# refs

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:27734801
data:
  {"abstract":"Many eukaryotes assemble a ring-shaped actomyosin network that contracts to drive cytokinesis. Unlike actomyosin in sarcomeres, which cycles through contraction and relaxation, the cytokinetic ring disassembles during contraction through an unknown mechanism. Here we find in  Schizosaccharomyces japonicus  and  Schizosaccharomyces pombe  that, during actomyosin ring contraction, actin filaments associated with actomyosin rings are expelled as micron-scale bundles containing multiple actomyosin ring proteins. Using functional isolated actomyosin rings we show that expulsion of actin bundles does not require continuous presence of cytoplasm. Strikingly, mechanical compression of actomyosin rings results in expulsion of bundles predominantly at regions of high curvature. Our work unprecedentedly reveals that the increased curvature of the ring itself promotes its disassembly. It is likely that such a curvature-induced mechanism may operate in disassembly of other contractile networks.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":2,"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":"Huang J, Chew TG, Gu Y, Palani S, Kamnev A, Martin DS, Carter NJ, Cross RA, Oliferenko S, Balasubramanian MK","authors_abbrev":"Huang J et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-07-09 15:10:46","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-09 15:10:46","canto_session_key":"f47401f00ac444e0","canto_session_submitted_date":"2021-07-09 15:10:39","canto_triage_status":"Curatable","citation":"Elife 2016 10 13;5","cv_annotations":{"cellular_component":[{"annotations":[115856],"is_not":false,"summary":null,"term":"GO:0032432"},{"annotations":[115855],"is_not":false,"summary":null,"term":"GO:0005826"}]},"doi":"10.7554/eLife.21383","gene_count":1,"genes_by_uniquename":{"SJAG_04887":null},"genotypes_by_uniquename":{},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2016","pubmed_entrez_date":"2016-10-14","pubmed_publication_date":"13 10 2016","terms_by_termid":{"GO:0005826":null,"GO:0032432":null},"title":"Curvature-induced expulsion of actomyosin bundles during cytokinetic ring contraction.","uniquename":"PMID:27734801"}


id: PMID:25361970
data:
  {"abstract":"PomBase (http://www.pombase.org) is the model organism database for the fission yeast Schizosaccharomyces pombe. PomBase provides a central hub for the fission yeast community, supporting both exploratory and hypothesis-driven research. It provides users easy access to data ranging from the sequence level, to molecular and phenotypic annotations, through to the display of genome-wide high-throughput studies. Recent improvements to the site extend annotation specificity, improve usability and allow for monthly data updates. Both in-house curators and community researchers provide manually curated data to PomBase. The genome browser provides access to published high-throughput data sets and the genomes of three additional Schizosaccharomyces species (Schizosaccharomyces cryophilus, Schizosaccharomyces japonicus and Schizosaccharomyces octosporus). ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"McDowall MD, Harris MA, Lock A, Rutherford K, Staines DM, Bähler J, Kersey PJ, Oliver SG, Wood V","authors_abbrev":"McDowall MD et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Database","citation":"Nucleic Acids Res 2015 Jan;43(Database issue):D656-61","cv_annotations":{},"doi":"10.1093/nar/gku1040","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":"2014-11-02","pubmed_publication_date":"Jan 2015","terms_by_termid":{},"title":"PomBase 2015: updates to the fission yeast database.","uniquename":"PMID:25361970"}


id: PMID:32265131
data:
  {"abstract":"The N- and O-linked oligosaccharides from fission yeast Schizosaccharomyces pombe not only contain large amounts of d-mannose (Man) but also contain large amounts of d-galactose (Gal). Although the galactomannans of S. pombe are mainly composed of α1,2- or α1,3-linked Gals, some of the terminal α1,2-linked Gals are found to be linked to pyruvylated β1,3-linked galactose (PvGal). We have determined the structural characteristics of the N-glycans and O-glycans in three Schizosaccharomyces species (S. japonicus, S. octosporus, and S. cryophilus) using lectin blot,  1 H NMR spectroscopy, and size-fractionation high performance liquid chromatography (HPLC), and found that the galactosylation of oligosaccharides was a common feature in fission yeasts. In addition, each of the terminal Galα1,2-, Galβ1,3- and non-substituted Man residues exhibited distinct characteristics. A BLAST search of gene databases in Schizosaccharomyces identified genes homologous to pvg1 encoding pyruvyltransferase of S. pombe. These genes, when expressed in an S. pombe pvg1Δ strains, led to the pyruvylation of non-reducing terminal β-linked Gal, suggesting the biosynthetic pathway of PvGal-containing oligosaccharides is highly conserved in fission yeasts.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Fukunaga T, Tanaka N, Furumoto T, Nakakita S, Ohashi T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Fukunaga 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 Biosci Bioeng 2020 Aug;130(2):128-136","cv_annotations":{},"doi":"10.1016/j.jbiosc.2020.03.008","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":"2020-04-09","pubmed_publication_date":"Aug 2020","terms_by_termid":{},"title":"Characterization of N- and O-linked galactosylated oligosaccharides from fission yeast species.","uniquename":"PMID:32265131"}


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: PMID:28228545
data:
  {"abstract":"Inactivation of retrotransposons is accompanied by the emergence of centromere-binding protein-B (CENPB) in  Schizosaccharomyces , as well as in metazoans. The RNA interference (RNAi)-induced transcriptional silencing (RITS) complex, comprising chromodomain protein-1 (Chp1), Tas3 (protein with unknown function), and Argonaute (Ago1), plays an important role in RNAi-mediated heterochromatinization. We find that whereas the Ago1 subunit of the RITS complex is highly conserved, Tas3 is lost and Chp1 is truncated in  Schizosaccharomyces cryophilus  and  Schizosaccharomyces octosporus  We show that truncated Chp1 loses the property of heterochromatin localization and silencing when transformed in  Schizosaccharomyces pombe  Furthermore, multiple copies of CENPB, related to  Tc1/mariner and Tc5  transposons, occur in all  Schizosaccharomyces  species, as well as in humans, but with loss of transposase function (except  Schizosaccharomyces japonicus ). We propose that acquisition of  Tc1/mariner and Tc5  elements by horizontal transfer in  S. pombe  (and humans) is accompanied by alteration of their function from a transposase/endonuclease to a heterochromatin protein, designed to suppress transposon expression and recombination. The resulting redundancy of RITS may have eased the selection pressure, resulting in progressive loss or truncation of  tas3  and  chp1  genes in  S. octosporus  and  S. cryophilus  and triggered similar evolutionary dynamics in the metazoan orthologues.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Upadhyay U, Srivastava S, Khatri I, Nanda JS, Subramanian S, Arora A, Singh J","authors_abbrev":"Upadhyay U et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Phylogeny and evolutionary studies","citation":"Mol Biol Cell 2017 Apr 15;28(8):1132-1146","cv_annotations":{},"doi":"10.1091/mbc.E16-07-0485","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":"2017-02-24","pubmed_publication_date":"15 Apr 2017","terms_by_termid":{},"title":"Ablation of RNA interference and retrotransposons accompany acquisition and evolution of transposases to heterochromatin protein CENPB.","uniquename":"PMID:28228545"}


id: PMID:9884240
data:
  {"abstract":"Fission yeast cells grow by extension at the ends (poles) and divide by transverse fission. It has previously been reported that Schizosaccharomyces japonicus var. japonicus can switch to unipolar, filamentous growth. Here it is shown that the yeast-to-mycelium transition is a gradual process involving a changeover to unipolar growth associated with asymmetric divisions, the development of large polarly located vacuoles, the modifications of the actin and microtubular cytoskeleton and the repression of cell separation after division. High concentrations of glucose in the medium or supplementation of the medium with caffeine or cAMP support the bipolar yeast phase, inhibit the transition to the mycelial phase and induce the conversion of hyphae to yeasts. These effects suggest that cAMP may be involved in the regulation of dimorphism. Temperatures below 18 degrees C or over 35 degrees C are restrictive for the mycelial phase and provoke a return to yeast phase.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-10-07","authors":"Sipiczki M, Takeo K, Grallert A","authors_abbrev":"Sipiczki M et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-10-07 12:31:51","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-10-07 12:31:51","canto_session_key":"5ac54d09f220d215","canto_session_submitted_date":"2021-09-30 09:01:47","canto_triage_status":"Curatable","citation":"Microbiology (Reading) 1998 Dec;144 ( Pt 12):3475-3485","cv_annotations":{},"doi":"10.1099/00221287-144-12-3475","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1998","pubmed_entrez_date":"1999-01-12","pubmed_publication_date":"Dec 1998","terms_by_termid":{},"title":"Growth polarity transitions in a dimorphic fission yeast.","uniquename":"PMID:9884240"}


