메뉴 건너뛰기




Volumn 13, Issue 6, 2013, Pages 518-528

Pyruvate decarboxylase activity is regulated by the Ser/Thr protein phosphatase Sit4p in the yeast Saccharomyces cerevisiae

Author keywords

Fermentation; Pyruvate decarboxylase; Sit4

Indexed keywords

ALKALINE PHOSPHATASE; ANTIBODY; APROTININ; LEUPEPTIN; LIGAND; PDC1P PROTEIN; PEPSTATIN; PHOSPHOPROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOSERINE; PROTEIN; PROTEIN A; PYROPHOSPHATE; PYRUVATE DECARBOXYLASE; PYRUVIC ACID; RESIN; SEPHAROSE; SERINE; SIT4P PROTEIN; THIAMINE; UNCLASSIFIED DRUG;

EID: 84881549977     PISSN: 15671356     EISSN: 15671364     Source Type: Journal    
DOI: 10.1111/1567-1364.12052     Document Type: Article
Times cited : (17)

References (56)
  • 1
    • 79960890549 scopus 로고    scopus 로고
    • Genome-wide survey of yeast mutations leading to activation of the yeast cell integrity MAPK pathway: novel insights into diverse MAPK outcomes
    • Arias P, Díez-Muñiz S, García R, Nombela C, Rodríguez-Peña JM & Arroyo J (2011) Genome-wide survey of yeast mutations leading to activation of the yeast cell integrity MAPK pathway: novel insights into diverse MAPK outcomes. BMC Genomics 12: 390.
    • (2011) BMC Genomics , vol.12 , pp. 390
    • Arias, P.1    Díez-Muñiz, S.2    García, R.3    Nombela, C.4    Rodríguez-Peña, J.M.5    Arroyo, J.6
  • 2
    • 0024977379 scopus 로고
    • A suppressor of a HIS4 transcriptional defect encodes a protein with homology to the catalytic subunit of protein phosphatases
    • Arndt KT, Styles CA & Fink GR (1989) A suppressor of a HIS4 transcriptional defect encodes a protein with homology to the catalytic subunit of protein phosphatases. Cell 56: 527-537.
    • (1989) Cell , vol.56 , pp. 527-537
    • Arndt, K.T.1    Styles, C.A.2    Fink, G.R.3
  • 4
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller B, Mueller LN, Mueller M, Domon B & Aebersold R (2007) Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat Methods 4: 231-237.
    • (2007) Nat Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 6
    • 78650632764 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals interconnected system-wide responses to perturbations of kinases and phosphatases in yeast
    • Bodenmiller B, Wanka S, Kraft C et al. (2010) Phosphoproteomic analysis reveals interconnected system-wide responses to perturbations of kinases and phosphatases in yeast. Sci Signal 3: rs4.
    • (2010) Sci Signal , vol.3
    • Bodenmiller, B.1    Wanka, S.2    Kraft, C.3
  • 8
    • 0023095029 scopus 로고
    • Promoter and nucleotide sequences of the Zymomonas mobilis pyruvate decarboxylase
    • Conway T, Osman YA, Konnan JI, Hoffmann EM & Ingram LO (1987) Promoter and nucleotide sequences of the Zymomonas mobilis pyruvate decarboxylase. J Bacteriol 169: 949-954.
    • (1987) J Bacteriol , vol.169 , pp. 949-954
    • Conway, T.1    Osman, Y.A.2    Konnan, J.I.3    Hoffmann, E.M.4    Ingram, L.O.5
  • 9
    • 0029808294 scopus 로고    scopus 로고
    • Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases
    • Di Como CJ & Arndt KT (1996) Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes Dev 10: 1904-1916.
    • (1996) Genes Dev , vol.10 , pp. 1904-1916
    • Di Como, C.J.1    Arndt, K.T.2
  • 11
    • 0033563156 scopus 로고    scopus 로고
    • Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity
    • Eberhardt I, Cederberg H, Li H, König S, Jordan F & Hohmann S (1999) Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity. Eur J Biochem 262: 191-201.
    • (1999) Eur J Biochem , vol.262 , pp. 191-201
    • Eberhardt, I.1    Cederberg, H.2    Li, H.3    König, S.4    Jordan, F.5    Hohmann, S.6
  • 12
    • 0026343742 scopus 로고
    • The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase
    • Feng ZH, Wilson SE, Peng ZY, Schlender KK, Reimann EM & Trumbly RJ (1991) The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase. J Biol Chem 266: 23796-23801.
