:0000729"}]},"doi":"10.1111/gtc.12368","gene_count":1,"genes_by_uniquename":{"SJAG_01143":null},"genotypes_by_uniquename":{"mid1delta":{"display_name":"mid1delta","display_uniquename":"mid1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01143:allele-1","expression":"Null"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2016","pubmed_entrez_date":"2016-04-10","pubmed_publication_date":"Jun 2016","terms_by_termid":{"FYPO:0000729":null,"GO:0005826":null,"GO:0051329":null,"GO:1903475":null,"GO:1990753":null},"title":"Anillin-related protein Mid1 regulates timely formation of the contractile ring in the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:27059155"}


id: GO_REF:0000110
data:
  {"abstract":"Gene Ontology annotation of Drosophila melanogaster nuclear genes encoding proteins targeted to the mitochondrion based on analysis by MitoDrome (http://mitodrome.ba.itb.cnr.it/) by comparison of human mitochondrial proteins available in SWISSPROT vs. the Drosophila genome, ESTs and cDNA sequences available in the FlyBase database (PMID:12520013).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"FlyBase","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Gene Ontology annotation of Drosophila melanogaster nuclear genes encoding proteins targeted to the mitochondrion.","uniquename":"GO_REF:0000110"}


id: PMID:31380845
data:
  {"abstract":"Lipid metabolism and its regulation are of interest to both basic and applied life sciences and biotechnology. In this regard, various yeast species are used as models in lipid metabolic research or for industrial lipid production. Lipid droplets are highly dynamic storage bodies and their cellular content represents a convenient readout of the lipid metabolic state. Fluorescence microscopy is a method of choice for quantitative analysis of cellular lipid droplets, as it relies on widely available equipment and allows analysis of individual lipid droplets. Furthermore, microscopic image analysis can be automated, greatly increasing overall analysis throughput. Here, we describe an experimental and analytical workflow for automated detection and quantitative description of individual lipid droplets in three different model yeast species: the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus, and the budding yeast Saccharomyces cerevisiae. Lipid droplets are visualized with BODIPY 493/503, and cell-impermeable fluorescent dextran is added to the culture media to help identify cell boundaries. Cells are subjected to 3D epifluorescence microscopy in green and blue channels and the resulting z-stack images are processed automatically by a MATLAB pipeline. The procedure outputs rich quantitative data on cellular lipid droplet content and individual lipid droplet characteristics in a tabular format suitable for downstream analyses in major spreadsheet or statistical packages. We provide example analyses of lipid droplet content under various conditions that affect cellular lipid metabolism.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Princová J, Schätz M, Ťupa O, Převorovský M","authors_abbrev":"Princová J et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"J Vis Exp 2019 07 17;(149)","cv_annotations":{},"doi":"10.3791/59889","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2019","pubmed_entrez_date":"2019-08-06","pubmed_publication_date":"17 07 2019","terms_by_termid":{},"title":"Analysis of Lipid Droplet Content in Fission and Budding Yeasts using Automated Image Processing.","uniquename":"PMID:31380845"}


id: PMID:32243490
data:
  {"abstract":"The nuclear envelope (NE) undergoes dynamic remodeling to maintain NE integrity, a process involving the inner nuclear membrane protein LEM2 recruiting CHMP7/Cmp7 and then ESCRT-III. However, prior work has hinted at CHMP7/ESCRT-independent mechanisms. To identify such mechanisms, we studied NE assembly in Schizosaccharomyces japonicus, a fission yeast that undergoes partial mitotic NE breakdown and reassembly. S. japonicus cells lacking Cmp7 have compromised NE sealing after mitosis but are viable. A genetic screen identified mutations that promote NE integrity in cmp7Δ cells. Unexpectedly, loss of Lem2 or its interacting partner Nur1 suppressed cmp7Δ defects. In the absence of Cmp7, Lem2 formed aggregates that appear to interfere with ESCRT-independent NE sealing. A gain-of-function mutation implicated a membrane and ESCRT-III regulator, Alx1, in this alternate pathway. Additional results suggest a potentially general role for unsaturated fatty acids in NE integrity. These findings establish the existence of mechanisms for NE sealing independent of the canonical ESCRT pathway.","alleles_by_uniquename":{"SJAG_01242:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01242","name":"vps32delta","uniquename":"SJAG_01242:allele-1"},"SJAG_01745:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01745","name":"lem2delta","uniquename":"SJAG_01745:allele-1"},"SJAG_03891:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03891","name":"alx1delta","uniquename":"SJAG_03891:allele-1"},"SJAG_05207:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_05207","name":"cmp7delta","uniquename":"SJAG_05207:allele-1"}},"annotation_curators":[{"annotation_count":21,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"},{"annotation_count":4,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-09","authors":"Lee IJ, Stokasimov E, Dempsey N, Varberg JM, Jacob E, Jaspersen SL, Pellman D","authors_abbrev":"Lee IJ et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-07-14 11:10:55","canto_approver_orcid":"0000-0001-6330-7526","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-09 15:55:25","canto_session_key":"e134ba05c345c3f5","canto_session_submitted_date":"2021-07-09 15:55:19","canto_triage_status":"Curatable","citation":"J Cell Biol 2020 06 01;219(6)","cv_annotations":{"biological_process":[{"annotations":[115308,115309,115310,115311],"is_not":false,"summary":null,"term":"GO:0007084"}],"cellular_component":[{"annotations":[115307],"is_not":false,"summary":null,"term":"GO:0005783"},{"annotations":[115293,115295,115305],"is_not":false,"summary":null,"term":"GO:0044732"},{"annotations":[115294,115296,115304],"is_not":false,"summary":null,"term":"GO:0005635"}],"single_locus_phenotype":[{"annotations":[115297],"is_not":false,"summary":null,"term":"FYPO:0001375"},{"annotations":[115302],"is_not":false,"summary":null,"term":"FYPO:0000080"},{"annotations":[115298,115299,115306],"is_not":false,"summary":null,"term":"FYPO:0007772"},{"annotations":[115303],"is_not":false,"summary":null,"term":"FYPO:0000714"},{"annotations":[115300,115301],"is_not":false,"summary":null,"term":"FYPO:0001234"}]},"doi":"10.1083/jcb.201908232","gene_count":6,"genes_by_uniquename":{"SJAG_01050":null,"SJAG_01242":null,"SJAG_01745":null,"SJAG_03891":null,"SJAG_03943":null,"SJAG_05207":null},"genetic_interactions":[[{"gene_a_uniquename":"SJAG_01242","gene_b_uniquename":"SJAG_03891","interaction_type":"Phenotypic Enhancement"},[{"reference_uniquename":"PMID:32243490","throughput":"low"}]],[{"gene_a_uniquename":"SJAG_01242","gene_b_uniquename":"SJAG_01050","interaction_type":"Phenotypic Suppression"},[{"reference_uniquename":"PMID:32243490","throughput":"low"}]],[{"gene_a_uniquename":"SJAG_01242","gene_b_uniquename":"SJAG_01745","interaction_type":"Phenotypic Suppression"},[{"reference_uniquename":"PMID:32243490","throughput":"low"}]],[{"gene_a_uniquename":"SJAG_05207","gene_b_uniquename":"SJAG_03943","interaction_type":"Dosage Rescue"},[{"reference_uniquename":"PMID:32243490","throughput":"low"}]],[{"gene_a_uniquename":"SJAG_01745","gene_b_uniquename":"SJAG_01050","interaction_type":"Phenotypic Suppression"},[{"reference_uniquename":"PMID:32243490","throughput":"low"}]],[{"gene_a_uniquename":"SJAG_05207","gene_b_uniquename":"SJAG_01745","interaction_type":"Phenotypic Suppression"},[{"reference_uniquename":"PMID:32243490","throughput":"low"}]]],"genotypes_by_uniquename":{"alx1delta":{"display_name":"alx1delta","display_uniquename":"alx1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03891:allele-1","expression":"Null"}]}]},"cmp7delta":{"display_name":"cmp7delta","display_uniquename":"cmp7delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_05207:allele-1","expression":"Null"}]}]},"lem2delta":{"display_name":"lem2delta","display_uniquename":"lem2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01745:allele-1","expression":"Null"}]}]},"vps32delta":{"display_name":"vps32delta","display_uniquename":"vps32delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01242:allele-1","expression":"Null"}]}]}},"ltp_gene_count":6,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2020","pubmed_entrez_date":"2020-04-04","pubmed_publication_date":"01 06 2020","terms_by_termid":{"FYECO:0000006":null,"FYPO:0000080":null,"FYPO:0000714":null,"FYPO:0001234":null,"FYPO:0001375":null,"FYPO:0007772":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000003":null,"GO:0005635":null,"GO:0005783":null,"GO:0007084":null,"GO:0044732":null},"title":"Factors promoting nuclear envelope assembly independent of the canonical ESCRT pathway.","uniquename":"PMID:32243490"}