id: PMID:22586155
data:
  {"abstract":"tRNA genes are interspersed throughout eukaryotic DNA, contributing to genome architecture and evolution in addition to translation of the transcriptome. Codon use correlates with tRNA gene copy number in noncomplex organisms including yeasts. Synonymous codons impact translation with various outcomes, dependent on relative tRNA abundances. Availability of whole-genome sequences allowed us to examine tRNA gene copy number variation (tgCNV) and codon use in four Schizosaccharomyces species and Saccharomyces cerevisiae. tRNA gene numbers vary from 171 to 322 in the four Schizosaccharomyces despite very high similarity in other features of their genomes. In addition, we performed whole-genome sequencing of several related laboratory strains of Schizosaccharomyces pombe and found tgCNV at a cluster of tRNA genes. We examined for the first time effects of wobble rules on correlation of tRNA gene number and codon use and showed improvement for S. cerevisiae and three of the Schizosaccharomyces species. In contrast, correlation in Schizosaccharomyces japonicus is poor due to markedly divergent tRNA gene content, and much worsened by the wobble rules. In japonicus, some tRNA iso-acceptor genes are absent and others are greatly reduced relative to the other yeasts, while genes for synonymous wobble iso-acceptors are amplified, indicating wobble use not apparent in any other eukaryote. We identified a subset of japonicus-specific wobbles that improves correlation of codon use and tRNA gene content in japonicus. We conclude that tgCNV is high among Schizo species and occurs in related laboratory strains of S. pombe (and expectedly other species), and tRNAome-codon analyses can provide insight into species-specific wobble decoding.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Iben JR, Maraia RJ","authors_abbrev":"Iben JR et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"RNA 2012 Jul;18(7):1358-72","cv_annotations":{},"doi":"10.1261/rna.032151.111","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2012","pubmed_entrez_date":"2012-05-16","pubmed_publication_date":"Jul 2012","terms_by_termid":{},"title":"tRNAomics: tRNA gene copy number variation and codon use provide bioinformatic evidence of a new anticodon:codon wobble pair in a eukaryote.","uniquename":"PMID:22586155"}


id: PMID:26457121
data:
  {"abstract":"Transposable elements (TEs) are common constituents of centromeres. However, it is not known what causes this relationship. Schizosaccharomyces japonicus contains 10 families of Long Terminal Repeat (LTR)-retrotransposons and these elements cluster in centromeres and telomeres. In the related yeast, Schizosaccharomyces pombe LTR-retrotransposons Tf1 and Tf2 are distributed in the promoter regions of RNA pol II transcribed genes. Sequence analysis of TEs indicates that Tj1 of S. japonicus is related to Tf1 and Tf2, and uses the same mechanism of self-primed reverse transcription. Thus, we wondered why these related retrotransposons localized in different regions of the genome.\nTo characterize the integration behavior of Tj1 we expressed it in S. pombe. We found Tj1 was active and capable of generating de novo integration in the chromosomes of S. pombe. The expression of Tj1 is similar to Type C retroviruses in that a stop codon at the end of Gag must be present for efficient integration. 17 inserts were sequenced, 13 occurred within 12 bp upstream of tRNA genes and 3 occurred at other RNA pol III transcribed genes. The link between Tj1 integration and RNA pol III transcription is reminiscent of Ty3, an LTR-retrotransposon of Saccharomyces cerevisiae that interacts with TFIIIB and integrates upstream of tRNA genes.\nThe integration of Tj1 upstream of tRNA genes and the centromeric clustering of tRNA genes in S. japonicus demonstrate that the clustering of this TE in centromere sequences is due to a unique pattern of integration.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Guo Y, Singh PK, Levin HL","authors_abbrev":"Guo Y et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Mob DNA 2015;6:19","cv_annotations":{},"doi":"10.1186/s13100-015-0048-2","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":"2015-10-13","pubmed_publication_date":"2015","terms_by_termid":{},"title":"A long terminal repeat retrotransposon of Schizosaccharomyces japonicus integrates upstream of RNA pol III transcribed genes.","uniquename":"PMID:26457121"}


id: PMID:24184107
data:
  {"abstract":"During cellular proliferation, the mother nucleus divides into two daughters, each carrying a full complement of chromosomes and capable of driving the next cell cycle. Mitotic chromosome segregation must be coordinated with remodeling of other nuclear components, including the nuclear envelope (NE) and the non-membrane-bound nucleolus. Here, we show that in the fission yeast Schizosaccharomyces japonicus, which breaks and reforms the NE during mitosis, the evolutionary conserved LEM-domain protein Man1 promotes equal partitioning of the nuclear membrane, nucleolar remodeling, and efficient inheritance of the nuclear pore complexes (NPCs) by the daughter nuclei. Analyses of man1 mutants and results obtained using an artificial chromatin-nuclear pore tether suggest that Man1 may exert its function by linking the NPCs to segregating chromatin. By integrating the partitioning of the nuclear membrane and nucleolar material with chromosome segregation, cells build two nearly identical copies of the original nucleus.","alleles_by_uniquename":{"SJAG_01834:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01834","name":"pom152delta","uniquename":"SJAG_01834:allele-1"},"SJAG_03449:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03449","name":"man1delta","uniquename":"SJAG_03449:allele-1"},"SJAG_03449:allele-2":{"allele_type":"partial_amino_acid_deletion","description":"man1DHEH","gene_uniquename":"SJAG_03449","name":"Man1DHEH","uniquename":"SJAG_03449:allele-2"},"SJAG_03449:allele-3":{"allele_type":"amino_acid_insertion_and_deletion","description":"man1-1-488","gene_uniquename":"SJAG_03449","name":"man1-1-488","uniquename":"SJAG_03449:allele-3"}},"annotation_curators":[{"annotation_count":17,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"},{"annotation_count":2,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-27","authors":"Yam C, Gu Y, Oliferenko S","authors_abbrev":"Yam C et al.","canto_added_date":"2021-05-10 02:38:18","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-01 07:25:17","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-27 11:54:17","canto_session_key":"0f2dda384385121f","canto_session_submitted_date":"2021-07-27 11:54:10","canto_triage_status":"Curatable","citation":"Curr Biol 2013 Nov 18;23(22):2303-2310","cv_annotations":{"biological_process":[{"annotations":[116086],"is_not":false,"summary":null,"term":"GO:0101024"}],"cellular_component":[{"annotations":[116071],"is_not":false,"summary":null,"term":"GO:0000781"},{"annotations":[116070],"is_not":false,"summary":null,"term":"GO:0140573"},{"annotations":[116073],"is_not":false,"summary":null,"term":"GO:0005643"},{"annotations":[116072],"is_not":false,"summary":null,"term":"GO:0030875"}],"molecular_function":[{"annotations":[116087],"is_not":false,"summary":null,"term":"GO:0062239"}],"single_locus_phenotype":[{"annotations":[116074,116079,116081],"is_not":false,"summary":null,"term":"FYPO:0003779"},{"annotations":[116083,116084,116085],"is_not":false,"summary":null,"term":"FYPO:0000671"},{"annotations":[116076,116077,116078,116080],"is_not":false,"summary":null,"term":"FYPO:0004890"},{"annotations":[116075],"is_not":false,"summary":null,"term":"FYPO:0001234"},{"annotations":[116082],"is_not":false,"summary":null,"term":"FYPO:0004683"}]},"doi":"10.1016/j.cub.2013.09.057","gene_count":5,"genes_by_uniquename":{"SJAG_00302":null,"SJAG_01777":null,"SJAG_01834":null,"SJAG_03449":null,"SJAG_03603":null},"genotypes_by_uniquename":{"Man1DHEH-man1DHEH-partial_amino_acid_deletion-expression-not_assayed_or_wild_type":{"display_name":"Man1DHEH(man1DHEH)","display_uniquename":"Man1DHEH-man1DHEH-partial_amino_acid_deletion-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03449:allele-2","expression":"Not assayed or wild type"}]}]},"man1-1-488-man1-1-488-amino_acid_insertion_and_deletion-expression-not_assayed_or_wild_type":{"display_name":"man1-1-488(aa)","display_uniquename":"man1-1-488-man1-1-488-amino_acid_insertion_and_deletion-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03449:allele-3","expression":"Not assayed or wild type"}]}]},"man1delta":{"display_name":"man1delta","display_uniquename":"man1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03449:allele-1","expression":"Null"}]}]},"pom152delta":{"display_name":"pom152delta","display_uniquename":"pom152delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01834:allele-1","expression":"Null"}]}]}},"ltp_gene_count":5,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2013","pubmed_entrez_date":"2013-11-05","pubmed_publication_date":"18 Nov 2013","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000162":null,"FYPO:0000671":null,"FYPO:0001234":null,"FYPO:0003779":null,"FYPO:0004683":null,"FYPO:0004890":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null,"GO:0000781":null,"GO:0005643":null,"GO:0030875":null,"GO:0062239":null,"GO:0101024":null,"GO:0140573":null},"title":"Partitioning and remodeling of the Schizosaccharomyces japonicus mitotic nucleus require chromosome tethers.","uniquename":"PMID:24184107"}