    • (1991) J Biol Chem , vol.266 , pp. 23796-23801
    • Feng, Z.H.1    Wilson, S.E.2    Peng, Z.Y.3    Schlender, K.K.4    Reimann, E.M.5    Trumbly, R.J.6
  • 13
    • 0027102212 scopus 로고
    • SIT4 protein phosphatase is required for the normal accumulation of SWI4, CLN1, CLN2, and HCS26 RNAs during late G1
    • Fernandez-Sarabia MJ, Sutton A, Zhong T & Arndt KT (1992) SIT4 protein phosphatase is required for the normal accumulation of SWI4, CLN1, CLN2, and HCS26 RNAs during late G1. Genes Dev 6: 2417-2428.
    • (1992) Genes Dev , vol.6 , pp. 2417-2428
    • Fernandez-Sarabia, M.J.1    Sutton, A.2    Zhong, T.3    Arndt, K.T.4
  • 14
    • 61349119934 scopus 로고    scopus 로고
    • Functional organization of the S. cerevisiae phosphorylation network
    • Fiedler D, Braberg H, Mehta M et al. (2009) Functional organization of the S. cerevisiae phosphorylation network. Cell 136: 952-963.
    • (2009) Cell , vol.136 , pp. 952-963
    • Fiedler, D.1    Braberg, H.2    Mehta, M.3
  • 15
    • 0032537592 scopus 로고    scopus 로고
    • Structure-function relationships and flexible tetramer assembly in pyruvate decarboxylase revealed by analysis of crystal structures
    • Furey W, Arjunan P, Chen L, Sax M, Guo F & Jordan F (1998) Structure-function relationships and flexible tetramer assembly in pyruvate decarboxylase revealed by analysis of crystal structures. Biochim Biophys Acta 1385: 253-270.
    • (1998) Biochim Biophys Acta , vol.1385 , pp. 253-270
    • Furey, W.1    Arjunan, P.2    Chen, L.3    Sax, M.4    Guo, F.5    Jordan, F.6
  • 16
    • 0016834360 scopus 로고
    • Pyruvate decarboxylase III. Specificity restrictions for thiamine pyrophosphate in the protein association step, sub-unit structure
    • Gounaris AD, Turkenkopf I, Civerchia LL & Greenlie J (1975) Pyruvate decarboxylase III. Specificity restrictions for thiamine pyrophosphate in the protein association step, sub-unit structure. Biochim Biophys Acta 405: 492-499.
    • (1975) Biochim Biophys Acta , vol.405 , pp. 492-499
    • Gounaris, A.D.1    Turkenkopf, I.2    Civerchia, L.L.3    Greenlie, J.4
  • 19
    • 27744553838 scopus 로고    scopus 로고
    • Three novel antibiotic marker cassettes for gene disruption and marker switching in Schizosaccharomyces pombe
    • Hentges P, Van Driessche B, Tafforeau L, Vandenhaute J & Carr AM (2005) Three novel antibiotic marker cassettes for gene disruption and marker switching in Schizosaccharomyces pombe. Yeast 22: 1013-1019.
    • (2005) Yeast , vol.22 , pp. 1013-1019
    • Hentges, P.1    Van Driessche, B.2    Tafforeau, L.3    Vandenhaute, J.4    Carr, A.M.5
  • 20
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y, Gruhler A, Heilbut A et al. (2002) Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415: 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3
  • 21
    • 0026315442 scopus 로고
    • Characterization of PDC6, a third structural gene for pyruvate decarboxylase in Saccharomyces cerevisiae
    • Hohmann S (1991) Characterization of PDC6, a third structural gene for pyruvate decarboxylase in Saccharomyces cerevisiae. J Bacteriol 173: 7963-7969.
    • (1991) J Bacteriol , vol.173 , pp. 7963-7969
    • Hohmann, S.1
  • 23
    • 0020560838 scopus 로고
    • Apphed microbiology and biotechnology purification and kinetic characteristics of pyruvate decarboxylase and ethanol dehydrogenase from Zymomonas mobilis in relation to ethanol production purification of alcohol dehydrogenase purification of pyruvate deca
    • Hoppner TC & Doelle HW (1983) Apphed microbiology and biotechnology purification and kinetic characteristics of pyruvate decarboxylase and ethanol dehydrogenase from Zymomonas mobilis in relation to ethanol production purification of alcohol dehydrogenase purification of pyruvate deca. Eur J Appl Microbiol 410: 152-157.