id: PMID:21802294
data:
  {"abstract":"Eukaryotes segregate chromosomes in \"open\" or \"closed\" mitosis, depending on whether their nuclear envelopes (NEs) break down or remain intact. Here we show that the control of the nuclear surface area may determine the choice between these two modes. The dividing nucleus does not expand its surface in the fission yeast Schizosaccharomyces japonicus, confining the mitotic spindle and causing it to buckle. The NE ruptures in anaphase, releasing the compressive stress and allowing chromosome segregation. Blocking the NE expansion in the related species Schizosaccharomyces pombe that undergoes closed mitosis induces spindle buckling and collapse in the absence of an intrinsic NE rupture mechanism. We propose that scaling considerations could have shaped the evolution of eukaryotic mitosis by necessitating either nuclear surface expansion or the NE breakdown.","alleles_by_uniquename":{"SJAG_01330:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01330","name":"mad2delta","uniquename":"SJAG_01330:allele-1"},"SJAG_01745:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01745","name":"lem2delta","uniquename":"SJAG_01745:allele-1"}},"annotation_curators":[{"annotation_count":16,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"},{"annotation_count":1,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-05","authors":"Yam C, He Y, Zhang D, Chiam KH, Oliferenko S","authors_abbrev":"Yam C et al.","canto_added_date":"2021-05-10 02:38:30","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-01 07:44:20","canto_approver_orcid":"0000-0001-6330-7526","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-05 11:58:24","canto_session_key":"ec486c9b0898d3c4","canto_session_submitted_date":"2021-07-05 12:18:55","canto_triage_status":"Curatable","citation":"Curr Biol 2011 Aug 09;21(15):1314-9","cv_annotations":{"biological_process":[{"annotations":[115286],"is_not":false,"summary":null,"term":"GO:0101024"}],"cellular_component":[{"annotations":[115275],"is_not":false,"summary":null,"term":"GO:0000785"},{"annotations":[115279,115280],"is_not":false,"summary":null,"term":"GO:0005783"},{"annotations":[115281],"is_not":false,"summary":null,"term":"GO:0098826"},{"annotations":[115274],"is_not":false,"summary":null,"term":"GO:0000776"},{"annotations":[115271],"is_not":false,"summary":null,"term":"GO:0005874"},{"annotations":[115276,115277,115278,115282],"is_not":false,"summary":null,"term":"GO:0005643"},{"annotations":[115272,115273],"is_not":false,"summary":null,"term":"GO:0005730"}],"single_locus_phenotype":[{"annotations":[115284],"is_not":false,"summary":null,"term":"FYPO:0003779"},{"annotations":[115283],"is_not":false,"summary":null,"term":"FYPO:0004318"},{"annotations":[115285],"is_not":false,"summary":null,"term":"FYPO:0007772"}]},"doi":"10.1016/j.cub.2011.06.052","gene_count":13,"genes_by_uniquename":{"SJAG_00175":null,"SJAG_00471":null,"SJAG_00684":null,"SJAG_00943":null,"SJAG_01006":null,"SJAG_01330":null,"SJAG_01374":null,"SJAG_01460":null,"SJAG_01745":null,"SJAG_02509":null,"SJAG_02830":null,"SJAG_03299":null,"SJAG_03603":null},"genotypes_by_uniquename":{"lem2delta":{"display_name":"lem2delta","display_uniquename":"lem2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01745:allele-1","expression":"Null"}]}]},"mad2delta":{"display_name":"mad2delta","display_uniquename":"mad2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01330:allele-1","expression":"Null"}]}]}},"ltp_gene_count":13,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2011","pubmed_entrez_date":"2011-08-02","pubmed_publication_date":"09 Aug 2011","terms_by_termid":{"FYECO:0000162":null,"FYPO:0003779":null,"FYPO:0004318":null,"FYPO:0007772":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"GO:0000776":null,"GO:0000785":null,"GO:0005643":null,"GO:0005730":null,"GO:0005783":null,"GO:0005874":null,"GO:0098826":null,"GO:0101024":null},"title":"Divergent strategies for controlling the nuclear membrane satisfy geometric constraints during nuclear division.","uniquename":"PMID:21802294"}


id: PMID:29173643
data:
  {"abstract":"In the beverage fermentation industry, especially at the craft or micro level, there is a movement to incorporate as many local ingredients as possible to both capture terroir and stimulate local economies. In the case of craft beer, this has traditionally only encompassed locally sourced barley, hops, and other agricultural adjuncts. The identification and use of novel yeasts in brewing lags behind. We sought to bridge this gap by bio-prospecting for wild yeasts, with a focus on the American Midwest. We isolated 284 different strains from 54 species of yeast and have begun to determine their fermentation characteristics. During this work, we found several isolates of five species that produce lactic acid and ethanol during wort fermentation: Hanseniaspora vineae, Lachancea fermentati, Lachancea thermotolerans, Schizosaccharomyces japonicus, and Wickerhamomyces anomalus. Tested representatives of these species yielded excellent attenuation, lactic acid production, and sensory characteristics, positioning them as viable alternatives to lactic acid bacteria (LAB) for the production of sour beers. Indeed, we suggest a new LAB-free paradigm for sour beer production that we term \"primary souring\" because the lactic acid production and resultant pH decrease occurs during primary fermentation, as opposed to kettle souring or souring via mixed culture fermentation.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Osburn K, Amaral J, Metcalf SR, Nickens DM, Rogers CM, Sausen C, Caputo R, Miller J, Li H, Tennessen JM, Bochman ML","authors_abbrev":"Osburn K et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Biotech","citation":"Food Microbiol 2018 Apr;70:76-84","cv_annotations":{},"doi":"10.1016/j.fm.2017.09.007","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2018","pubmed_entrez_date":"2017-11-28","pubmed_publication_date":"Apr 2018","terms_by_termid":{},"title":"Primary souring: A novel bacteria-free method for sour beer production.","uniquename":"PMID:29173643"}


id: PMID:25308606
data:
  {"abstract":"The non-pathogenic dimorphic fission yeast, Schizosaccharomyces japonicus, could be a suitable model organism for investigation of the genetic background of mycelial growth, as it has a haploid chromosome set and its genome is sequenced. Since earlier results have suggested that its morphological transition required solid substrates, but molecular biological experiments would require hyphae production in a liquid medium, we wanted to find circumstances which would enable hyphae production in liquid media. Several external conditions were investigated, but the strongest inducer was fetal bovine serum (FBS). Its positive effect could be hampered by heat and was dependent on pH, temperature and concentration of the serum. Other protein-containing compounds, such as peptone and bovine serum albumin or amino acids, proved to be ineffective or weak. Generally, the uninduced and induced mycelial growth of Sz. japonicus could be improved by lower external pH and higher temperature.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Papp L, Sipiczki M, Holb IJ, Miklós I","authors_abbrev":"Papp L et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Yeast 2014 Dec;31(12):475-82","cv_annotations":{},"doi":"10.1002/yea.3048","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2014","pubmed_entrez_date":"2014-10-14","pubmed_publication_date":"Dec 2014","terms_by_termid":{},"title":"Optimal conditions for mycelial growth of Schizosaccharomyces japonicus cells in liquid medium: it enables the molecular investigation of dimorphism.","uniquename":"PMID:25308606"}