id: PMID:36148799
data:
  {"abstract":"Tropomyosins are structurally conserved α-helical coiled-coil proteins that bind along the length of filamentous actin (F-actin) in fungi and animals. Tropomyosins play essential roles in the stability of actin filaments and in regulating myosin II contractility. Despite the crucial role of tropomyosin in actin cytoskeletal regulation, in vivo investigations of tropomyosin are limited, mainly due to the suboptimal live-cell imaging tools currently available. Here, we report on an mNeonGreen (mNG)-tagged tropomyosin, with native promoter and linker length configuration, that clearly reports tropomyosin dynamics in Schizosaccharomyces pombe (Cdc8), Schizosaccharomyces japonicus (Cdc8) and Saccharomyces cerevisiae (Tpm1 and Tpm2). We also describe a fluorescent probe to visualize mammalian tropomyosin (TPM2 isoform). Finally, we generated a camelid nanobody against S. pombe Cdc8, which mimics the localization of mNG-Cdc8 in vivo. Using these tools, we report the presence of tropomyosin in previously unappreciated patch-like structures in fission and budding yeasts, show flow of tropomyosin (F-actin) cables to the cytokinetic actomyosin ring and identify rearrangements of the actin cytoskeleton during mating. These powerful tools and strategies will aid better analyses of tropomyosin and F-actin cables in vivo.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":3,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-11-25","authors":"Hatano T, Lim TC, Billault-Chaumartin I, Dhar A, Gu Y, Massam-Wu T, Scott W, Adishesha S, Chapa-Y-Lazo B, Springall L, Sivashanmugam L, Mishima M, Martin SG, Oliferenko S, Palani S, Balasubramanian MK","authors_abbrev":"Hatano T et al.","canto_added_date":"2022-11-25 12:03:53","canto_annotation_status":"APPROVED","canto_approved_date":"2022-11-25 12:11:22","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2022-11-25 12:11:22","canto_session_key":"d572e8fc7f8a7a38","canto_session_submitted_date":"2022-11-25 12:11:07","canto_triage_status":"Curatable","citation":"J Cell Sci 2022 Sep 15;135(18)","cv_annotations":{"cellular_component":[{"annotations":[115878],"is_not":false,"summary":null,"term":"GO:0070648"},{"annotations":[115880],"is_not":false,"summary":null,"term":"GO:1990819"},{"annotations":[115879],"is_not":false,"summary":null,"term":"GO:0110085"}]},"doi":"10.1242/jcs.260288","gene_count":1,"genes_by_uniquename":{"SJAG_04887":null},"genotypes_by_uniquename":{},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-09-23","pubmed_publication_date":"15 Sep 2022","terms_by_termid":{"GO:0070648":null,"GO:0110085":null,"GO:1990819":null},"title":"mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells.","uniquename":"PMID:36148799"}


id: PMID:28342076
data:
  {"abstract":"Environmental glucose is an important regulator of biological processes, as it can launch different cell processes depending on its concentration. Thus, low glucose concentration can induce entry into quiescence, which ensures long-term viability for the cells or in other cases mycelial growth in the dimorphic species, which, in turn, provides the cells with fresh nutrients. Several genes, such as the genes of cAMP cascade, are involved in glucose sensing and response. Since this signal transduction pathway seemed to be an evolutionarily conserved process, we assumed that its genes were also conserved and preserved their functional homology. To obtain evidence, Schizosaccharomyces pombe rsv1 and its orthologous genes were investigated using in silico and experimental approaches. Our results supported that the Rsv1 zinc-finger transcription factors of Schizosaccharomyces japonicus and Schizosaccharomyces octosporus and the Candida albicans cas5p were really functional homologues of the S. pombe Rsv1. Namely, the homologous proteins were able to restore mutant phenotype of the S. pombe rsv1-deleted cells. Bioinformatic anaysis revealed that the most conserved parts of the proteins always contained the C2H2 domains and the complementation abilities of the counterpart genes were not uniform regarding the investigated features, which can be in connection with the conserved regions outside C2H2.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Pataki E, Sipiczki M, Miklos I","authors_abbrev":"Pataki E et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Curr Microbiol 2017 Jun;74(6):710-717","cv_annotations":{},"doi":"10.1007/s00284-017-1227-9","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":"2017-03-26","pubmed_publication_date":"Jun 2017","terms_by_termid":{},"title":"Schizosaccharomyces pombe rsv1 Transcription Factor and its Putative Homologues Preserved their Functional Homology and are Evolutionarily Conserved.","uniquename":"PMID:28342076"}


id: PMID:23873862
data:
  {"abstract":"Many fungi respond to light and regulate fungal development and behavior. A blue light-activated complex has been identified in Neurospora crassa as the product of the wc-1 and wc-2 genes. Orthologs of WC-1 and WC-2 have hitherto been found only in filamentous fungi and not in yeast, with the exception of the basidiomycete pathogenic yeast Cryptococcus. Here, we report that the fission yeast Schizosaccharomyces japonicus responds to blue light depending on Wcs1 and Wcs2, orthologs of components of the WC complex. Surprisingly, those of ascomycete S. japonicus are more closely related to those of the basidiomycete. S. japonicus reversibly changes from yeast to hyphae in response to environmental stresses. After incubation at 30°C, a colony of yeast was formed, and then hyphal cells extended from the periphery of the colony. When light cycles were applied, distinct dark- and bright-colored hyphal cell stripes were formed because the growing hyphal cells had synchronously activated cytokinesis. In addition, temperature cycles of 30°C for 12 h and 35°C for 12 h or of 25°C for 12 h and 30°C for 12 h during incubation in the dark induced a response in the hyphal cells similar to that of light. The stripe formation of the temperature cycles was independent of the wcs genes. Both light and temperature, which are daily external cues, have the same effect on growing hyphal cells. A dual sensing mechanism of external cues allows organisms to adapt to daily changes of environmental alteration. ","alleles_by_uniquename":{"SJAG_02860:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02860","name":"wcs1delta","uniquename":"SJAG_02860:allele-1"},"SJAG_05242:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_05242","name":"wcs2delta","uniquename":"SJAG_05242:allele-1"}},"annotation_curators":[{"annotation_count":7,"community_curator":true,"file_name":null,"file_type":null,"name":"Sho Okamoto","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-12-01","authors":"Okamoto S, Furuya K, Nozaki S, Aoki K, Niki H","authors_abbrev":"Okamoto S et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2022-12-01 10:29:08","canto_curator_name":"Sho Okamoto","canto_curator_role":"community","canto_first_approved_date":"2022-12-01 10:29:08","canto_session_key":"0e71b7054e7d7754","canto_session_submitted_date":"2022-12-01 10:28:58","canto_triage_status":"Curatable","citation":"Eukaryot Cell 2013 Sep;12(9):1235-43","cv_annotations":{"biological_process":[{"annotations":[116246,116247],"is_not":false,"summary":null,"term":"GO:0071483"}],"molecular_function":[{"annotations":[116245],"is_not":false,"summary":null,"term":"GO:0009882"}],"single_locus_phenotype":[{"annotations":[116248,116249],"is_not":false,"summary":null,"term":"FYPO:0008031"},{"annotations":[116250,116251],"is_not":false,"summary":null,"term":"FYPO:0008046"}]},"doi":"10.1128/EC.00109-13","gene_count":2,"genes_by_uniquename":{"SJAG_02860":null,"SJAG_05242":null},"genotypes_by_uniquename":{"wcs1delta":{"display_name":"wcs1delta","display_uniquename":"wcs1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02860:allele-1","expression":"Null"}]}]},"wcs2delta":{"display_name":"wcs2delta","display_uniquename":"wcs2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_05242:allele-1","expression":"Null"}]}]}},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2013","pubmed_entrez_date":"2013-07-23","pubmed_publication_date":"Sep 2013","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000126":null,"FYPO:0008031":null,"FYPO:0008046":null,"FYPO_EXT:0000001":null,"GO:0009882":null,"GO:0071483":null},"title":"Synchronous activation of cell division by light or temperature stimuli in the dimorphic yeast Schizosaccharomyces japonicus.","uniquename":"PMID:23873862"}