    • (1983) Eur J Appl Microbiol , vol.410 , pp. 152-157
    • Hoppner, T.C.1    Doelle, H.W.2
  • 24
    • 33745442172 scopus 로고    scopus 로고
    • Deviation of carbohydrate metabolism by the SIT4 phosphatase in Saccharomyces cerevisiae
    • Jablonka W, Guzmán S, Ramírez J & Montero-Lomelí M (2006) Deviation of carbohydrate metabolism by the SIT4 phosphatase in Saccharomyces cerevisiae. Biochim Biophys Acta 1760: 1281-1291.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 1281-1291
    • Jablonka, W.1    Guzmán, S.2    Ramírez, J.3    Montero-Lomelí, M.4
  • 25
    • 36549072484 scopus 로고    scopus 로고
    • SIT4 regulation of Mig1p-mediated catabolite repression in Saccharomyces cerevisiae
    • Jin C, Barrientos A, Epstein CB, Butow RA & Tzgoloff A (2007) SIT4 regulation of Mig1p-mediated catabolite repression in Saccharomyces cerevisiae. FEBS Lett 581: 5658-5663.
    • (2007) FEBS Lett , vol.581 , pp. 5658-5663
    • Jin, C.1    Barrientos, A.2    Epstein, C.B.3    Butow, R.A.4    Tzgoloff, A.5
  • 26
    • 0032537477 scopus 로고    scopus 로고
    • Regulation of thiamin diphosphate-dependent 2-oxo acid decarboxylases by substrate and thiamin diphosphate.Mg(II) - evidence for tertiary and quaternary interactions
    • Jordan F, Nemeria N, Guo F, Baburina I, Gao Y, Kahyaoglu A, Li H, Wang J, Yi J, Guest JR & Furey W (1998) Regulation of thiamin diphosphate-dependent 2-oxo acid decarboxylases by substrate and thiamin diphosphate.Mg(II) - evidence for tertiary and quaternary interactions. Biochim Biophys Acta 1385: 287-306.
    • (1998) Biochim Biophys Acta , vol.1385 , pp. 287-306
    • Jordan, F.1    Nemeria, N.2    Guo, F.3    Baburina, I.4    Gao, Y.5    Kahyaoglu, A.6    Li, H.7    Wang, J.8    Yi, J.9    Guest, J.R.10    Furey, W.11
  • 27
    • 0023057207 scopus 로고
    • Analysis of the primary structure and promoter function of a pyruvate decarboxylase gene (PDC1) from Saccharomyces cerevisiae
    • Kellermann E, Seeboth PG & Hollenberg CP (1986) Analysis of the primary structure and promoter function of a pyruvate decarboxylase gene (PDC1) from Saccharomyces cerevisiae. Nucleic Acid Res 14: 8963-8977.
    • (1986) Nucleic Acid Res , vol.14 , pp. 8963-8977
    • Kellermann, E.1    Seeboth, P.G.2    Hollenberg, C.P.3
  • 28
    • 66449102566 scopus 로고    scopus 로고
    • Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation
    • Kutter S, Weiss MS, Wille G, Golbik R, Spinka M & König S (2009) Covalently bound substrate at the regulatory site of yeast pyruvate decarboxylases triggers allosteric enzyme activation. J Biol Chem 284: 12136-12144.
    • (2009) J Biol Chem , vol.284 , pp. 12136-12144
    • Kutter, S.1    Weiss, M.S.2    Wille, G.3    Golbik, R.4    Spinka, M.5    König, S.6
  • 29
    • 84862789978 scopus 로고    scopus 로고
    • TOR signaling regulates ribosome and tRNA synthesis via LAMMER/Clk and GSK-3 family kinases
    • Lee J, Moir RD, Mcintosh KB & Willis IM (2012) TOR signaling regulates ribosome and tRNA synthesis via LAMMER/Clk and GSK-3 family kinases. Mol Cell 45: 836-843.
    • (2012) Mol Cell , vol.45 , pp. 836-843
    • Lee, J.1    Moir, R.D.2    Mcintosh, K.B.3    Willis, I.M.4
  • 31
  • 36
    • 0025897608 scopus 로고
    • A constitutive thiamine metabolism mutation, THI80, causing reduced thiamine pyrophosphokinase activity in Saccharomyces cerevisiae
    • Nishimura H, Kawasaki Y, Nosaka K, Kaneko Y & Iwashima A (1991) A constitutive thiamine metabolism mutation, THI80, causing reduced thiamine pyrophosphokinase activity in Saccharomyces cerevisiae. J Bacteriol 173: 2716-2719.