id: PMID:33022982
data:
  {"abstract":"Nowadays commercial preparations of yeast polysaccharides (PSs), in particular mannoproteins, are widely used for wine colloidal and tartrate salt stabilization. In this context, the industry has developed different processes for the isolation and purification of PSs from the cell wall of  Saccharomyces cerevisiae . This yeast releases limited amounts of mannoproteins in the growth medium, thus making their direct isolation from the culture broth not economically feasible. On the contrary,  Schizosaccharomyces japonicus , a non- Saccharomyces  yeast isolated from wine, releases significant amounts of PSs during the alcoholic fermentation. In the present work, PSs released by  Sch. japonicus  were recovered from the growth medium by ultrafiltration and their impact on the wine colloidal stability was evaluated. Interestingly, these PSs contribute positively to the wine protein stability. The visible haziness of the heat-treated wine decreases as the concentration of added PSs increases. SDS-PAGE Gel electrophoresis results of the haze and of the supernatant after the heat stability test are consistent with the turbidity measurements. Moreover, particle size distributions of the heat-treated wines, as obtained by Dynamic Light Scattering (DLS), show a reduction in the average dimension of the protein aggregates as the concentration of added PSs increases.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Millarini V, Ignesti S, Cappelli S, Ferraro G, Adessi A, Zanoni B, Fratini E, Domizio P","authors_abbrev":"Millarini V et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Biotech","citation":"Foods 2020 Oct 03;9(10)","cv_annotations":{},"doi":"10.3390/foods9101407","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2020","pubmed_entrez_date":"2020-10-07","pubmed_publication_date":"03 Oct 2020","terms_by_termid":{},"title":"Protection of Wine from Protein Haze Using  Schizosaccharomyces japonicus  Polysaccharides.","uniquename":"PMID:33022982"}


id: PMID:37088673
data:
  {"abstract":"Making wine via spontaneous fermentation without sulfur dioxide and commercial yeast (spontaneous winemaking) is increasing in recent year, but there is scant research regarding microbial communities present in Japan during spontaneous winemaking using culture-independent molecular methods. We analyzed fungal communities and populations during laboratory-scale spontaneous winemaking using sterilized labware to avoid winery-resident microbes. In the spontaneous fermentation of four grape varieties (Pinot Noir, Riesling, Koshu, and Koshusanjaku) grown in the same Japanese vineyard, our analysis of yeast and other fungal species by next-generation sequencing based on the ITS1 region demonstrated that Saccharomyces cerevisiae was eventually dominant in seven of 12 fermentation batches (three replications for each grape variety), whereas non-Saccharomyces species (e.g., Schizosaccharomyces japonicus, Lachancea dasiensis, and Hanseniaspora valbyensis) became dominant in four batches at the end of fermentation. In another batch, lactic acid bacteria (LAB) became dominant and the fermentation remained incomplete. Diverse microbes were involved in the spontaneous fermentation (particularly in Koshusanjaku), indicating that residual sugar remained and lactic and acetic acid largely increased. Compared to the control wine made with SO 2  and commercial yeast, the concentration of lactic acid was 47-fold higher in the must dominated by L. dasiensis, and the concentrations of acetic acid and lactic acid were 10-fold and 20-fold higher in the must dominated by LAB, respectively. Even when indigenous S. cerevisiae became dominant, the finished wines obtained high sensory-analysis scores for complexity but low scores for varietal typicality, indicating the risk of fermentation with unselected wild yeast on the grapes grown in Japan.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Shimizu H, Kamada A, Koyama K, Iwashita K, Goto-Yamamoto N","authors_abbrev":"Shimizu H et al.","canto_added_date":"2023-05-04 00:40:03","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Biosci Bioeng 2023 Apr 21;","cv_annotations":{},"doi":"10.1016/j.jbiosc.2023.03.013","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-04-23","pubmed_publication_date":"21 Apr 2023","terms_by_termid":{},"title":"Yeast diversity during the spontaneous fermentation of wine with only the microbiota on grapes cultivated in Japan.","uniquename":"PMID:37088673"}