id: PMID:35226668
data:
  {"abstract":"RNA interference (RNAi) is a conserved mechanism of small RNA-mediated genome regulation commonly involved in suppression of transposable elements (TEs) through both post-transcriptional silencing, and transcriptional repression via heterochromatin assembly. The fission yeast Schizosaccharomyces pombe has been extensively utilised as a model for studying RNAi pathways. However, this species is somewhat atypical in that TEs are not major targets of RNAi, and instead small RNAs correspond primarily to non-coding pericentromeric repeat sequences, reflecting a specialised role for the pathway in promoting heterochromatin assembly in these regions. In contrast, in the related fission yeast Schizosaccharomyces japonicus, sequenced small RNAs correspond primarily to TEs. This suggests there may be fundamental differences in the operation of RNAi pathways in these two related species. To investigate these differences, we probed RNAi function in S. japonicus. Unexpectedly, and in contrast to S. pombe, we found that RNAi is essential in this species. Moreover, viability of RNAi mutants can be rescued by mutations implicated in enhancing RNAi-independent heterochromatin propagation. These rescued strains retain heterochromatic marks on TE sequences, but exhibit derepression of TEs at the post-transcriptional level. Our findings indicate that S. japonicus retains the ancestral role of RNAi in facilitating suppression of TEs via both post-transcriptional silencing and heterochromatin assembly, with specifically the heterochromatin pathway being essential for viability, likely due to a function in genome maintenance. The specialised role of RNAi in heterochromatin assembly in S. pombe appears to be a derived state that emerged after the divergence of S. japonicus.","alleles_by_uniquename":{"SJAG_02409:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02409","name":"stc1delta","uniquename":"SJAG_02409:allele-1"},"SJAG_02594:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02594","name":"arb1delta","uniquename":"SJAG_02594:allele-1"},"SJAG_02621:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02621","name":"ago1delta","uniquename":"SJAG_02621:allele-1"},"SJAG_02668:allele-1":{"allele_type":"amino_acid_mutation","description":"R77W","gene_uniquename":"SJAG_02668","name":"mpe1-R77W","uniquename":"SJAG_02668:allele-1"},"SJAG_03118:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03118","name":"leo1delta","uniquename":"SJAG_03118:allele-1"},"SJAG_03118:allele-2":{"allele_type":"nonsense_mutation","description":"aa61->stop","gene_uniquename":"SJAG_03118","name":"frameshift","uniquename":"SJAG_03118:allele-2"},"SJAG_03356:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03356","name":"rdp1delta","uniquename":"SJAG_03356:allele-1"},"SJAG_03689:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03689","name":"dcr1delta","uniquename":"SJAG_03689:allele-1"},"SJAG_03916:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03916","name":"chp1delta","uniquename":"SJAG_03916:allele-1"},"SJAG_04061:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04061","name":"arb2delta","uniquename":"SJAG_04061:allele-1"},"SJAG_04574:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04574","name":"clr4delta","uniquename":"SJAG_04574:allele-1"}},"annotation_curators":[{"annotation_count":31,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-03-07","authors":"Chapman E, Taglini F, Bayne EH","authors_abbrev":"Chapman E et al.","canto_added_date":"2022-03-07 09:13:19","canto_annotation_status":"APPROVED","canto_approved_date":"2022-03-07 12:35:06","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2022-03-07 12:35:06","canto_session_key":"3d6467bf1cb92446","canto_session_submitted_date":"2022-03-07 12:34:56","canto_triage_status":"Curatable","citation":"PLoS Genet 2022 Feb 28;18(2):e1010100","cv_annotations":{"biological_process":[{"annotations":[116338,116339],"is_not":false,"summary":null,"term":"GO:0031507"},{"annotations":[116336,116337],"is_not":false,"summary":null,"term":"GO:0016441"}],"multi_locus_phenotype":[{"annotations":[116332,116334],"is_not":false,"summary":null,"term":"FYPO:0004982"},{"annotations":[116333,116335],"is_not":false,"summary":null,"term":"FYPO:0004573"},{"annotations":[116329],"is_not":false,"summary":null,"term":"FYPO:0002061"},{"annotations":[116330,116331],"is_not":false,"summary":null,"term":"FYPO:0006989"},{"annotations":[116324,116325,116326,116327],"is_not":false,"summary":null,"term":"FYPO:0002058"}],"single_locus_phenotype":[{"annotations":[116318],"is_not":false,"summary":null,"term":"FYPO:0004205"},{"annotations":[116320],"is_not":false,"summary":null,"term":"FYPO:0004982"},{"annotations":[116322],"is_not":false,"summary":null,"term":"FYPO:0000595"},{"annotations":[116319],"is_not":false,"summary":null,"term":"FYPO:0004574"},{"annotations":[116311,116312,116313,116314,116315,116316,116317,116328],"is_not":false,"summary":null,"term":"FYPO:0002061"},{"annotations":[116323],"is_not":false,"summary":null,"term":"FYPO:0006989"},{"annotations":[116321],"is_not":false,"summary":null,"term":"FYPO:0000596"}]},"doi":"10.1371/journal.pgen.1010100","gene_count":10,"genes_by_uniquename":{"SJAG_02409":null,"SJAG_02594":null,"SJAG_02621":null,"SJAG_02668":null,"SJAG_03118":null,"SJAG_03356":null,"SJAG_03689":null,"SJAG_03916":null,"SJAG_04061":null,"SJAG_04574":null},"genetic_interactions":[[{"gene_a_uniquename":"SJAG_03689","gene_b_uniquename":"SJAG_03118","interaction_type":"Phenotypic Suppression"},[{"reference_uniquename":"PMID:35226668","throughput":"low"}]],[{"gene_a_uniquename":"SJAG_03689","gene_b_uniquename":"SJAG_02668","interaction_type":"Phenotypic Suppression"},[{"reference_uniquename":"PMID:35226668","throughput":"low"}]]],"genotypes_by_uniquename":{"ago1delta":{"display_name":"ago1delta","display_uniquename":"ago1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02621:allele-1","expression":"Null"}]}]},"ago1delta__leo1delta":{"display_name":"ago1delta leo1delta","display_uniquename":"ago1delta__leo1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02621:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03118:allele-1","expression":"Null"}]}]},"arb1delta":{"display_name":"arb1delta","display_uniquename":"arb1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02594:allele-1","expression":"Null"}]}]},"arb2delta":{"display_name":"arb2delta","display_uniquename":"arb2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04061:allele-1","expression":"Null"}]}]},"chp1delta":{"display_name":"chp1delta","display_uniquename":"chp1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03916:allele-1","expression":"Null"}]}]},"clr4delta":{"display_name":"clr4delta","display_uniquename":"clr4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04574:allele-1","expression":"Null"}]}]},"clr4delta__leo1delta":{"display_name":"clr4delta leo1delta","display_uniquename":"clr4delta__leo1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04574:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03118:allele-1","expression":"Null"}]}]},"dcr1delta":{"display_name":"dcr1delta","display_uniquename":"dcr1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03689:allele-1","expression":"Null"}]}]},"dcr1delta__frameshift-aa61->stop-nonsense_mutation-expression-not_assayed_or_wild_type":{"display_name":"dcr1delta frameshift(aa61->stop)","display_uniquename":"dcr1delta__frameshift-aa61->stop-nonsense_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03689:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03118:allele-2","expression":"Not assayed or wild type"}]}]},"dcr1delta__leo1delta":{"display_name":"dcr1delta leo1delta","display_uniquename":"dcr1delta__leo1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03689:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03118:allele-1","expression":"Null"}]}]},"dcr1delta__mpe1-R77W-R77W-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"dcr1delta mpe1-R77W(aa)","display_uniquename":"dcr1delta__mpe1-R77W-R77W-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03689:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_02668:allele-1","expression":"Not assayed or wild type"}]}]},"rdp1delta":{"display_name":"rdp1delta","display_uniquename":"rdp1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03356:allele-1","expression":"Null"}]}]},"stc1delta":{"display_name":"stc1delta","display_uniquename":"stc1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02409:allele-1","expression":"Null"}]}]}},"ltp_gene_count":10,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-02-28","pubmed_publication_date":"28 Feb 2022","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000162":null,"FYPO:0000595":null,"FYPO:0000596":null,"FYPO:0002058":null,"FYPO:0002061":null,"FYPO:0004205":null,"FYPO:0004573":null,"FYPO:0004574":null,"FYPO:0004982":null,"FYPO:0006989":null,"FYPO_EXT:0000001":null,"GO:0016441":null,"GO:0031507":null},"title":"Separable roles for RNAi in regulation of transposable elements and viability in the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:35226668"}


id: PMID:35359202
data:
  {"abstract":"The fission yeast genus Schizosaccharomyces contains important model organisms for biological research. In particular, S. pombe is a widely used model eukaryote. So far little is known about the natural and artificial habitats of species in this genus. Finding out where S. pombe and other fission yeast species occur and how they live in their habitats can promote better understanding of their biology. Here we investigate in which substrates S. pombe, S. octosporus, S. osmophilus and S. japonicus are present. To this end about 2100 samples consisting of soil, tree sap fluxes, fresh fruit, dried fruit, honey, cacao beans, molasses and other substrates were analyzed. Effective isolation methods that allow efficient isolation of the above mentioned species were developed. Based on the frequency of isolating different fission yeast species in various substrates and on extensive literature survey, conclusions are drawn on their ecology. The results suggest that the primary habitat of S. pombe and S. octosporus is honeybee honey. Both species were also frequently detected on certain dried fruit like raisins, mango or pineapple to which they could be brought by the honey bees during ripening or during drying. While S. pombe was regularly isolated from grape mash and from fermented raw cacao beans S. octosporus was never isolated from fresh fruit. The main habitat of S. osmophilus seems to be solitary bee beebread. It was rarely isolated from raisins. S. japonicus was mainly found in forest substrates although it occurs on fruit and in fruit fermentations, too.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Brysch-Herzberg M, Jia GS, Seidel M, Assali I, Du LL","authors_abbrev":"Brysch-Herzberg M et al.","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Phylogeny and evolutionary studies","citation":"Antonie Van Leeuwenhoek 2022 May;115(5):661-695","cv_annotations":{},"doi":"10.1007/s10482-022-01720-0","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2022","pubmed_entrez_date":"2022-04-01","pubmed_publication_date":"May 2022","terms_by_termid":{},"title":"Insights into the ecology of Schizosaccharomyces species in natural and artificial habitats.","uniquename":"PMID:35359202"}


id: PMID:9720056
data:
  {"abstract":"The cells of Schizosaccharomyces japonicus var. versatilis responded to the presence of cytochalasin D (CD), an inhibitor of actin polymerization, by the disappearance of contractile actin rings (ARs) that had already formed and by inhibition of new ring formation. Actin cables disappeared. Actin patches remained preserved and became co-localized with regions of actual cell wall formation (at cell poles and at the site of septum development). Removal of the AR arrested formation of the primary septum and led to the production of aberrant septum protrusions in that region. Nuclear division was accomplished in the presence of CD but new ARs were not produced. The wall (septum) material was deposited in the form of a wide band at the inner surface of the lateral cell wall in the cell centre. This layer showed a thin fibrillar structure. The removal of CD resulted in rapid formation of new ARs in the equatorial region of the cells. This implies that the signal for AR localization was not abolished either by CD effects or by removal of an AR already formed. Some of the newly developed ARs showed atypical localization and orientation. In addition, redundant, subcortically situated actin bundles were produced. The removal of CD was quickly followed by the development of primary septa co-localized with ARs. Wall protrusions occurred co-localized with the redundant actin bundles. If these were completed in a circle, redundant septa developed. The AR is a mechanism which, in time and space, triggers cytokinesis by building a septum sequentially dependent on the AR. Aberrant septa were not capable of separating daughter cells. However, non-separated daughter cells subsequently gave rise to normal cells.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Gabriel M, Horký D, Svoboda A, Kopecká M","authors_abbrev":"Gabriel 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":"Microbiology (Reading) 1998 Aug;144 ( Pt 8):2331-2344","cv_annotations":{},"doi":"10.1099/00221287-144-8-2331","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1998","pubmed_entrez_date":"1998-08-28","pubmed_publication_date":"Aug 1998","terms_by_termid":{},"title":"Cytochalasin D interferes with contractile actin ring and septum formation in Schizosaccharomyces japonicus var. versatilis.","uniquename":"PMID:9720056"}