    • (1991) J Bacteriol , vol.173 , pp. 2716-2719
    • Nishimura, H.1    Kawasaki, Y.2    Nosaka, K.3    Kaneko, Y.4    Iwashima, A.5
  • 37
    • 0031573036 scopus 로고    scopus 로고
    • Mutation THI81 causing a deficiency in the signal transduction of thiamine pyrophosphate in Saccharomyces cerevisiae
    • Nishimura H, Kawasaki Y, Nosaka K & Kaneko Y (1997) Mutation THI81 causing a deficiency in the signal transduction of thiamine pyrophosphate in Saccharomyces cerevisiae. FEMS Microb Lett 156: 245-249.
    • (1997) FEMS Microb Lett , vol.156 , pp. 245-249
    • Nishimura, H.1    Kawasaki, Y.2    Nosaka, K.3    Kaneko, Y.4
  • 38
    • 0026701003 scopus 로고
    • Upstream activation element of the PH03 gene encoding for thiamine-repressible acid phosphatase in Saccharomyces cerevisiae
    • Nosaka K, Kaneko Y, Nishimura H & Iwashima A (1992) Upstream activation element of the PH03 gene encoding for thiamine-repressible acid phosphatase in Saccharomyces cerevisiae. FEBS Lett 305: 244-248.
    • (1992) FEBS Lett , vol.305 , pp. 244-248
    • Nosaka, K.1    Kaneko, Y.2    Nishimura, H.3    Iwashima, A.4
  • 39
    • 0001363302 scopus 로고
    • Changes in the enzyme activities of Saccharomyces cerevisiae during aerobic growth on different carbon sources
    • Polakis ES & Bartley W (1965) Changes in the enzyme activities of Saccharomyces cerevisiae during aerobic growth on different carbon sources. Biochem J 97: 284-297.
    • (1965) Biochem J , vol.97 , pp. 284-297
    • Polakis, E.S.1    Bartley, W.2
  • 40
    • 0026020276 scopus 로고
    • Saccharomyces cerevisiae gene SIT4 is involved in the control of glycogen metabolism
    • Posas F, Clotet J & Arino J (1991) Saccharomyces cerevisiae gene SIT4 is involved in the control of glycogen metabolism. FEBS Lett 279: 341-345.
    • (1991) FEBS Lett , vol.279 , pp. 341-345
    • Posas, F.1    Clotet, J.2    Arino, J.3
  • 41
    • 0030448870 scopus 로고    scopus 로고
    • Pyruvate metabolism in Saccharomyces cerevisiae
    • Pronk JT, Yde Steensma H & Van Dijken JP (1996) Pyruvate metabolism in Saccharomyces cerevisiae. Yeast 12: 1607-1633.
    • (1996) Yeast , vol.12 , pp. 1607-1633
    • Pronk, J.T.1    Yde Steensma, H.2    Van Dijken, J.P.3
  • 42
    • 28444460297 scopus 로고    scopus 로고
    • Global analysis of protein phosphorylation in yeast
    • Ptacek J, Devgan G & Michaud G et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438: 679-684.
    • (2005) Nature , vol.438 , pp. 679-684
    • Ptacek, J.1    Devgan, G.2    Michaud, G.3
  • 43
    • 33645130011 scopus 로고    scopus 로고
    • Glucose signaling in Saccharomyces cerevisiae
    • Santangelo GM (2006) Glucose signaling in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 70: 253-282.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 253-282
    • Santangelo, G.M.1
  • 44
    • 0024538747 scopus 로고
    • A deletion of the PDC1 gene for pyruvate decarboxylase of yeast causes a different phenotype than previously isolated point mutations
    • Schaaff I, Green JB, Gozalbo D & Hohmann S (1989) A deletion of the PDC1 gene for pyruvate decarboxylase of yeast causes a different phenotype than previously isolated point mutations. Curr Genetics 15: 75-81.
    • (1989) Curr Genetics , vol.15 , pp. 75-81
    • Schaaff, I.1    Green, J.B.2    Gozalbo, D.3    Hohmann, S.4
  • 45
    • 0020457910 scopus 로고
    • Genetic analysis of the pyruvate decarboxylase reaction in yeast glycolysis
    • Schmitt HD & Zimmermann FK (1982) Genetic analysis of the pyruvate decarboxylase reaction in yeast glycolysis. J Bacteriol 151: 1146-1152.
