{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T20:49:43Z","timestamp":1789073383201,"version":"build-2803163510"},"reference-count":43,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T00:00:00Z","timestamp":1782950400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T00:00:00Z","timestamp":1782950400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100010157","name":"Noda Institute for Scientific Research","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010157","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["21H02103"],"award-info":[{"award-number":["21H02103"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["25K09036"],"award-info":[{"award-number":["25K09036"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100011041","name":"Asahi Group Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100011041","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>\n                    Pyruvate decarboxylase (PDC) catalyzes the decarboxylation of pyruvate to yield acetaldehyde, using thiamine pyrophosphate as a coenzyme.\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    has two functional PDCs, Pdc1 and Pdc5, whose reactions constitute the first step in the alcoholic fermentation pathway.\n                    <jats:italic>PDC1<\/jats:italic>\n                    is abundantly expressed in wild\u2010type cells, whereas\n                    <jats:italic>PDC5<\/jats:italic>\n                    is markedly repressed when cells are cultured in a glucose medium.\n                    <jats:italic>PDC5<\/jats:italic>\n                    expression is induced in a Pdc1 deletion mutant, a phenomenon referred to as autoregulation, and this induction depends on the transcriptional regulator Pdc2. Therefore, it has been proposed that Pdc1 plays a role as a regulator of gene expression, in addition to its function as a PDC. However, the regulatory mechanism by which Pdc1 represses the\n                    <jats:italic>PDC5<\/jats:italic>\n                    induction remains poorly understood. In addition, the phenotypes resulting from\n                    <jats:italic>PDC1<\/jats:italic>\n                    deficiency alone are poorly understood because\n                    <jats:italic>PDC5<\/jats:italic>\n                    expression, through autoregulation, compensates for the overall PDC activity in the cell. Here, we showed that a\n                    <jats:italic>PDC1<\/jats:italic>\n                    deletion mutant exhibited increased sensitivity to 2\u2010deoxyglucose (2\u2010DG). We found that overexpression of\n                    <jats:italic>PDC2<\/jats:italic>\n                    suppressed the 2\u2010DG\u2010sensitive phenotype of\n                    <jats:italic>pdc1\u2206<\/jats:italic>\n                    cells and that 2\u2010DG decreased cellular PDC activity through inhibiting Pdc2. The suppressive effect of Pdc2 was abolished by truncation of an intrinsically disordered region at its C terminus. The increased sensitivity to 2\u2010DG may be useful for understanding the mechanism by which Pdc1 regulates\n                    <jats:italic>PDC5<\/jats:italic>\n                    expression via Pdc2.\n                  <\/jats:p>","DOI":"10.1111\/febs.70640","type":"journal-article","created":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T07:09:49Z","timestamp":1782976189000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["<scp>\n                      <i>PDC1<\/i>\n                    <\/scp>\n                    deficiency results in 2\u2010deoxyglucose sensitivity through inhibition of Pdc2 activity in yeast"],"prefix":"10.1111","author":[{"given":"Mayu","family":"Kubota","sequence":"first","affiliation":[{"name":"Laboratory of Molecular Microbiology, Division of Applied Life Sciences, Graduate School of Agriculture Kyoto University  Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daika","family":"Seki","sequence":"additional","affiliation":[{"name":"Division of Food Science and Biotechnology, Graduate School of Agriculture Shinshu University  Nagano Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hitomi","family":"Nakamura","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Microbiology, Division of Applied Life Sciences, Graduate School of Agriculture Kyoto University  Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9960-9155","authenticated-orcid":false,"given":"Akira","family":"Hosomi","sequence":"additional","affiliation":[{"name":"Division of Food Science and Biotechnology, Graduate School of Agriculture Shinshu University  Nagano Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshiharu","family":"Inoue","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Microbiology, Division of Applied Life Sciences, Graduate School of Agriculture Kyoto University  Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9350-5988","authenticated-orcid":false,"given":"Wataru","family":"Nomura","sequence":"additional","affiliation":[{"name":"Laboratory of Molecular Microbiology, Division of Applied Life Sciences, Graduate School of Agriculture Kyoto University  Japan"},{"name":"Division of Food Science and Biotechnology, Graduate School of Agriculture Shinshu University  Nagano Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,7,2]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"crossref","first-page":"8963","DOI":"10.1093\/nar\/14.22.8963","article-title":"Analysis of the primary structure and promoter function of a pyruvate decarboxylase gene (PDC1) from Saccharomyces cerevisiae","volume":"14","author":"Kellermann E","year":"1986","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_3_1","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1002\/(SICI)1097-0061(199612)12:16<1607::AID-YEA70>3.0.CO;2-4","article-title":"Pyruvate metabolism in Saccharomyces cerevisiae","volume":"12","author":"Pronk JT","year":"1996","journal-title":"Yeast"},{"key":"e_1_2_10_4_1","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1007\/BF00327674","article-title":"The synthesis of yeast pyruvate decarboxylase is regulated by large variations in the messenger RNA level","volume":"192","author":"Schmitt HD","year":"1983","journal-title":"Mol Gen Genet"},{"key":"e_1_2_10_5_1","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1111\/j.1432-1033.1990.tb15442.x","article-title":"Autoregulation may control the expression of yeast pyruvate decarboxylase structural genes PDC1 and PDC5","volume":"188","author":"Hohmann S","year":"1990","journal-title":"Eur J Biochem"},{"key":"e_1_2_10_6_1","doi-asserted-by":"crossref","first-page":"7963","DOI":"10.1128\/jb.173.24.7963-7969.1991","article-title":"Characterization of PDC6, a third structural gene for pyruvate decarboxylase in Saccharomyces cerevisiae","volume":"173","author":"Hohmann S","year":"1991","journal-title":"J Bacteriol"},{"key":"e_1_2_10_7_1","doi-asserted-by":"crossref","DOI":"10.1093\/femsyr\/foaf014","article-title":"The advances in creating Crabtree\u2010negative Saccharomyces cerevisiae and the application for chemicals biosynthesis","volume":"25","author":"Guo Y","year":"2025","journal-title":"FEMS Yeast Res"},{"key":"e_1_2_10_8_1","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1002\/(SICI)1097-0061(19960315)12:3<247::AID-YEA911>3.0.CO;2-I","article-title":"Pyruvate decarboxylase: an indispensable enzyme for growth of Saccharomyces cerevisiae on glucose","volume":"12","author":"Flikweert MT","year":"1996","journal-title":"Yeast"},{"key":"e_1_2_10_9_1","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1046\/j.1432-1327.1999.00370.x","article-title":"Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity","volume":"262","author":"Eberhardt I","year":"1999","journal-title":"Eur J Biochem"},{"key":"e_1_2_10_10_1","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1007\/s00438-006-0130-z","article-title":"Pdc2 coordinates expression of the THI regulon in the yeast Saccharomyces cerevisiae","volume":"276","author":"Mojzita D","year":"2006","journal-title":"Mol Gen Genomics"},{"key":"e_1_2_10_11_1","doi-asserted-by":"crossref","first-page":"3991","DOI":"10.1016\/j.febslet.2008.10.051","article-title":"Thiamin\u2010dependent transactivation activity of PDC2 in Saccharomyces cerevisiae","volume":"582","author":"Nosaka K","year":"2008","journal-title":"FEBS Lett"},{"key":"e_1_2_10_12_1","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1111\/j.1574-6968.2012.02543.x","article-title":"Facilitated recruitment of Pdc2p, a yeast transcriptional activator, in response to thiamin starvation","volume":"330","author":"Nosaka K","year":"2012","journal-title":"FEMS Microbiol Lett"},{"key":"e_1_2_10_13_1","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/S0014-5793(99)00449-4","article-title":"Thiamine repression and pyruvate decarboxylase autoregulation independently control the expression of the Saccharomyces cerevisiae PDC5 gene","volume":"449","author":"Muller EH","year":"1999","journal-title":"FEBS Lett"},{"key":"e_1_2_10_14_1","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1128\/MMBR.00012-16","article-title":"The expanding landscape of moonlighting proteins in yeasts","volume":"80","author":"Gancedo C","year":"2016","journal-title":"Microbiol Mol Biol Rev"},{"key":"e_1_2_10_15_1","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1016\/0300-9084(92)90070-U","article-title":"The inhibition of bovine heart hexokinase by 2\u2010deoxy\u2010D\u2010glucose\u20106\u2010phosphate: characterization by 31P NMR and metabolic implications","volume":"74","author":"Chen W","year":"1992","journal-title":"Biochimie"},{"key":"e_1_2_10_16_1","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1016\/S0021-9258(18)64988-9","article-title":"Localization of the primary metabolic block produced by 2\u2010deoxyglucose","volume":"224","author":"Wick