id: PMID:28655757
data:
  {"abstract":"Cytokinesis in many eukaryotes involves a tension-generating actomyosin-based contractile ring. Many components of actomyosin rings turn over during contraction, although the significance of this turnover has remained enigmatic. Here, using  Schizosaccharomyces japonicus , we investigate the role of turnover of actin and myosin II in its contraction. Actomyosin ring components self-organize into ∼1-µm-spaced clusters instead of undergoing full-ring contraction in the absence of continuous actin polymerization. This effect is reversed when actin filaments are stabilized. We tested the idea that the function of turnover is to ensure actin filament homeostasis in a synthetic system, in which we abolished turnover by fixing rings in cell ghosts with formaldehyde. We found that these rings contracted fully upon exogenous addition of a vertebrate myosin. We conclude that actin turnover is required to maintain actin filament homeostasis during ring contraction and that the requirement for turnover can be bypassed if homeostasis is achieved artificially.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":5,"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":"Chew TG, Huang J, Palani S, Sommese R, Kamnev A, Hatano T, Gu Y, Oliferenko S, Sivaramakrishnan S, Balasubramanian MK","authors_abbrev":"Chew TG et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-07-09 13:45:34","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-07-09 13:45:34","canto_session_key":"5ead7a365a97d8ab","canto_session_submitted_date":"2021-07-09 13:45:28","canto_triage_status":"Curatable","citation":"J Cell Biol 2017 09 04;216(9):2657-2667","cv_annotations":{"cellular_component":[{"annotations":[116098,116099,116100,116101,116102],"is_not":false,"summary":null,"term":"GO:0005826"}]},"doi":"10.1083/jcb.201701104","gene_count":5,"genes_by_uniquename":{"SJAG_01665":null,"SJAG_02431":null,"SJAG_03596":null,"SJAG_03703":null,"SJAG_04498":null},"genotypes_by_uniquename":{},"ltp_gene_count":5,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2017-06-29","pubmed_publication_date":"04 09 2017","terms_by_termid":{"GO:0005826":null},"title":"Actin turnover maintains actin filament homeostasis during cytokinetic ring contraction.","uniquename":"PMID:28655757"}


id: PMID:5315726
data:
  {"abstract":"","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bulder CJ","authors_abbrev":"Bulder CJ","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Antonie Van Leeuwenhoek 1971;37(3):353-8","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1971","pubmed_entrez_date":"1971-01-01","pubmed_publication_date":"1971","terms_by_termid":{},"title":"Anaerobic growth, ergosterol content and sensitivity to a polyene antibiotic, of the yeast Schizosaccharomyces japonicus.","uniquename":"PMID:5315726"}


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: PMID:34353908
data:
  {"abstract":"Biosynthesis of sterols, which are key constituents of canonical eukaryotic membranes, requires molecular oxygen. Anaerobic protists and deep-branching anaerobic fungi are the only eukaryotes in which a mechanism for sterol-independent growth has been elucidated. In these organisms, tetrahymanol, formed through oxygen-independent cyclization of squalene by a squalene-tetrahymanol cyclase, acts as a sterol surrogate. This study confirms an early report [C. J. E. A. Bulder,  Antonie Van Leeuwenhoek , 37, 353-358 (1971)] that  Schizosaccharomyces japonicus  is exceptional among yeasts in growing anaerobically on synthetic media lacking sterols and unsaturated fatty acids. Mass spectrometry of lipid fractions of anaerobically grown  Sch. japonicus  showed the presence of hopanoids, a class of cyclic triterpenoids not previously detected in yeasts, including hop-22(29)-ene, hop-17(21)-ene, hop-21(22)-ene, and hopan-22-ol. A putative gene in  Sch. japonicus  showed high similarity to bacterial squalene-hopene cyclase (SHC) genes and in particular to those of  Acetobacter  species. No orthologs of the putative  Sch. japonicus  SHC were found in other yeast species. Expression of the  Sch. japonicus  SHC gene ( Sjshc1 ) in  Saccharomyces cerevisiae  enabled hopanoid synthesis and stimulated anaerobic growth in sterol-free media, thus indicating that one or more of the hopanoids produced by SjShc1 could at least partially replace sterols. Use of hopanoids as sterol surrogates represents a previously unknown adaptation of eukaryotic cells to anaerobic growth. The fast anaerobic growth of  Sch. japonicus  in sterol-free media is an interesting trait for developing robust fungal cell factories for application in anaerobic industrial processes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bouwknegt J, Wiersma SJ, Ortiz-Merino RA, Doornenbal ESR, Buitenhuis P, Giera M, Müller C, Pronk JT","authors_abbrev":"Bouwknegt J et al.","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Proc Natl Acad Sci U S A 2021 Aug 10;118(32)","cv_annotations":{},"doi":"10.1073/pnas.2105225118","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":"2021-08-06","pubmed_publication_date":"10 Aug 2021","terms_by_termid":{},"title":"A squalene-hopene cyclase in  Schizosaccharomyces japonicus  represents a eukaryotic adaptation to sterol-limited anaerobic environments.","uniquename":"PMID:34353908"}


id: GO_REF:0000033
data:
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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 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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_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":[116193],"is_not":false,"summary":null,"term":"GO:0005730"}],"multi_locus_phenotype":[{"annotations":[116207,116208,116209,116211],"is_not":false,"summary":null,"term":"FYPO:0000674"}],"single_locus_phenotype":[{"annotations":[116194,116195,116196,116210],"is_not":false,"summary":null,"term":"FYPO:0000080"},{"annotations":[116203,116204,116205],"is_not":false,"summary":null,"term":"FYPO:0000618"},{"annotations":[116212,116213,116214],"is_not":false,"summary":null,"term":"FYPO:0001327"},{"annotations":[116200,116201,116202],"is_not":false,"summary":null,"term":"FYPO:0001387"},{"annotations":[116197,116198,116199],"is_not":false,"summary":null,"term":"FYPO:0000324"},{"annotations":[116206],"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 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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","references_by_uniquename":{"PMID:23786411":null},"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:32140970
data:
  {"abstract":"In eukaryotes, chromosome ends (telomeres) are tethered to the inner nuclear membrane. During the early stages of meiosis, telomeres move along the nuclear membrane and gather near the spindle-pole body, resulting in a bouquet-like arrangement of chromosomes. This chromosomal configuration appears to be widely conserved among eukaryotes, and is assumed to play an important role in the normal progression of meiosis, by mediating the proper pairing of homologous chromosomes. In fission yeast, the Bqt1-Bqt2 protein complex plays a key role in tethering the telomere to the inner nuclear membrane. However, the structural details of the complex required to clarify how telomeres are gathered near the spindle-pole body remain enigmatic. Previously, we devised a preparation procedure for the Schizosaccharomyces japonicus Bqt1-Bqt2 complex, in which a SUMO tag was fused to the N-terminus of the Bqt1 protein. This allowed us to purify the Bqt1-Bqt2 complex from the soluble fraction. In the present study, we found that a maltose-binding protein homolog, Athe_0614, served as a better fusion partner than the SUMO protein, resulting in the marked increase in the solubility of the Bqt1-Bqt2 complex. The Athe_0614 fusion partner may open up new avenues for X-ray crystallographic analyses of the structure of the Bqt1-Bqt2 complex.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Yuzurihara H, Aizawa Y, Saotome M, Ichikawa Y, Yokoyama H, Chikashige Y, Haraguchi T, Hiraoka Y, Kurumizaka H, Kagawa W","authors_abbrev":"Yuzurihara H et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Protein J 2020 04;39(2):174-181","cv_annotations":{},"doi":"10.1007/s10930-020-09887-z","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":"2020-03-07","pubmed_publication_date":"04 2020","terms_by_termid":{},"title":"Improved Methods for Preparing the Telomere Tethering Complex Bqt1-Bqt2 for Structural Studies.","uniquename":"PMID:32140970"}


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_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":[116236],"is_not":false,"summary":null,"term":"GO:0030995"}],"single_locus_phenotype":[{"annotations":[116235],"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:8590481
data:
  {"abstract":"Fission yeasts form a small but heterogeneous group of ascomycetes and it is still unclear whether they should be subdivided into three genera (Schizosaccharomyces, Octosporomyces, Hasegawaea) or remain a single genus (Schizosaccharomyces). In order to decide whether a new genus Hasegawaea should be established for the species Schizosaccharomyces japonicus and Schizosaccharomyces versatilis, we have characterized the entire rDNA cluster in Schizosaccharomyces japonicus var. versatilis and compared it with the homologous region from Schizosaccharomyces pombe and with complete rRNA gene sequences from other yeast genera. From a phage genomic library a recombinant lambda phage containing the entire rDNA repeat unit was isolated. In this paper we report the primary sequence of the 18s, 5.8s and 25s rRNA coding regions. The S. japonicus var. versatilis rRNA genes are 1823 (18s), 158 (5.8s) and 3422 (25s) nucleotides long. The two sequences of the larger rRNA genes exhibit 95.7% (18s) and 93% (25s) similarity with the homologous genes from S. pombe. The differences between the rRNA genes of S. japonicus and S. pombe, however, are much smaller than the intrageneric differences within the rDNA sequences of other yeast genera. Therefore, subdivision of fission yeasts into the genera Schizosaccharomyces and Hasegawaea does not to seem to be justified.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Naehring J, Kiefer S, Wolf K","authors_abbrev":"Naehring J et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Curr Genet 1995 Sep;28(4):353-9","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":"1995-09-01","pubmed_publication_date":"Sep 1995","terms_by_termid":{},"title":"Nucleotide sequence of the Schizosaccharomyces japonicus var. versatilis ribosomal RNA gene cluster and its phylogenetic implications.","uniquename":"PMID:8590481"}