id: PMID:25866389
data:
  {"abstract":"Strategies to position the division apparatus exhibit a bewildering diversity [1], but how these mechanisms evolve remains virtually unknown. Here, we explore the plasticity of division site positioning in fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. We demonstrate that, whereas both species divide in the middle, only S. pombe uses the anillin Mid1 as a primary nucleus-derived cue to assemble the actomyosin ring at the equatorial cortex. We trace this variance to the divergence in subcellular targeting of Mid1 and show that duplication of an ancestral anillin early in the Schizosaccharomyces lineage may have led to subfunctionalization of the Mid1 orthologs. In contrast to S. pombe, medial assembly of the actomyosin ring in mitotic S. japonicus relies on the cortical anchor protein Cdc15 regulated by the tip-localized kinase Pom1. Our data suggest that division site placement is determined by cortical positioning of the actomyosin-plasma membrane linkers and that both identity of the linker and control of its subcellular targeting are highly modular.","alleles_by_uniquename":{"SJAG_00118:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00118","name":"mid2delta","uniquename":"SJAG_00118:allele-1"},"SJAG_01143:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01143","name":"mid1delta","uniquename":"SJAG_01143:allele-1"},"SJAG_01143:allele-2":{"allele_type":"partial_amino_acid_deletion","description":"711-723","gene_uniquename":"SJAG_01143","name":"mid1-delta(711-723 a.a.)","uniquename":"SJAG_01143:allele-2"},"SJAG_02392:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02392","name":"pom1delta","uniquename":"SJAG_02392:allele-1"},"SJAG_03596:allele-1":{"allele_type":"amino_acid_mutation","description":"L264P,P442T","gene_uniquename":"SJAG_03596","name":"cdc15-A","uniquename":"SJAG_03596:allele-1"},"SJAG_04332:allele-1":{"allele_type":"amino_acid_mutation","description":"I30T,T572P","gene_uniquename":"SJAG_04332","name":"cdc25-D9","uniquename":"SJAG_04332:allele-1"}},"annotation_curators":[{"annotation_count":3,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"},{"annotation_count":34,"community_curator":true,"file_name":null,"file_type":null,"name":"Ying Gu","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-05-12","authors":"Gu Y, Yam C, Oliferenko S","authors_abbrev":"Gu Y et al.","canto_added_date":"2021-05-10 02:37:54","canto_annotation_status":"APPROVED","canto_approved_date":"2021-05-16 08:31:49","canto_approver_orcid":"0000-0001-6330-7526","canto_curator_name":"Ying Gu","canto_curator_role":"community","canto_first_approved_date":"2021-05-12 14:24:14","canto_session_key":"bc986e831d627df1","canto_session_submitted_date":"2021-05-14 13:43:22","canto_triage_status":"Curatable","citation":"Curr Biol 2015 May 04;25(9):1187-94","cv_annotations":{"biological_process":[{"annotations":[115337],"is_not":false,"summary":null,"term":"GO:1902408"},{"annotations":[115338],"is_not":false,"summary":null,"term":"GO:1903617"},{"annotations":[115336],"is_not":true,"summary":null,"term":"GO:1902408"}],"cellular_component":[{"annotations":[115344,115345],"is_not":false,"summary":null,"term":"GO:0051286"},{"annotations":[115340,115342,115347,115349],"is_not":false,"summary":null,"term":"GO:1990753"},{"annotations":[115341,115343,115346,115348,115350],"is_not":false,"summary":null,"term":"GO:0110085"}],"multi_locus_phenotype":[{"annotations":[115328],"is_not":false,"summary":null,"term":"FYPO:0000231"},{"annotations":[115332],"is_not":false,"summary":null,"term":"FYPO:0005503"},{"annotations":[115334],"is_not":false,"summary":null,"term":"FYPO:0007177"},{"annotations":[115333],"is_not":false,"summary":null,"term":"FYPO:0000729"},{"annotations":[115330],"is_not":false,"summary":null,"term":"FYPO:0003946"},{"annotations":[115329],"is_not":false,"summary":null,"term":"FYPO:0000118"}],"qualitative_gene_expression":[{"annotations":[115320,115339],"is_not":false,"summary":null,"term":"PomGeneEx:0000011"}],"single_locus_phenotype":[{"annotations":[115321],"is_not":false,"summary":null,"term":"FYPO:0000231"},{"annotations":[115352,115353],"is_not":false,"summary":null,"term":"FYPO:0000731"},{"annotations":[115326],"is_not":false,"summary":null,"term":"FYPO:0005503"},{"annotations":[115323,115324,115331,115335],"is_not":false,"summary":null,"term":"FYPO:0007177"},{"annotations":[115354],"is_not":false,"summary":null,"term":"FYPO:0002026"},{"annotations":[115351],"is_not":false,"summary":null,"term":"FYPO:0003535"},{"annotations":[115322],"is_not":false,"summary":null,"term":"FYPO:0000729"},{"annotations":[115325],"is_not":false,"summary":null,"term":"FYPO:0007701"},{"annotations":[115318,115319],"is_not":false,"summary":null,"term":"FYPO:0000118"},{"annotations":[115327],"is_not":false,"summary":null,"term":"FYPO:0000644"}]},"doi":"10.1016/j.cub.2015.02.056","gene_count":8,"genes_by_uniquename":{"SJAG_00118":null,"SJAG_01143":null,"SJAG_01665":null,"SJAG_02392":null,"SJAG_03596":null,"SJAG_03703":null,"SJAG_04332":null,"SJAG_04498":null},"genotypes_by_uniquename":{"cdc15-A-L264P,P442T-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"cdc15-A(L264P,P442T aa)","display_uniquename":"cdc15-A-L264P,P442T-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03596:allele-1","expression":"Not assayed or wild type"}]}]},"cdc15-A-L264P,P442T-amino_acid_mutation-expression-not_assayed_or_wild_type__mid1delta":{"display_name":"cdc15-A(L264P,P442T aa) mid1delta","display_uniquename":"cdc15-A-L264P,P442T-amino_acid_mutation-expression-not_assayed_or_wild_type__mid1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03596:allele-1","expression":"Not assayed or wild type"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_01143:allele-1","expression":"Null"}]}]},"cdc25-D9-I30T,T572P-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"cdc25-D9(I30T,T572P aa)","display_uniquename":"cdc25-D9-I30T,T572P-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04332:allele-1","expression":"Not assayed or wild type"}]}]},"mid1-delta(711-723_a.a.)-711-723-partial_amino_acid_deletion-expression-not_assayed_or_wild_type":{"display_name":"mid1-delta(711-723 a.a.)(aa)","display_uniquename":"mid1-delta(711-723_a.a.)-711-723-partial_amino_acid_deletion-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01143:allele-2","expression":"Not assayed or wild type"}]}]},"mid1delta":{"display_name":"mid1delta","display_uniquename":"mid1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01143:allele-1","expression":"Null"}]}]},"mid1delta__mid2delta":{"display_name":"mid1delta mid2delta","display_uniquename":"mid1delta__mid2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01143:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_00118:allele-1","expression":"Null"}]}]},"mid1delta__pom1delta":{"display_name":"mid1delta pom1delta","display_uniquename":"mid1delta__pom1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01143:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_02392:allele-1","expression":"Null"}]}]},"mid2delta":{"display_name":"mid2delta","display_uniquename":"mid2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00118:allele-1","expression":"Null"}]}]},"pom1delta":{"display_name":"pom1delta","display_uniquename":"pom1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02392:allele-1","expression":"Null"}]}]}},"ltp_gene_count":8,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-04-14","pubmed_publication_date":"04 May 2015","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000005":null,"FYECO:0000137":null,"FYECO:0000162":null,"FYPO:0000118":null,"FYPO:0000231":null,"FYPO:0000644":null,"FYPO:0000729":null,"FYPO:0000731":null,"FYPO:0002026":null,"FYPO:0003535":null,"FYPO:0003946":null,"FYPO:0005503":null,"FYPO:0007177":null,"FYPO:0007701":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"GO:0000085":null,"GO:0000087":null,"GO:0051286":null,"GO:0051325":null,"GO:0051329":null,"GO:0110085":null,"GO:1902408":null,"GO:1903617":null,"GO:1990753":null,"PomGeneEx:0000011":null},"title":"Rewiring of cellular division site selection in evolution of fission yeasts.","uniquename":"PMID:25866389"}


id: PMID:19330769
data:
  {"abstract":"The fission yeast Schizosaccharomyces japonicus var. japonicus belong to the genus Schizosaccharomyces, together with Schizosaccharomyces pombe, which has been well studied as a model organism. In contrast, Sz. japonicus is poorly characterized and genetic tools were yet to be developed. We here report the isolation of the heterothallic haploids NIG2017, NIG2025 and NIG2028, which were derivatives of a Sz. japonicus homothallic strain (NIG2008). Based on the genomic sequence of Sz. japonicus, released by the Broad Institute, we found that Sz. japonicus also possesses orthologues of the mating-type genes of Sz. pombe; two mat-M (-) and two mat-P (+) genes. As expected, heterothallic strains were defective in one of the Sz. japonicus mat genes (mat(sj)). We confirmed that NIG2017 and NIG2025 strains only expressed mRNA from the mat(sj)-P genes, while homothallic strains expressed both mat(sj)-M and mat(sj)-P. Although the NIG2028 strain expressed both gene products, mat(sj)-P was found mutated, which may have conferred the heterothallic phenotype of the mutant. Thus, we concluded that these were stable heterothallic strains. We designated NIG2017 and NIG2025 as h(+) and NIG 2028 as h(-), respectively. We also found additional h(-) strains (NIG5872 and NIG5873) that arose from the cross between NIG2017 and NIG2028 derivatives. In addition to that, we have constructed a ura4(sj)-deleted strain and an ade6(sj)-mutated strain. We used these heterothallic strains and the auxotroph strains to perform spore dissection analysis to determine the genetic distances between several loci, and found that the mating type loci and ade6(sj) locus were linked to centromeres.","alleles_by_uniquename":{"SJAG_01081:allele-1":{"allele_type":"nonsense_mutation","description":"S427>stop","gene_uniquename":"SJAG_01081","name":"ade6-domE","uniquename":"SJAG_01081:allele-1"},"SJAG_03164:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03164","name":"ura4delta","uniquename":"SJAG_03164:allele-1"}},"annotation_curators":[{"annotation_count":2,"community_curator":true,"file_name":null,"file_type":null,"name":"Sho Okamoto","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-11-23","authors":"Furuya K, Niki H","authors_abbrev":"Furuya K et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2022-11-23 13:08:27","canto_approver_orcid":"0000-0002-8138-6851","canto_curator_name":"Sho Okamoto","canto_curator_role":"community","canto_first_approved_date":"2022-11-23 13:08:26","canto_session_key":"386d294cfcac2a63","canto_session_submitted_date":"2022-11-23 13:07:46","canto_triage_status":"Curatable","citation":"Yeast 2009 Apr;26(4):221-33","cv_annotations":{"single_locus_phenotype":[{"annotations":[115377],"is_not":false,"summary":null,"term":"FYPO:0000747"},{"annotations":[115378],"is_not":false,"summary":null,"term":"FYPO:0001012"}]},"doi":"10.1002/yea.1662","gene_count":2,"genes_by_uniquename":{"SJAG_01081":null,"SJAG_03164":null},"genotypes_by_uniquename":{"ade6-domE-S427>stop-nonsense_mutation-expression-not_assayed_or_wild_type":{"display_name":"ade6-domE(S427>stop)","display_uniquename":"ade6-domE-S427>stop-nonsense_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01081:allele-1","expression":"Not assayed or wild type"}]}]},"ura4delta":{"display_name":"ura4delta","display_uniquename":"ura4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03164:allele-1","expression":"Null"}]}]}},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2009","pubmed_entrez_date":"2009-03-31","pubmed_publication_date":"Apr 2009","terms_by_termid":{"FYPO:0000747":null,"FYPO:0001012":null},"title":"Isolation of heterothallic haploid and auxotrophic mutants of Schizosaccharomyces japonicus.","uniquename":"PMID:19330769"}