AN","year":"1957","journal-title":"J Biol Chem"},{"key":"e_1_2_10_17_1","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1126\/science.1715094","article-title":"Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast","volume":"253","author":"Heitman J","year":"1991","journal-title":"Science"},{"key":"e_1_2_10_18_1","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/S1097-2765(02)00636-6","article-title":"Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control","volume":"10","author":"Loewith R","year":"2002","journal-title":"Mol Cell"},{"key":"e_1_2_10_19_1","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/BF00315774","article-title":"The expression of a specific 2\u2010deoxyglucose\u20106P phosphatase prevents catabolite repression mediated by 2\u2010deoxyglucose in yeast","volume":"28","author":"Randez\u2010Gil F","year":"1995","journal-title":"Curr Genet"},{"key":"e_1_2_10_20_1","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1007\/s00294-020-01122-7","article-title":"'Sugarcoating' 2\u2010deoxyglucose: mechanisms that suppress its toxic effects","volume":"67","author":"Schmidt MC","year":"2021","journal-title":"Curr Genet"},{"key":"e_1_2_10_21_1","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.aaw8000","article-title":"The induction of HAD\u2010like phosphatases by multiple signaling pathways confers resistance to the metabolic inhibitor 2\u2010deoxyglucose","volume":"12","author":"Defenouill\u00e8re Q","year":"2019","journal-title":"Sci Signal"},{"key":"e_1_2_10_22_1","doi-asserted-by":"crossref","first-page":"20920","DOI":"10.1074\/jbc.M909851199","article-title":"Characterization of two 5\u2010aminoimidazole\u20104\u2010carboxamide ribonucleotide transformylase\/inosine monophosphate cyclohydrolase isozymes from Saccharomyces cerevisiae","volume":"275","author":"Tibbetts AS","year":"2000","journal-title":"J Biol Chem"},{"key":"e_1_2_10_23_1","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1007\/BF00279908","article-title":"Characterisation of PDC2, a gene necessary for high level expression of pyruvate decarboxylase structural genes in Saccharomyces cerevisiae","volume":"241","author":"Hohmann S","year":"1993","journal-title":"Mol Gen Genet"},{"key":"e_1_2_10_24_1","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1021\/bi961341l","article-title":"Role of Glu51 for cofactor binding and catalytic activity in pyruvate decarboxylase from yeast studied by site\u2010directed mutagenesis","volume":"36","author":"Killenberg\u2010Jabs M","year":"1997","journal-title":"Biochemistry"},{"key":"e_1_2_10_25_1","doi-asserted-by":"crossref","first-page":"5630","DOI":"10.1021\/bi00184a035","article-title":"Substrate activation of brewers' yeast pyruvate decarboxylase is abolished by mutation of cysteine 221 to serine","volume":"33","author":"Baburina I","year":"1994","journal-title":"Biochemistry"},{"key":"e_1_2_10_26_1","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0167-4838(98)00075-2","article-title":"Regulation of thiamin diphosphate\u2010dependent 2\u2010oxo acid decarboxylases by substrate and thiamin diphosphate. Mg(II) \u2010 evidence for tertiary and quaternary interactions","volume":"1385","author":"Jordan F","year":"1998","journal-title":"Biochim Biophys Acta"},{"key":"e_1_2_10_27_1","doi-asserted-by":"crossref","first-page":"W329","DOI":"10.1093\/nar\/gky384","article-title":"IUPred2A: context\u2010dependent prediction of protein disorder as a function of redox state and protein binding","volume":"46","author":"M\u00e9sz\u00e1ros B","year":"2018","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_28_1","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1016\/j.molcel.2020.05.032","article-title":"Intrinsically disordered regions direct transcription factor in vivo binding specificity","volume":"79","author":"Brodsky S","year":"2020","journal-title":"Mol Cell"},{"key":"e_1_2_10_29_1","doi-asserted-by":"crossref","first-page":"1472","DOI":"10.1128\/EC.00189-14","article-title":"Protein acetylation and acetyl coenzyme a metabolism in budding yeast","volume":"13","author":"Galdieri L","year":"2014","journal-title":"Eukaryot Cell"},{"key":"e_1_2_10_30_1","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1111\/j.1365-2958.1996.tb02570.x","article-title":"ERA, a novel cis\u2010acting element required for autoregulation and ethanol repression of PDC1 transcription in Saccharomyces cerevisiae","volume":"21","author":"Liesen T","year":"1996","journal-title":"Mol Microbiol"},{"key":"e_1_2_10_31_1","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1093\/genetics\/145.3.587","article-title":"Suppression of pdc2 regulating pyruvate decarboxylase synthesis in yeast","volume":"145","author":"Velmurugan S","year":"1997","journal-title":"Genetics"},{"key":"e_1_2_10_32_1","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1534\/genetics.114.169060","article-title":"Genetic