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: GO_REF:0000108
data:
  {"alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"canto_curator_role":"JaponicusDB","cv_annotations":{"biological_process":[{"annotations":[65608],"is_not":false,"summary":null,"term":"GO:0071266"},{"annotations":[61496],"is_not":false,"summary":null,"term":"GO:0042886"},{"annotations":[56809,57293,57751,58937,63557,64049,64177,66808],"is_not":false,"summary":null,"term":"GO:0106074"},{"annotations":[68746],"is_not":false,"summary":null,"term":"GO:0140331"},{"annotations":[66396],"is_not":false,"summary":null,"term":"GO:0009785"},{"annotations":[63911],"is_not":false,"summary":null,"term":"GO:0070574"},{"annotations":[60868,64748],"is_not":false,"summary":null,"term":"GO:0034219"},{"annotations":[58265,69202,69430],"is_not":false,"summary":null,"term":"GO:1905039"},{"annotations":[57232,65394],"is_not":false,"summary":null,"term":"GO:0098869"},{"annotations":[57761,57990,58336,59186,61019,61837,61906,62094,64238,65443,65668,66128,66213,66297,67233,68416,68498,69586],"is_not":false,"summary":null,"term":"GO:0006338"},{"annotations":[67937],"is_not":false,"summary":null,"term":"GO:0009224"},{"annotations":[68613],"is_not":false,"summary":null,"term":"GO:0006761"},{"annotations":[62750,63143],"is_not":false,"summary":null,"term":"GO:0071897"},{"annotations":[61630],"is_not":false,"summary":null,"term":"GO:0140479"},{"annotations":[64329],"is_not":false,"summary":null,"term":"GO:0046710"},{"annotations":[63372],"is_not":false,"summary":null,"term":"GO:0006868"},{"annotations":[59226],"is_not":false,"summary":null,"term":"GO:0006177"},{"annotations":[63756],"is_not":false,"summary":null,"term":"GO:1903790"},{"annotations":[64495],"is_not":false,"summary":null,"term":"GO:0051170"},{"annotations":[56959],"is_not":false,"summary":null,"term":"GO:0120009"},{"annotations":[63371],"is_not":false,"summary":null,"term":"GO:1903826"},{"annotations":[61325],"is_not":false,"summary":null,"term":"GO:0097052"},{"annotations":[65403],"is_not":false,"summary":null,"term":"GO:0015825"},{"annotations":[59137,60764,62465],"is_not":false,"summary":null,"term":"GO:0019249"},{"annotations":[57343,61103,69588],"is_not":false,"summary":null,"term":"GO:0098734"},{"annotations":[56752],"is_not":false,"summary":null,"term":"GO:1903830"},{"annotations":[64549],"is_not":false,"summary":null,"term":"GO:1901553"},{"annotations":[57284],"is_not":false,"summary":null,"term":"GO:0000165"},{"annotations":[60266,69093],"is_not":false,"summary":null,"term":"GO:0061025"},{"annotations":[59138,60765],"is_not":false,"summary":null,"term":"GO:0061727"},{"annotations":[61692,65723],"is_not":false,"summary":null,"term":"GO:0098656"},{"annotations":[58296],"is_not":false,"summary":null,"term":"GO:0098655"},{"annotations":[65404],"is_not":false,"summary":null,"term":"GO:0034220"},{"annotations":[63873],"is_not":false,"summary":null,"term":"GO:0035672"},{"annotations":[59337],"is_not":false,"summary":null,"term":"GO:0035435"},{"annotations":[61469,61659,63231],"is_not":false,"summary":null,"term":"GO:0036092"},{"annotations":[61389,65490,67227,67432,68383,68941],"is_not":false,"summary":null,"term":"GO:1901800"},{"annotations":[61982,62982,65367,66481],"is_not":false,"summary":null,"term":"GO:0045944"},{"annotations":[57426,67278],"is_not":false,"summary":null,"term":"GO:0071805"},{"annotations":[58599],"is_not":false,"summary":null,"term":"GO:0006457"},{"annotations":[56898,60938,66688],"is_not":false,"summary":null,"term":"GO:0071806"},{"annotations":[67428],"is_not":false,"summary":null,"term":"GO:0015986"},{"annotations":[58168,59167,59431,59532,60796,60869,61148,61474,61731,62075,63416,63906,63913,64749,67966,68471],"is_not":false,"summary":null,"term":"GO:1902600"},{"annotations":[57179,66407,68641],"is_not":false,"summary":null,"term":"GO:0006357"},{"annotations":[58087],"is_not":false,"summary":null,"term":"GO:0019430"},{"annotations":[59970],"is_not":false,"summary":null,"term":"GO:0106005"},{"annotations":[60858],"is_not":false,"summary":null,"term":"GO:0034337"},{"annotations":[65034,67219],"is_not":false,"summary":null,"term":"GO:0051123"},{"annotations":[57876,58209,59331,60301,62397,63341,63966,64082,68111],"is_not":false,"summary":null,"term":"GO:0001172"},{"annotations":[64333],"is_not":false,"summary":null,"term":"GO:0031167"},{"annotations":[61149,67279],"is_not":false,"summary":null,"term":"GO:0035725"},{"annotations":[57729],"is_not":false,"summary":null,"term":"GO:1903711"},{"annotations":[61678],"is_not":false,"summary":null,"term":"GO:1902981"},{"annotations":[61827],"is_not":false,"summary":null,"term":"GO:0006415"},{"annotations":[57012],"is_not":false,"summary":null,"term":"GO:0055085"},{"annotations":[63370],"is_not":false,"summary":null,"term":"GO:0015828"},{"annotations":[66388],"is_not":false,"summary":null,"term":"GO:0015790"}],"cellular_component":[{"annotations":[61980],"is_not":false,"summary":null,"term":"GO:0005938"},{"annotations":[58579,58656,59434,59704,59868,6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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:26343758
data:
  {"abstract":"CENP-A is a centromere-specific histone H3 variant that is required for kinetochore assembly and accurate chromosome segregation. For it to function properly, CENP-A must be specifically localized to centromeres. In fission yeast, Scm3sp and the Mis18 complex, composed of Mis16, Eic1, and Mis18, function as a CENP-A(Cnp1)-specific chaperone and a recruiting factor, respectively, and together ensure accurate delivery of CENP-A(Cnp1) to centromeres. Although how Scm3sp specifically recognizes CENP-A(Cnp1) has been revealed recently, the recruiting mechanism of CENP-A(Cnp1) via the Mis18 complex remains unknown. In this study, we have determined crystal structures of Schizosaccharomyces japonicus Mis16 alone and in complex with the helix 1 of histone H4 (H4α1). Crystal structures followed by mutant analysis and affinity pull-downs have revealed that Mis16 recognizes both H4α1 and Scm3sp independently within the CENP-A(Cnp1)/H4:Scm3sp complex. This observation suggests that Mis16 gains CENP-A(Cnp1) specificity by recognizing both Scm3sp and histone H4. Our studies provide insights into the molecular mechanisms underlying specific recruitment of CENP-A(Cnp1)/H4:Scm3sp into centromeres. ","alleles_by_uniquename":{},"annotation_curators":[{"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":"2021-05-13","authors":"An S, Kim H, Cho US","authors_abbrev":"An S et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-05-13 14:11:41","canto_curator_name":"Val Wood","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-05-13 14:11:41","canto_session_key":"fb189c5ef542852c","canto_session_submitted_date":"2021-05-12 16:00:22","canto_triage_status":"Curatable","citation":"J Mol Biol 2015 Oct 09;427(20):3230-3240","cv_annotations":{"molecular_function":[{"annotations":[116237,116238,116239,116240],"is_not":false,"summary":null,"term":"GO:0042393"}]},"doi":"10.1016/j.jmb.2015.08.022","gene_count":4,"genes_by_uniquename":{"SJAG_00303":null,"SJAG_02513":null,"SJAG_03542":null,"SJAG_03867":null},"genotypes_by_uniquename":{},"ltp_gene_count":3,"ortholog_annotations":[],"paralog_annotations":[],"pdb_entries":[{"entry_authors":"An S,Kim H,Cho U-S","entry_authors_abbrev":"An S et al.","experimental_method":"X-ray","gene_chains":[{"chain":"B","gene_uniquename":"SJAG_03542","position":"1-103"},{"chain":"A","gene_uniquename":"SJAG_03867","position":"1-427"}],"pdb_id":"4xyi","reference_uniquename":"PMID:26343758","resolution":"3.0","title":"Mis16 with H4 peptide"},{"entry_authors":"An S,Kim H,Cho U-S","entry_authors_abbrev":"An S et al.","experimental_method":"X-ray","gene_chains":[{"chain":"A","gene_uniquename":"SJAG_03867","position":"1-427"}],"pdb_id":"4xyh","reference_uniquename":"PMID:26343758","resolution":"2.3","title":"Wild-type full length Mis16 in Schizosaccharomyces japonicus"}],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-09-08","pubmed_publication_date":"09 Oct 2015","terms_by_termid":{"GO:0042393":null},"title":"Mis16 Independently Recognizes Histone H4 and the CENP-ACnp1-Specific Chaperone Scm3sp.","uniquename":"PMID:26343758"}