id: GO_REF:0000087
data:
  {"abstract":"We have created a standard template for classes describing the protein localization and establishment of protein localization to a cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0008104 and 'has_target_end_location' some C\" (protein localization) and \"GO:0045184 and 'has_target_end_location' some C\" (establishment of protein localization), where C is cellular component.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of protein localization and establishment of protein localization as biological process in the Gene Ontology","uniquename":"GO_REF:0000087"}


id: PMID:37233261
data:
  {"abstract":"Gene targeting is a commonly used method to reveal the function of genes. Although it is an attractive tool for molecular studies, it can frequently be a challenge because its efficiency can be low and it requires the screening of a large number of transformants. Generally, these problems originate from the elevated level of ectopic integration caused by non-homologous DNA end joining (NHEJ). To eliminate this problem, NHEJ-related genes are frequently deleted or disrupted. Although these manipulations can improve gene targeting, the phenotype of the mutant strains raised the question of whether mutations have side effects. The aim of this study was to disrupt the  lig4  gene in the dimorphic fission yeast,  S. japonicus , and investigate the phenotypic changes of the mutant strain. The mutant cells have shown various phenotypic changes, such as increased sporulation on complete medium, decreased hyphal growth, faster chronological aging, and higher sensitivity to heat shock, UV light, and caffeine. In addition, higher flocculation capacity has been observed, especially at lower sugar concentrations. These changes were supported by transcriptional profiling. Many genes belonging to metabolic and transport processes, cell division, or signaling had altered mRNA levels compared to the control strain. Although the disruption improved the gene targeting, we assume that the  lig4  inactivation can cause unexpected physiological side effects, and we have to be very careful with the manipulations of the NHEJ-related genes. To reveal the exact mechanisms behind these changes, further investigations are required.","alleles_by_uniquename":{"SJAG_02527:allele-1":{"allele_type":"disruption","description":"RNA sequencing revealed that only the 5' end of the disrupted allele showed low RNA expression and coverage","gene_uniquename":"SJAG_02527","name":"lig4::KanMX6","uniquename":"SJAG_02527:allele-1"}},"annotation_curators":[{"annotation_count":7,"community_curator":true,"file_name":null,"file_type":null,"name":"Ida Miklos","orcid":"0000-0002-7074-4019"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2023-08-08","authors":"Acs-Szabo L, Papp LA, Takacs S, Miklos I","authors_abbrev":"Acs-Szabo L et al.","canto_added_date":"2023-05-27 00:40:04","canto_annotation_status":"APPROVED","canto_approved_date":"2023-08-08 20:07:33","canto_approver_orcid":"0000-0002-8138-6851","canto_curator_name":"Ida Miklos","canto_curator_role":"community","canto_first_approved_date":"2023-08-08 20:07:33","canto_session_key":"c74bdd0a67b132f8","canto_session_submitted_date":"2023-08-08 20:07:15","canto_triage_status":"Curatable","citation":"J Fungi (Basel) 2023 May 10;9(5)","cv_annotations":{"single_locus_phenotype":[{"annotations":[115549],"is_not":false,"summary":null,"term":"FYPO:0007776"},{"annotations":[115551],"is_not":false,"summary":null,"term":"FYPO:0009111"},{"annotations":[115548],"is_not":false,"summary":null,"term":"FYPO:0000588"},{"annotations":[115554],"is_not":false,"summary":null,"term":"FYPO:0005705"},{"annotations":[115552],"is_not":false,"summary":null,"term":"FYPO:0005231"},{"annotations":[115550],"is_not":false,"summary":null,"term":"FYPO:0000097"},{"annotations":[115553],"is_not":false,"summary":null,"term":"FYPO:0001408"}]},"doi":"10.3390/jof9050550","gene_count":1,"genes_by_uniquename":{"SJAG_02527":null},"genotypes_by_uniquename":{"lig4::KanMX6-RNA_sequencing_revealed_that_only_the_5'_end_of_the_disrupted_allele_showed_low_RNA_expression_and_coverage-disruption-expression-knockdown":{"display_name":"lig4::KanMX6(RNA sequencing revealed that only the 5' end of the disrupted allele showed low RNA expression and coverage)[Knockdown]","display_uniquename":"lig4::KanMX6-RNA_sequencing_revealed_that_only_the_5'_end_of_the_disrupted_allele_showed_low_RNA_expression_and_coverage-disruption-expression-knockdown","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02527:allele-1","expression":"Knockdown"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-05-26","pubmed_publication_date":"10 May 2023","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000081":null,"FYECO:0000117":null,"FYECO:0000126":null,"FYECO:0000137":null,"FYECO:0000315":null,"FYPO:0000097":null,"FYPO:0000588":null,"FYPO:0001408":null,"FYPO:0005231":null,"FYPO:0005705":null,"FYPO:0007776":null,"FYPO:0009111":null},"title":"Disruption of the  Schizosaccharomyces japonicus lig4  Disturbs Several Cellular Processes and Leads to a Pleiotropic Phenotype.","uniquename":"PMID:37233261"}


id: GO_REF:0000074
data:
  {"abstract":"We have created a standard template for classes describing the export of a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom template is \"GO:0006810 and 'exports' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of export of a chemical as biological process in the Gene Ontology","uniquename":"GO_REF:0000074"}


id: PMID:28733395
data:
  {"abstract":" Schizosaccharomyces japonicus  is a dimorphic yeast. Depending on the nutrient conditions, the transition between growth as yeast cells and growth as hyphal cells can be reversibly induced. In addition to nutrient stress, induced DNA lesions, such as those produced by camptothecin, also induce hyphal growth regardless of the nutrient status. This protocol describes both methods of induction.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Niki H","authors_abbrev":"Niki H","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Cold Spring Harb Protoc 2017 Dec 01;2017(12):pdb.prot091868","cv_annotations":{},"doi":"10.1101/pdb.prot091868","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2017-07-23","pubmed_publication_date":"01 Dec 2017","terms_by_termid":{},"title":"Induction of Hyphal Growth in  Schizosaccharomyces japonicus .","uniquename":"PMID:28733395"}


id: PMID:37279666
data:
  {"abstract":"A new study finds that Schizosaccharomyces japonicus, a eukaryote that lost the ability to respire, modified its central carbon metabolism to maintain efficient ATP production, cofactor regeneration, and amino-acid production. This remarkable metabolic flexibility opens new avenues towards applications.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Cool L, Hanon S, Verstrepen KJ","authors_abbrev":"Cool L et al.","canto_added_date":"2023-06-08 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Curr Biol 2023 Jun 05;33(11):R444-R447","cv_annotations":{},"doi":"10.1016/j.cub.2023.05.002","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-06-06","pubmed_publication_date":"05 Jun 2023","terms_by_termid":{},"title":"Metabolism: How a eukaryote adapted to life without respiration.","uniquename":"PMID:37279666"}


id: GO_REF:0000097
data:
  {"abstract":"FlyBase occasionally makes GO annotations based on information that has been sent to us directly by researchers as a personal communication to FlyBase. In each case, the full details of the communication including any associated data and analyses are recorded in a FlyBase publication (FBrf) available from our website (http://flybase.org).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"FlyBase","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Gene Ontology annotation based on personal communication to FlyBase","uniquename":"GO_REF:0000097"}