analysis of resistance and sensitivity to 2\u2010deoxyglucose in Saccharomyces cerevisiae","volume":"198","author":"RR MC","year":"2014","journal-title":"Genetics"},{"key":"e_1_2_10_33_1","doi-asserted-by":"crossref","first-page":"3701","DOI":"10.1038\/s41467-022-31282-8","article-title":"Lsm7 phase\u2010separated condensates trigger stress granule formation","volume":"13","author":"Lindstr\u00f6m M","year":"2022","journal-title":"Nat Commun"},{"key":"e_1_2_10_34_1","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.tcb.2015.10.003","article-title":"TOR complexes and the maintenance of cellular homeostasis","volume":"26","author":"Eltschinger S","year":"2016","journal-title":"Trends Cell Biol"},{"key":"e_1_2_10_35_1","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/B978-0-12-152812-6.50010-X","article-title":"The role of compartmentation in the control of glycolysis","volume":"12","author":"Ottaway JH","year":"1977","journal-title":"Curr Top Cell Regul"},{"key":"e_1_2_10_36_1","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.48480","article-title":"RNA promotes phase separation of glycolysis enzymes into yeast G bodies in hypoxia","volume":"9","author":"Fuller GG","year":"2020","journal-title":"elife"},{"key":"e_1_2_10_37_1","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.1002\/(SICI)1097-0061(199911)15:15<1669::AID-YEA480>3.0.CO;2-6","article-title":"A series of protein phosphatase gene disruptants in Saccharomyces cerevisiae","volume":"15","author":"Sakumoto N","year":"1999","journal-title":"Yeast"},{"key":"e_1_2_10_38_1","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1002\/(SICI)1097-0061(199807)14:10<953::AID-YEA293>3.0.CO;2-U","article-title":"Additional modules for versatile and economical PCR\u2010based gene deletion and modification in Saccharomyces cerevisiae","volume":"14","author":"Longtine MS","year":"1998","journal-title":"Yeast"},{"key":"e_1_2_10_39_1","doi-asserted-by":"crossref","first-page":"2519","DOI":"10.1093\/nar\/24.13.2519","article-title":"A new efficient gene disruption cassette for repeated use in budding yeast","volume":"24","author":"G\u00fcldener U","year":"1996","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_10_40_1","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1002\/yea.1142","article-title":"A versatile toolbox for PCR\u2010based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes","volume":"21","author":"Janke C","year":"2004","journal-title":"Yeast"},{"key":"e_1_2_10_41_1","doi-asserted-by":"crossref","first-page":"13887","DOI":"10.1038\/s41598-020-70802-8","article-title":"Methylglyoxal inhibits nuclear division through alterations in vacuolar morphology and accumulation of Atg18 on the vacuolar membrane in Saccharomyces cerevisiae","volume":"10","author":"Nomura W","year":"2020","journal-title":"Sci Rep"},{"key":"e_1_2_10_42_1","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1038\/s42003-024-06411-2","article-title":"Activation of the cell wall integrity pathway negatively regulates TORC2\u2010Ypk1\/2 signaling through blocking eisosome disassembly in Saccharomyces cerevisiae","volume":"7","author":"Nomura W","year":"2024","journal-title":"Commun Biol"},{"key":"e_1_2_10_43_1","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1042\/BJ20091334","article-title":"Calcineurin\/Crz1 destabilizes Msn2 and Msn4 in the nucleus in response to Ca2+ in Saccharomyces cerevisiae","volume":"427","author":"Takatsume Y","year":"2010","journal-title":"Biochem J"},{"key":"e_1_2_10_44_1","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/0076-6879(71)18287-0","article-title":"Yeast pyruvate decarboxylase (2\u2010oxoacid carboxy\u2010lyase, EC 4.1.1.1) assay of thiamine pyrophosphate","volume":"18","author":"Ullrich J","year":"1970","journal-title":"Methods Enzymol"}],"container-title":["The FEBS Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/febs.70640","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/full-xml\/10.1111\/febs.70640","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/febs.70640","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T07:09:55Z","timestamp":1782976195000},"score":1,"resource":{"primary":{"URL":"https:\/\/febs.onlinelibrary.wiley.com\/doi\/10.1111\/febs.70640"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7,2]]},"references-count":43,"alternative-id":["10.1111\/febs.70640"],"URL":"https:\/\/doi.org\/10.1111\/febs.70640","archive":["Portico"],"relation":{},"ISSN":["1742-464X","1742-4658"],"issn-type":[{"value":"1742-464X","type":"print"},{"value":"1742-4658","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,7,2]]},"assertion":[{"value":"2025-10-31","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-06-22","order":2,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2026-07-02","order":3,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}],"article-number":"febs.70640"}}