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_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":[115903],"is_not":false,"summary":null,"term":"GO:0101024"}],"cellular_component":[{"annotations":[115892],"is_not":false,"summary":null,"term":"GO:0000785"},{"annotations":[115896,115897],"is_not":false,"summary":null,"term":"GO:0005783"},{"annotations":[115898],"is_not":false,"summary":null,"term":"GO:0098826"},{"annotations":[115891],"is_not":false,"summary":null,"term":"GO:0000776"},{"annotations":[115888],"is_not":false,"summary":null,"term":"GO:0005874"},{"annotations":[115893,115894,115895,115899],"is_not":false,"summary":null,"term":"GO:0005643"},{"annotations":[115889,115890],"is_not":false,"summary":null,"term":"GO:0005730"}],"single_locus_phenotype":[{"annotations":[115901],"is_not":false,"summary":null,"term":"FYPO:0003779"},{"annotations":[115900],"is_not":false,"summary":null,"term":"FYPO:0004318"},{"annotations":[115902],"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:10379403
data:
  {"abstract":"The order Schizosaccharomycetales contains a dimorphic and two yeast species. Sch. japonicus can form both yeast cells and mycelium, depending on the substrate and the culturing conditions. Sch. pombe is a strictly unicellular organism, but it can be forced to form mycelial cell chains by inactivating members of the sep gene family. The mutations in most of the sep genes confer pleitropic phenotypes indicating functional involvement in MAP-kinase-mediated signalling pathways. Two of them were found to encode transcription factor homologues of other eukaryotes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Sipiczki M, Grallert A, Miklós I, Zilahi E, Bozsik A, Szilágyi Z","authors_abbrev":"Sipiczki M et al.","canto_added_date":"2023-05-04 00:40:04","canto_annotation_status":"SESSION_CREATED","canto_curator_role":"JaponicusDB","canto_session_key":"eb5db4e2ead0caf4","canto_triage_status":"Cell composition or WT feature","citation":"Acta Microbiol Immunol Hung 1999;46(2-3):297-302","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1999","pubmed_entrez_date":"1999-06-24","pubmed_publication_date":"1999","terms_by_termid":{},"title":"Genetics, physiology and cytology of yeast-mycelial dimorphism in fission yeasts.","uniquename":"PMID:10379403"}


id: PMID:26104357
data:
  {"abstract":"Cells of the highly diverged Schizosaccharomyces (S.) pombe and S. japonicus fission yeasts exist in one of two sex/mating types, called P (for plus) or M (for minus), specified by which allele, M or P, resides at mat1. The fission yeasts have evolved an elegant mechanism for switching P or M information at mat1 by a programmed DNA recombination event with a copy of one of the two silent mating-type genes residing nearby in the genome. The switching process is highly cell-cycle and generation dependent such that only one of four grandchildren of a cell switches mating type. Extensive studies of fission yeast established the natural DNA strand chirality at the mat1 locus as the primary basis of asymmetric cell division. The asymmetry results from a unique site- and strand-specific epigenetic \"imprint\" at mat1 installed in one of the two chromatids during DNA replication. The imprint is inherited by one daughter cell, maintained for one cell cycle, and is then used for initiating recombination during mat1 replication in the following cell cycle. This mechanism of cell-type switching is considered to be unique to these two organisms, but determining the operation of such a mechanism in other organisms has not been possible for technical reasons. This review summarizes recent exciting developments in the understanding of mating-type switching in fission yeasts and extends these observations to suggest how such a DNA strand-based epigenetic mechanism of cellular differentiation could also operate in diploid organisms. ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Klar AJS, Ishikawa K, Moore S","authors_abbrev":"Klar AJS et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Microbiol Spectr 2014 Oct;2(5)","cv_annotations":{},"doi":"10.1128/microbiolspec.MDNA3-0003-2014","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":"2015-06-25","pubmed_publication_date":"Oct 2014","terms_by_termid":{},"title":"A Unique DNA Recombination Mechanism of the Mating/Cell-type Switching of Fission Yeasts: a Review.","uniquename":"PMID:26104357"}


id: PMID:23150598
data:
  {"abstract":"A key question in developmental biology addresses the mechanism of asymmetric cell division. Asymmetry is crucial for generating cellular diversity required for development in multicellular organisms. As one of the potential mechanisms, chromosomally borne epigenetic difference between sister cells that changes mating/cell type has been demonstrated only in the Schizosaccharomyces pombe fission yeast. For technical reasons, it is nearly impossible to determine the existence of such a mechanism operating during embryonic development of multicellular organisms. Our work addresses whether such an epigenetic mechanism causes asymmetric cell division in the recently sequenced fission yeast, S. japonicus (with 36% GC content), which is highly diverged from the well-studied S. pombe species (with 44% GC content). We find that the genomic location and DNA sequences of the mating-type loci of S. japonicus differ vastly from those of the S. pombe species. Remarkably however, similar to S. pombe, the S. japonicus cells switch cell/mating type after undergoing two consecutive cycles of asymmetric cell divisions: only one among four \"granddaughter\" cells switches. The DNA-strand-specific epigenetic imprint at the mating-type locus1 initiates the recombination event, which is required for cellular differentiation. Therefore the S. pombe and S. japonicus mating systems provide the first two examples in which the intrinsic chirality of double helical structure of DNA forms the primary determinant of asymmetric cell division. Our results show that this unique strand-specific imprinting/segregation epigenetic mechanism for asymmetric cell division is evolutionary conserved. Motivated by these findings, we speculate that DNA-strand-specific epigenetic mechanisms might have evolved to dictate asymmetric cell division in diploid, higher eukaryotes as well.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Yu C, Bonaduce MJ, Klar AJ","authors_abbrev":"Yu C et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Genetics 2013 Jan;193(1):85-94","cv_annotations":{},"doi":"10.1534/genetics.112.146233","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":"2012-11-15","pubmed_publication_date":"Jan 2013","terms_by_termid":{},"title":"Defining the epigenetic mechanism of asymmetric cell division of Schizosaccharomyces japonicus yeast.","uniquename":"PMID:23150598"}