id: PMID:11921097
data:
  {"abstract":"The dimorphic fission yeast Schizosaccharomyces japonicus has proved to be an excellent experimental model for the investigation of the eukaryotic cell. Here we show that it has a haplontic life cycle, in which the diploid phase is confined to the zygote. To make it amenable to genetic and molecular analysis, we generated genetic markers and cloned a genomic sequence which acts as ars when integrated into a plasmid. Diploids suitable for testing complementation and recombination between markers can be formed by protoplast fusion. The complementation tests and the recombination frequencies determined in octads of spores identified 28 non-allelic groups (genes) of mutations of the auxotrophic and mycelium-negative mutants. Two groups of linked markers were also identified. The cloned fragment, which expresses ars activity, encodes a putative amino acid sequence highly similar to a conserved domain of proteins Cut1 (Schizosaccharomyces pombe), BimB (Aspergillus nidulans) and Esp1 (Saccharomyces cerevisiae).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bozsik A, Szilagyi Z, Benko Z, Sipiczki M","authors_abbrev":"Bozsik A et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Yeast 2002 Apr;19(6):485-98","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2002","pubmed_entrez_date":"2002-03-29","pubmed_publication_date":"Apr 2002","terms_by_termid":{},"title":"Marker construction and cloning of a cut1-like sequence with ARS activity in the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:11921097"}


id: GO_REF:0000119
data:
  {"abstract":"The Alliance of Genome Resources (https://www.alliancegenome.org/) has procedures in place to establish orthology relationships","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"The Gene Ontology Consortium","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs","uniquename":"GO_REF:0000119"}


id: PMID:12527786
data:
  {"abstract":"The fission yeasts are members of the fungal order Schizosaccharomycetales, a candidate deep-diverging group within Ascomycota. Although a great deal of molecular information is available from Schizosaccharomyces pombe, a model eukaryote, very little is available from other members of this group. In order to better characterize mitochondrial genome evolution in this fungal lineage, the mitochondrial DNA (mtDNA) of two additional fission yeasts, Schizosaccharomyces octosporus and Schizosaccharomyces japonicus var. japonicus, was sequenced. Whereas the mtDNA of S.pombe is only 19 431 bp, the mtDNA of S.octosporus is 44 227 bp, and that of S.japonicus var. japonicus is over 80 kb. The size variation of these mtDNAs is due largely to non-coding regions. The gene content in the latter two mtDNAs is almost identical to that of the completely sequenced S.pombe mtDNA, which encodes 25 tRNA species, the large and small mitochondrial ribosomal RNAs (rnl and rns), the RNA component of mitochondrial RNaseP (rnpB), mitochondrial small subunit ribosomal protein 3 (rps3), cytochrome oxidase subunits 1, 2 and 3 (cox1, cox2 and cox3) and ATP-synthase subunits 6, 8 and 9 (atp6, atp8 and atp9). However, trnI2(cau) (C modified to lysidine) is absent in the S.octosporus mtDNA, as are corresponding ATA codons in its protein-coding genes, and rps3 and rnpB are not found in the mtDNA of S.japonicus var. japonicus. The mtDNA of S.octosporus contains five double hairpin elements, the first report of these elements in an ascomycete. This study provides further evidence in favor of the mobility of these elements, and supports their role in mitochondrial genome rearrangement. The results of our phylogenetic analysis support the monophyly of the Schizosaccharomycetales, but question their grouping within the Archiascomycota.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bullerwell CE, Leigh J, Forget L, Lang BF","authors_abbrev":"Bullerwell CE et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Nucleic Acids Res 2003 Jan 15;31(2):759-68","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2003","pubmed_entrez_date":"2003-01-16","pubmed_publication_date":"15 Jan 2003","terms_by_termid":{},"title":"A comparison of three fission yeast mitochondrial genomes.","uniquename":"PMID:12527786"}


id: PMID:33837814
data:
  {"abstract":"The capability of RNA isolation with good efficiency and high quality is essential for a downstream application such as RNA sequencing. It requires successful cell culturing and an effective RNA isolation method. Although effective methods are available, production of the homogenous mycelia and extraction of good-quality mycelial RNA from true invasive hyphae, which penetrated into the agar plates, are difficult. To overcome these problems, the aim of this study was to develop technical modifications which allow production of homogenous mycelial biomass without extra stimuli agents and improve quality of the RNA extracted from the fungal hyphae. Our alternative culture medium was suitable for production both yeast-phase cells and hyphae of the Schizosaccharomyces japonicus and other dimorphic species, such as the Candida albicans, Saccharomyces cerevisiae, and Jaminaea angkorensis. To improve quality of the mycelial RNA, we developed an isolation procedure of the hyphal tip, which eliminated the unnecessary vacuoles-containing parts of the hyphae. To increase RNA quantity, we used glass beads in the RNA extraction protocol to achieve stronger breaking of the mycelial walls. All these modifications can also be useful for researchers working with other dimorphic fungi and can contribute to the higher comparability of the transcriptional data coming from yeast-phase cells and hyphae or even from different species.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Papp LA, Ács-Szabó L, Póliska S, Miklós I","authors_abbrev":"Papp LA et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Curr Genet 2021 Oct;67(5):823-830","cv_annotations":{},"doi":"10.1007/s00294-021-01181-4","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-04-10","pubmed_publication_date":"Oct 2021","terms_by_termid":{},"title":"A modified culture medium and hyphae isolation method can increase quality of the RNA extracted from mycelia of a dimorphic fungal species.","uniquename":"PMID:33837814"}


id: PMID:33791858
data:
  {"abstract":"Mitogen-activated protein kinase (MAPK) signalling pathways regulate multiple cellular functions in eukaryotic organisms in response to environmental cues, including the dynamic remodeling of the actin cytoskeleton. The fission yeast S. pombe is an optimal model to investigate the conserved regulatory mechanisms of cytokinesis, which relies in an actomyosin-based contractile ring (CAR) that prompts the physical separation of daughter cells during cellular division. Our group has recently shown that p38 MAPK ortholog Sty1, the core component of the stress-activated pathway (SAPK), negatively modulates CAR assembly and integrity in S. pombe during actin cytoskeletal damage induced with Latrunculin A and in response to environmental stress. This response involves downregulation of protein levels of the formin For3, which assembles actin filaments for cables and the CAR, likely through an ubiquitin-mediated degradation mechanism. Contrariwise, Sty1 function positively reinforces CAR assembly during stress in the close relative dimorphic fission yeast S. japonicus. The opposite effect of SAPK signaling on CAR integrity may represent an evolutionary refined adaptation to cope with the marked differences in cytokinesis onset in both fission yeast species.","alleles_by_uniquename":{"SJAG_00266:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00266","name":"atf1delta","uniquename":"SJAG_00266:allele-1"},"SJAG_02592:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02592","name":"sty1delta","uniquename":"SJAG_02592:allele-1"}},"annotation_curators":[{"annotation_count":4,"community_curator":true,"file_name":null,"file_type":null,"name":"Elisa Gómez Gil","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-09-14","authors":"Madrid M, Gómez-Gil E, Cansado J","authors_abbrev":"Madrid M et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-14 21:24:28","canto_approver_orcid":"0000-0002-8138-6851","canto_curator_name":"Elisa Gómez Gil","canto_curator_role":"community","canto_first_approved_date":"2021-09-14 21:24:28","canto_session_key":"84ac20b0ff20a3cd","canto_session_submitted_date":"2021-09-14 16:45:32","canto_triage_status":"Curatable","citation":"Curr Genet 2021 Oct;67(5):715-721","cv_annotations":{"PSI-MOD":[{"annotations":[115562],"is_not":false,"summary":null,"term":"MOD:00696"}],"single_locus_phenotype":[{"annotations":[115561],"is_not":false,"summary":null,"term":"FYPO:0002998"},{"annotations":[115559,115560],"is_not":false,"summary":null,"term":"FYPO:0000107"}]},"doi":"10.1007/s00294-021-01155-6","gene_count":2,"genes_by_uniquename":{"SJAG_00266":null,"SJAG_02592":null},"genotypes_by_uniquename":{"atf1delta":{"display_name":"atf1delta","display_uniquename":"atf1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00266:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]}},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-04-01","pubmed_publication_date":"Oct 2021","terms_by_termid":{"FYECO:0000248":null,"FYPO:0000107":null,"FYPO:0002998":null,"FYPO_EXT:0000001":null,"GO:0120306":null,"MOD:00696":null},"title":"Negative control of cytokinesis by stress-activated MAPK signaling.","uniquename":"PMID:33791858"}