    • (1982) J Bacteriol , vol.151 , pp. 1146-1152
    • Schmitt, H.D.1    Zimmermann, F.K.2
  • 46
    • 0025381813 scopus 로고
    • pdc1(0) mutants of Saccharomyces cerevisiae give evidence for an additional structural PDC gene: cloning of PDC5, a gene homologous to PDC1
    • Seeboth PG, Bohnsack K & Hollenberg CP (1990) pdc1(0) mutants of Saccharomyces cerevisiae give evidence for an additional structural PDC gene: cloning of PDC5, a gene homologous to PDC1. J Bacteriol 172: 678-685.
    • (1990) J Bacteriol , vol.172 , pp. 678-685
    • Seeboth, P.G.1    Bohnsack, K.2    Hollenberg, C.P.3
  • 47
    • 0037414754 scopus 로고    scopus 로고
    • PHO85 phosphorylates the GLC7 protein phosphatase regulator Glc8 in vivo
    • Tan YSH, Morcos PA & Cannon JF (2003) PHO85 phosphorylates the GLC7 protein phosphatase regulator Glc8 in vivo. J Biol Chem 278: 147-153.
    • (2003) J Biol Chem , vol.278 , pp. 147-153
    • Tan, Y.S.H.1    Morcos, P.A.2    Cannon, J.F.3
  • 49
    • 0024340089 scopus 로고
    • Localization and Kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621
    • Urk HV, Schipper D, Breedveld GJ, Mak PR, Scheffers WA & Van Dijken JP (1989) Localization and Kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621. Biochim Biophys Acta 992: 78-86.
    • (1989) Biochim Biophys Acta , vol.992 , pp. 78-86
    • Urk, H.V.1    Schipper, D.2    Breedveld, G.J.3    Mak, P.R.4    Scheffers, W.A.5    Van Dijken, J.P.6
  • 51
    • 0031038220 scopus 로고    scopus 로고
    • Suppression of PDC2 of regulating pyruvate decarboxylase synthesis in yeast
    • Velmurugan S, Lobo Z & Maitra PK (1997) Suppression of PDC2 of regulating pyruvate decarboxylase synthesis in yeast. Mol Biol 145: 587-594.
    • (1997) Mol Biol , vol.145 , pp. 587-594
    • Velmurugan, S.1    Lobo, Z.2    Maitra, P.K.3
  • 52
    • 0344824568 scopus 로고    scopus 로고
    • Interaction with Tap42 is required for the essential function of Sit4 and type 2A phosphatases
    • Wang H, Wang X & Jiang Y (2003) Interaction with Tap42 is required for the essential function of Sit4 and type 2A phosphatases. Mol Biol Cell 14: 4342-4351.
    • (2003) Mol Biol Cell , vol.14 , pp. 4342-4351
    • Wang, H.1    Wang, X.2    Jiang, Y.3
  • 53
    • 0028314909 scopus 로고
    • Effects of oxygen limitation on sugar metabolism in yeasts: a continuous-culture study of the Kluyver effect
    • Weusthuis RA, Visser W, Pronk JT, Scheffers WA & Van Dijken JP (1994) Effects of oxygen limitation on sugar metabolism in yeasts: a continuous-culture study of the Kluyver effect. Microbiology 140: 703-715.
    • (1994) Microbiology , vol.140 , pp. 703-715
    • Weusthuis, R.A.1    Visser, W.2    Pronk, J.T.3    Scheffers, W.A.4    Van Dijken, J.P.5
  • 54
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import in yeast
    • Yaffe MP & Schatz G (1984) Two nuclear mutations that block mitochondrial protein import in yeast. PNAS 81: 4819-4823.
    • (1984) PNAS , vol.81 , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2
  • 55
    • 0030448102 scopus 로고    scopus 로고
    • Effect of substitutions in the thiamin diphosphate-magnesium fold on the activation of the pyruvate dehydrogenase complex from Escherichia coli by cofactors and substrate
    • Yi J, Nemeria N, McNally A, Jordan F, Machado RS & Guest JR (1996) Effect of substitutions in the thiamin diphosphate-magnesium fold on the activation of the pyruvate dehydrogenase complex from Escherichia coli by cofactors and substrate. J Biol Chem 271: 33192-33200.
    • (1996) J Biol Chem , vol.271 , pp. 33192-33200
    • Yi, J.1    Nemeria, N.2    McNally, A.3    Jordan, F.4    Machado, R.S.5    Guest, J.R.6
  • 56
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H, Watts JD & Aebersold R (2001) A systematic approach to the analysis of protein phosphorylation. Nat Biotech 19: 375-378.
    • (2001) Nat Biotech , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.