id: PMID:30664646
data:
  {"abstract":"Cells of a specific cell type may divide within a certain size range. Yet, functionally optimal cellular organization is typically maintained across different cell sizes, a phenomenon known as scaling. The mechanisms underlying scaling and its physiological significance remain elusive. Here we approach this problem by interfering with scaling in the rod-shaped fission yeast Schizosaccharomyces japonicus that relies on cellular geometry cues to position the division site. We show that S. japonicus uses the Cdc42 polarity module to adjust its geometry to changes in the cell size. When scaling is prevented resulting in abnormal cellular length-to-width aspect ratio, cells exhibit severe division site placement defects. We further show that despite the generally accepted view, a similar scaling phenomenon can occur in the sister species, Schizosaccharomyces pombe. Our results demonstrate that scaling is required for normal cell function and delineate possible rules for cellular geometry maintenance in populations of proliferating cells.","alleles_by_uniquename":{"SJAG_00028:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00028","name":"rga6delta","uniquename":"SJAG_00028:allele-1"},"SJAG_00514:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00514","name":"scd1delta","uniquename":"SJAG_00514:allele-1"},"SJAG_03048:allele-1":{"allele_type":"amino_acid_mutation","description":"G146D","gene_uniquename":"SJAG_03048","name":"cdc2-1w","uniquename":"SJAG_03048:allele-1"},"SJAG_03581:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03581","name":"gef1delta","uniquename":"SJAG_03581:allele-1"},"SJAG_04280:allele-2":{"allele_type":"amino_acid_mutation","description":"T582G","gene_uniquename":"SJAG_04280","name":"wee1-as8","uniquename":"SJAG_04280:allele-2"},"SJAG_04280:allele-3":{"allele_type":"amino_acid_mutation","description":"G788E","gene_uniquename":"SJAG_04280","name":"wee1-G788E","uniquename":"SJAG_04280:allele-3"},"SJAG_04522:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04522","name":"rga4delta","uniquename":"SJAG_04522: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":22,"community_curator":true,"file_name":null,"file_type":null,"name":"Ying Gu","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-02","authors":"Gu Y, Oliferenko S","authors_abbrev":"Gu Y et al.","canto_added_date":"2021-05-10 02:37:31","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-01 07:53:28","canto_curator_name":"Ying Gu","canto_curator_role":"community","canto_first_approved_date":"2021-07-02 12:32:27","canto_session_key":"0922e2a5229110bd","canto_session_submitted_date":"2021-06-30 22:18:13","canto_triage_status":"Curatable","citation":"Nat Commun 2019 01 21;10(1):268","cv_annotations":{"biological_process":[{"annotations":[115990],"is_not":false,"summary":null,"term":"GO:0061171"},{"annotations":[115991,115992],"is_not":false,"summary":null,"term":"GO:0008360"}],"multi_locus_phenotype":[{"annotations":[115978,115983],"is_not":false,"summary":null,"term":"FYPO:0007783"},{"annotations":[115989],"is_not":false,"summary":null,"term":"FYPO:0004105"},{"annotations":[115980],"is_not":false,"summary":null,"term":"FYPO:0001369"},{"annotations":[115982],"is_not":false,"summary":null,"term":"FYPO:0004293"}],"single_locus_phenotype":[{"annotations":[115984],"is_not":false,"summary":null,"term":"FYPO:0000198"},{"annotations":[115985,115986,115988],"is_not":false,"summary":null,"term":"FYPO:0005503"},{"annotations":[115979],"is_not":false,"summary":null,"term":"FYPO:0007783"},{"annotations":[115973],"is_not":false,"summary":null,"term":"FYPO:0004105"},{"annotations":[115987],"is_not":false,"summary":null,"term":"FYPO:0002870"},{"annotations":[115981],"is_not":false,"summary":null,"term":"FYPO:0001369"},{"annotations":[115974],"is_not":false,"summary":null,"term":"FYPO:0001234"},{"annotations":[115968,115969,115972],"is_not":false,"summary":null,"term":"FYPO:0000648"},{"annotations":[115970,115971,115977],"is_not":false,"summary":null,"term":"FYPO:0001877"},{"annotations":[115975,115976],"is_not":false,"summary":null,"term":"FYPO:0006616"}]},"doi":"10.1038/s41467-018-08218-2","gene_count":8,"genes_by_uniquename":{"SJAG_00028":null,"SJAG_00030":null,"SJAG_00514":null,"SJAG_01794":null,"SJAG_03048":null,"SJAG_03581":null,"SJAG_04280":null,"SJAG_04522":null},"genotypes_by_uniquename":{"cdc2-1w-G146D-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"cdc2-1w(G146D aa)","display_uniquename":"cdc2-1w-G146D-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03048:allele-1","expression":"Not assayed or wild type"}]}]},"gef1delta":{"display_name":"gef1delta","display_uniquename":"gef1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03581:allele-1","expression":"Null"}]}]},"rga4delta":{"display_name":"rga4delta","display_uniquename":"rga4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04522:allele-1","expression":"Null"}]}]},"rga4delta__rga6delta":{"display_name":"rga4delta rga6delta","display_uniquename":"rga4delta__rga6delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04522:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_00028:allele-1","expression":"Null"}]}]},"rga4delta__wee1-G788E-G788E-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"rga4delta wee1-G788E(aa)","display_uniquename":"rga4delta__wee1-G788E-G788E-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04522:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_04280:allele-3","expression":"Not assayed or wild type"}]}]},"rga4delta__wee1-as8-T582G-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"rga4delta wee1-as8(T582G aa)","display_uniquename":"rga4delta__wee1-as8-T582G-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04522:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_04280:allele-2","expression":"Not assayed or wild type"}]}]},"rga6delta":{"display_name":"rga6delta","display_uniquename":"rga6delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00028:allele-1","expression":"Null"}]}]},"rga6delta__wee1-as8-T582G-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"rga6delta wee1-as8(T582G aa)","display_uniquename":"rga6delta__wee1-as8-T582G-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00028:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_04280:allele-2","expression":"Not assayed or wild type"}]}]},"scd1delta":{"display_name":"scd1delta","display_uniquename":"scd1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00514:allele-1","expression":"Null"}]}]},"wee1-G788E-G788E-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"wee1-G788E(aa)","display_uniquename":"wee1-G788E-G788E-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04280:allele-3","expression":"Not assayed or wild type"}]}]},"wee1-as8-T582G-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"wee1-as8(T582G aa)","display_uniquename":"wee1-as8-T582G-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04280:allele-2","expression":"Not assayed or wild type"}]}]}},"ltp_gene_count":6,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2019","pubmed_entrez_date":"2019-01-22","pubmed_publication_date":"21 01 2019","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000005":null,"FYECO:0000006":null,"FYECO:0000103":null,"FYECO:0000126":null,"FYECO:0000137":null,"FYECO:0000338":null,"FYPO:0000198":null,"FYPO:0000648":null,"FYPO:0001234":null,"FYPO:0001369":null,"FYPO:0001877":null,"FYPO:0002870":null,"FYPO:0004105":null,"FYPO:0004293":null,"FYPO:0005503":null,"FYPO:0006616":null,"FYPO:0007783":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"GO:0008360":null,"GO:0061171":null},"title":"Cellular geometry scaling ensures robust division site positioning.","uniquename":"PMID:30664646"}


id: PMID:1093
data:
  {"abstract":"(11 Cell extracts and extracellular culture fluids of species of the yeast genus Schizosaccharomyces exhibited exo-beta-(1 leads to 3)- and exo-beta-(1 leads to 6)-glucanase (EC 3.2.1.-) activities. (2) Using a combination of Sephadex G-100 and DEAE-cellulose chromatography, the exo-beta-(1 leads to 3)-glucanases from the cell extracts and culture fluid of Schizosaccharomyces japonicus var. versatilis were purified extensively. The enzymes from either location exhibited similar purification and other properties. (3) The purified enzymes hydrolysed the beta-(1 leads to 6)-glucosidic linkage in addition to the beta-(1 leads to 3) linkage. Heat denaturation, inhibition and electrophoretic studies indicated that both hydrolytic activities were properties of a single protein. Laminarin and pustulan hydrolysis followed Michaelis-Menten kinetics. The Km and V for laminarin hydrolysis were 6.25 mg/ml and 350 mumol of glucose released/min/mg protein, and for pustulan they were 166 mg/ml and 52 mumol of glucose released/min/mg protein. (4) The exo-beta-glucanase was assigned a molecular weight of 43 000. (5) the purified enzyme failed to hydrolyse isolated cell walls from either baker's yeast or Schizosaccharomyces pombe or to induce protoplast formation from intact cells of S. japonicus var. versatilis or Saccharomyces cerevisiae.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Fleet GH, Phaff HJ","authors_abbrev":"Fleet GH et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Biochim Biophys Acta 1975 Dec 18;410(2):318-32","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1975","pubmed_entrez_date":"1975-12-18","pubmed_publication_date":"18 Dec 1975","terms_by_termid":{},"title":"Glucanases in Schizosaccharomyces. Isolation and properties of an exo-beta-glucanase from the cell extracts and culture fluid of Schizosaccharomyces japonicus var. versatilis.","uniquename":"PMID:1093"}


id: PMID:34427722
data:
  {"abstract":"Fungal pathogens, from phytopathogenic fungus to human pathogens, are able to alternate between the yeast-like form and filamentous forms. This morphological transition (dimorphism) is in close connection with their pathogenic lifestyles and with their responses to changing environmental conditions. The mechanisms governing these morphogenetic conversions are still not fully understood. Therefore, we studied the filamentous growth of the less-known, non-pathogenic dimorphic fission yeast, S. japonicus, which belongs to an ancient and early evolved branch of the Ascomycota. Its RNA sequencing revealed that several hundred genes were up- or down-regulated in the hyphae compared to the yeast-phase cells. These genes belonged to different GO categories, confirming that mycelial growth is a rather complex process. The genes of transport- and metabolic processes appeared especially in high numbers among them. High expression of genes involved in glycolysis and ethanol production was found in the hyphae, while other results pointed to the regulatory role of the protein kinase A (PKA) pathway. The homologues of 49 S. japonicus filament-associated genes were found by sequence alignments also in seven distantly related dimorphic and filamentous species. The comparative genomic analyses between S. japonicus and the closely related but non-dimorphic S. pombe shed some light on the differences in their genomes. All these data can contribute to a better understanding of hyphal growth and those genomic rearrangements that underlie it.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":2,"community_curator":true,"file_name":null,"file_type":null,"name":"Ida Miklos","orcid":"0000-0002-7074-4019"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-10-06","authors":"Papp LA, Ács-Szabó L, Batta G, Miklós I","authors_abbrev":"Papp LA et al.","canto_added_date":"2021-09-29 13:11:40","canto_annotation_status":"APPROVED","canto_approved_date":"2021-10-06 13:34:09","canto_curator_name":"Ida Miklos","canto_curator_role":"community","canto_first_approved_date":"2021-10-06 13:34:09","canto_session_key":"acb5c82405799ef1","canto_session_submitted_date":"2021-09-29 13:38:18","canto_triage_status":"Curatable","citation":"Curr Genet 2021 Dec;67(6):953-968","cv_annotations":{"biological_process":[{"annotations":[116263,116264],"is_not":false,"summary":null,"term":"GO:0030448"}]},"doi":"10.1007/s00294-021-01206-y","gene_count":2,"genes_by_uniquename":{"SJAG_00124":null,"SJAG_04312":null},"genotypes_by_uniquename":{},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-08-24","pubmed_publication_date":"Dec 2021","terms_by_termid":{"GO:0030448":null},"title":"Molecular and comparative genomic analyses reveal evolutionarily conserved and unique features of the Schizosaccharomyces japonicus mycelial growth and the underlying genomic changes.","uniquename":"PMID:34427722"}


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":null}],"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":"2023-05-18 12:11:55","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":[116230],"is_not":false,"summary":null,"term":"FYPO:0007363"},{"annotations":[116228],"is_not":false,"summary":null,"term":"FYPO:0000026"},{"annotations":[116227],"is_not":false,"summary":null,"term":"FYPO:0001355"},{"annotations":[116229],"is_not":false,"summary":null,"term":"FYPO:0001489"},{"annotations":[116231],"is_not":false,"summary":null,"term":"FYPO:0004165"},{"annotations":[116225,116226],"is_not":false,"summary":null,"term":"FYPO:0007790"},{"annotations":[116219,116222],"is_not":false,"summary":null,"term":"FYPO:0000760"},{"annotations":[116221,116224],"is_not":false,"summary":null,"term":"FYPO:0000579"},{"annotations":[116220,116223],"is_not":false,"summary":null,"term":"FYPO:0000590"},{"annotations":[116216,116217,116218],"is_not":false,"summary":null,"term":"FYPO:0001357"},{"annotations":[116215],"is_not":false,"summary":null,"term":"FYPO:0001234"},{"annotations":[116232,116233,116234],"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"}