id: PMID:24309281
data:
  {"abstract":"How do nuclear components, apart from chromosomes, partition equally to daughter nuclei during mitosis? In Schizosaccharomyces japonicus, the conserved LEM-domain nuclear envelope protein Man1 ensures the formation of identical daughter nuclei by coupling nuclear pore complexes to the segregating chromosomes. ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Walters AD, Cohen-Fix O","authors_abbrev":"Walters AD et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Curr Biol 2013 Dec 02;23(23):R1045-7","cv_annotations":{},"doi":"10.1016/j.cub.2013.10.041","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2013","pubmed_entrez_date":"2013-12-07","pubmed_publication_date":"02 Dec 2013","terms_by_termid":{},"title":"Nuclear division: giving daughters their fair share.","uniquename":"PMID:24309281"}


id: GO_REF:0000069
data:
  {"abstract":"We have created a standard template for classes describing the transmembrane transport of a chemical entity (ChEBI) as a biological process. The underlying equivalence axiom template is \"GO:0055085 and 'transports or maintains localization of' some X\", where X is a chemical entity (CHEBI:24431). The approach to combine GO and ChEBI has been described in the following publication: PMID:23895341.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of transmembrane transport of a chemical as biological process in the Gene Ontology","uniquename":"GO_REF:0000069"}


id: GO_REF:0000086
data:
  {"abstract":"We have created a standard template for classes describing the differentiation process for a cell type as a biological process. The underlying equivalence axiom template is \"GO:0030154 and 'results in acquisition of features of' some C\", where C is a native cell (CL:0000003).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of cell differentiation as biological process in the Gene Ontology","uniquename":"GO_REF:0000086"}


id: PMID:12795405
data:
  {"abstract":"Spectrin, a component of the membrane skeleton in erythrocytes and other animal cells, has also been identified in plant and fungal cells. However, its postulated role, i.e., the maintenance of shape and elasticity of the plasma membrane, is probably not exerted in walled cells. To study spectrin in these cells, we chose yeasts because of a high morphological variability of their life cycle. The localization of spectrin in the cells and protoplasts of Saccharomyces cerevisiae and Schizosaccharomyces japonicus var. versatilis was detected by immunoblotting, indirect immunofluorescence, and immunogold electron microscopy techniques with the use of anti-chicken and anti-human erythrocyte spectrin antibodies. A protein band of 220-240 kDa and some bands of lower relative mass were detected in cell and protoplast extracts of both yeast strains. Spectrin-like proteins were revealed by fluorescence microscopy at cell surfaces and in vacuolar membranes. Immunogold-labelling showed spectrin-like proteins in the plasma membrane, endoplasmic reticulum, vacuoles, nuclei, vesicles, mitochondria, and cell walls. The topology of spectrin was not affected by actin depolymerization with Latrunculin B nor was it changed in either act1-1 or cdc42 mutants, under restrictive conditions. Under osmotic stress, both spectrin and actin were delocalized and appeared in the form of large clusters in the cytoplasm. It is concluded that a protein cross-reacting with spectrin antibodies is present in fission and budding yeasts. Generally, it is located in the proximity of the plasma membrane and other intracellular membranes, probably as a part of the membrane skeleton. No evidence of its relationship to either actin or growth zones of the cell can be provided.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Slaninová I, Holubárová A, Svoboda A","authors_abbrev":"Slaninová I et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Can J Microbiol 2003 Mar;49(3):189-96","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2003","pubmed_entrez_date":"2003-06-11","pubmed_publication_date":"Mar 2003","terms_by_termid":{},"title":"Immunodetection of spectrin-like proteins in yeasts.","uniquename":"PMID:12795405"}


id: GO_REF:0000076
data:
  {"abstract":"We have created a standard template for classes describing the transport or vesicle-mediated transport from cellular component to cellular component as a biological process. The underlying equivalence axiom templates are \"GO:0006810 and 'has_target_start_location' some F and 'has_target_end_location' some T\" (transport) and \"GO:0016192 and 'has_target_start_location' some F and 'has_target_end_location' some T\" (vesicle-mediated transport), where F and T are a cellular components.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of transport or vesicle-mediated transport from cell component to cell component as biological process in the Gene Ontology","uniquename":"GO_REF:0000076"}


id: GO_REF:0000091
data:
  {"abstract":"We have created a standard template for classes describing the cell migration process for a cell type as a biological process. The underlying equivalence axiom template is \"'cell migration' and 'alters_location_of' some C\", where C is a native cell (CL:0000004).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GO ontology editors","canto_curator_role":"JaponicusDB","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{},"title":"Representation of cell migration as biological processes in the Gene Ontology","uniquename":"GO_REF:0000091"}


id: PMID:12402243
data:
  {"abstract":"The structure and localization of the microtubule organization centres (MTOCs) of the fission yeast Schizosaccharomyces japonicus var. japonicus were examined by fluorescence microscopy and electron microscopy. Spindle pole bodies (SPBs), which are the fungal equivalent of centrosomes, of Sz. japonicus were visualized by immunofluorescent staining using a monoclonal anti-gamma-tubulin antibody. The behaviour of the SPBs during the cell cycle mostly coincided with previous reports on the most widely used fission yeast Schizosaccharomyces pombe. We cloned the gamma-tubulin gene from Sz. japonicus by PCR using redundant sets of primers corresponding to conserved regions of known gamma-tubulins. The predicted amino acid sequence of Sz. japonicus gamma-tubulin was most similar to the Sz. pombe gamma-tubulin. Under the electron microscope, the SPBs of Sz. japonicus were detected as electron-dense multilayered structures located just outside the nuclear envelope. The SPBs of Sz. japonicus were composed of three electron-dense layers and were surrounded by fuzzy material. Each layer showed structural changes according to the progression of the cell cycle. In mitotic cells, the SPBs were located on the fenestrae of the nuclear envelopes through which the mitotic spindle microtubules ran into the nucleoplasm. Our results show that Sz. japonicus is a very potent and attractive organism for the investigation of the microtubule nucleation system and morphogenesis in yeasts. The Accession No. for the nucleotide sequence of the Sz. japonicus gtb1(+) gene is AF159163.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Horio T, Kimura N, Basaki A, Tanaka Y, Noguchi T, Akashi T, Tanaka K","authors_abbrev":"Horio T et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Yeast 2002 Nov;19(15):1335-50","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2002","pubmed_entrez_date":"2002-10-29","pubmed_publication_date":"Nov 2002","terms_by_termid":{},"title":"Molecular and structural characterization of the spindle pole bodies in the fission yeast Schizosaccharomyces japonicus var japonicus.","uniquename":"PMID:12402243"}


id: PMID:37562570
data:
  {"abstract":"Membrane biophysical properties are critical to cell fitness and depend on unsaturated phospholipid acyl tails. These can only be produced in aerobic environments since eukaryotic desaturases require molecular oxygen. This raises the question of how cells maintain bilayer properties in anoxic environments. Using advanced microscopy, molecular dynamics simulations, and lipidomics by mass spectrometry we demonstrated the existence of an alternative pathway to regulate membrane fluidity that exploits phospholipid acyl tail length asymmetry, replacing unsaturated species in the membrane lipidome. We show that the fission yeast, Schizosaccharomyces japonicus, which can grow in aerobic and anaerobic conditions, is capable of utilizing this strategy, whereas its sister species, the well-known model organism Schizosaccharomyces pombe, cannot. The incorporation of asymmetric-tailed phospholipids might be a general adaptation to hypoxic environmental niches.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Panconi L, Lorenz CD, May RC, Owen DM, Makarova M","authors_abbrev":"Panconi L et al.","canto_added_date":"2023-08-12 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Biol Chem 2023 Sep;299(9):105134","cv_annotations":{},"doi":"10.1016/j.jbc.2023.105134","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-08-10","pubmed_publication_date":"Sep 2023","terms_by_termid":{},"title":"Phospholipid tail asymmetry allows cellular adaptation to anoxic environments.","uniquename":"PMID:37562570"}


id: PMID:24699070
data:
  {"abstract":"The post-cytokinetic separation of cells in cell-walled organisms involves enzymic processes that degrade a specific layer of the division septum and the region of the mother cell wall that edges the septum. In the fission yeast Schizosaccharomyces pombe, the 1,3-α-glucanase Agn1p, originally identified as a mutanase-like glycoside hydrolase family 71 (GH71) enzyme, dissolves the mother cell wall around the septum edge. Our search in the genomes of completely sequenced fungi identified GH71 hydrolases in Basidiomycota, Taphrinomycotina and Pezizomycotina, but not in Saccharomycotina. The most likely Agn1p orthologues in Pezizomycotina species are not mutanases having mutanase-binding domains, but experimentally non-characterized hypothetical proteins that have no carbohydrate-binding domains. The analysis of the GH71 domains corroborated the phylogenetic relationships of the Schizosaccharomyces species determined by previous studies, but suggested a closer relationship to the Basidiomycota proteins than to the Ascomycota proteins. In the Schizosaccharomyces genus, the Agn1p proteins are structurally conserved: their GH71 domains are flanked by N-terminal secretion signals and C-terminal sequences containing the conserved block YNFNA(Y)/HTG. The inactivation of the agn1(Sj) gene in Schizosaccharomyces japonicus, the only true dimorphic member of the genus, caused a severe cell-separation defect in its yeast phase, but had no effect on the hyphal growth and yeast-to-mycelium transition. It did not affect the mycelium-to-yeast transition either, only delaying the separation of the yeast cells arising from the fragmenting hyphae. The heterologous expression of agn1(Sj) partially rescued the separation defect of the agn1Δ cells of Schizosaccharomyces pombe. The results presented indicate that the fission yeast Agn1p 1,3-α-glucanases of Schizosaccharomyces japonicus and Schizosaccharomyces pombe share conserved functions in the yeast phase. ","alleles_by_uniquename":{"SJAG_03444:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03444","name":"agn1delta","uniquename":"SJAG_03444:allele-1"}},"annotation_curators":[{"annotation_count":1,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"},{"annotation_count":1,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-09","authors":"Sipiczki M, Balazs A, Monus A, Papp L, Horvath A, Sveiczer A, Miklos I","authors_abbrev":"Sipiczki M et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-01 07:35:20","canto_approver_orcid":"0000-0001-6330-7526","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-09 13:16:43","canto_session_key":"b8bc1733e6f2c600","canto_session_submitted_date":"2021-07-09 13:16:35","canto_triage_status":"Curatable","citation":"Microbiology (Reading) 2014 Jun;160(Pt 6):1063-1074","cv_annotations":{"biological_process":[{"annotations":[115414],"is_not":false,"summary":null,"term":"GO:0030995"}],"single_locus_phenotype":[{"annotations":[115413],"is_not":false,"summary":null,"term":"FYPO:0001971"}]},"doi":"10.1099/mic.0.077511-0","gene_count":1,"genes_by_uniquename":{"SJAG_03444":null},"genotypes_by_uniquename":{"agn1delta":{"display_name":"agn1delta","display_uniquename":"agn1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03444:allele-1","expression":"Null"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2014","pubmed_entrez_date":"2014-04-05","pubmed_publication_date":"Jun 2014","terms_by_termid":{"FYPO:0001971":null,"GO:0030995":null},"title":"Phylogenetic and comparative functional analysis of the cell-separation α-glucanase Agn1p in Schizosaccharomyces.","uniquename":"PMID:24699070"}


id: PMID:31956022
data:
  {"abstract":"Membrane function is fundamental to life. Each species explores membrane lipid diversity within a genetically predefined range of possibilities. How membrane lipid composition in turn defines the functional space available for evolution of membrane-centered processes remains largely unknown. We address this fundamental question using related fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus. We show that, unlike S. pombe that generates membranes where both glycerophospholipid acyl tails are predominantly 16-18 carbons long, S. japonicus synthesizes unusual \"asymmetrical\" glycerophospholipids where the tails differ in length by 6-8 carbons. This results in stiffer bilayers with distinct lipid packing properties. Retroengineered S. pombe synthesizing the S.-japonicus-type phospholipids exhibits unfolded protein response and downregulates secretion. Importantly, our protein sequence comparisons and domain swap experiments support the hypothesis that transmembrane helices co-evolve with membranes, suggesting that, on the evolutionary scale, changes in membrane lipid composition may necessitate extensive adaptation of the membrane-associated proteome.","alleles_by_uniquename":{"SJAG_01458:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01458","name":"acb1delta","uniquename":"SJAG_01458:allele-1"}},"annotation_curators":[{"annotation_count":4,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-09","authors":"Makarova M, Peter M, Balogh G, Glatz A, MacRae JI, Lopez Mora N, Booth P, Makeyev E, Vigh L, Oliferenko S","authors_abbrev":"Makarova M et al.","canto_added_date":"2021-05-10 02:37:19","canto_annotation_status":"APPROVED","canto_approved_date":"2021-07-09 13:38:09","canto_approver_orcid":"0000-0002-8138-6851","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-09 13:38:09","canto_session_key":"801e82954edbb6c1","canto_session_submitted_date":"2021-07-09 13:38:00","canto_triage_status":"Curatable","citation":"Curr Biol 2020 02 03;30(3):367-380.e8","cv_annotations":{"cellular_component":[{"annotations":[115152],"is_not":false,"summary":null,"term":"GO:0005801"},{"annotations":[115154],"is_not":false,"summary":null,"term":"GO:0005829"}],"single_locus_phenotype":[{"annotations":[115153],"is_not":false,"summary":null,"term":"FYPO:0000719"}]},"doi":"10.1016/j.cub.2019.11.043","gene_count":4,"genes_by_uniquename":{"SJAG_00816":null,"SJAG_01458":null,"SJAG_04107":null,"SJAG_04972":null},"genotypes_by_uniquename":{"acb1delta":{"display_name":"acb1delta","display_uniquename":"acb1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01458:allele-1","expression":"Null"}]}]}},"ltp_gene_count":4,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[{"evidence":"Co-purification","gene_uniquename":"SJAG_04972","interactor_uniquename":"SJAG_04107","reference_uniquename":"PMID:31956022","throughput":"low"}],"publication_year":"2020","pubmed_entrez_date":"2020-01-21","pubmed_publication_date":"03 02 2020","terms_by_termid":{"FYECO:0000126":null,"FYPO:0000719":null,"GO:0005801":null,"GO:0005829":null},"title":"Delineating the Rules for Structural Adaptation of Membrane-Associated Proteins to Evolutionary Changes in Membrane Lipidome.","uniquename":"PMID:31956022"}


id: GO_REF:0000107
data:
  {"abstract":"GO terms from a source species are projected onto one or more target species based on gene orthology obtained from Ensembl Compara. One-to-one, one-to-many and many-to-many orthology relations and anntations are transferred between orthologs that have at least a 40% peptide identity to each other. Only GO annotations with evidence codes ECO:0000314 (IDA), ECO:0000270 (IEP), ECO:0000316 (IGI), ECO:0000315 (IMP), and ECO:0000353 (IPI), or their descendants, are transferred; annotations with a 'NOT' qualifier are not transferred, and neither are annotations to GO:0005515 (protein binding). Annotations that are transferred using this method receive the evidence code ECO:0000265 (sequence orthology evidence used in automatic assertion), which maps up to the GO Inferred from Electronic Annotation (IEA) evidence code.  The model organism database identifier of the annotation source will be indicated in the 'With' column of the GOA association file.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"GOA 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