메뉴 건너뛰기




Volumn 7, Issue 2, 2004, Pages 115-119

A link between transcription and intermediary metabolism: A role for Sir2 in the control of acetyl-coenzyme A synthetase

Author keywords

2 O acetyl adenosine diphosphate ribose; Acetyl coenzyme A synthetase; Acs; Adenosine monophosphate; AMP; CoA; Coenzyme A; NAD+; NADH; OAADPr; Oxidized nicotinamide adenine dinucleotide; Reduced NAD; Silent information regulator; Sir2

Indexed keywords

ACETYL COENZYME A SYNTHETASE; SILENT INFORMATION REGULATOR PROTEIN 2;

EID: 1842610541     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2004.02.005     Document Type: Review
Times cited : (41)

References (35)
  • 1
    • 0033610894 scopus 로고    scopus 로고
    • CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide:5,6- dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2
    • Tsang A.W., Escalante-Semerena J.C. CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide:5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2. J Biol Chem. 273:1998;31788-31794.
    • (1998) J Biol Chem , vol.273 , pp. 31788-31794
    • Tsang, A.W.1    Escalante-Semerena, J.C.2
  • 4
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S.-I., Armstrong C.M., Kaeberlein M., Guarente L. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature. 403:2000;795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.-I.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 6
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., Gu W. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell. 107:2001;137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 7
    • 0036753953 scopus 로고    scopus 로고
    • Structure of a Sir2 enzyme bound to an acetylated p53 peptide
    • The first report of the structure of a sirtuin complexed with an acetylated protein substrate. This work identifies key residues of the sirtuin for substrate recognition and catalysis.
    • Avalos J.L., Celic I., Muhammad S., Cosgrove M.S., Boeke J.D., Wolberger C. Structure of a Sir2 enzyme bound to an acetylated p53 peptide. Mol Cell. 10:2002;523-535 The first report of the structure of a sirtuin complexed with an acetylated protein substrate. This work identifies key residues of the sirtuin for substrate recognition and catalysis.
    • (2002) Mol Cell , vol.10 , pp. 523-535
    • Avalos, J.L.1    Celic, I.2    Muhammad, S.3    Cosgrove, M.S.4    Boeke, J.D.5    Wolberger, C.6
  • 8
    • 0035868764 scopus 로고    scopus 로고
    • Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription
    • Muth V., Nadaud S., Grummt I., Voit R. Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. EMBO J. 20:2001;1353-1362.
    • (2001) EMBO J , vol.20 , pp. 1353-1362
    • Muth, V.1    Nadaud, S.2    Grummt, I.3    Voit, R.4
  • 9
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD(+)-dependent tubulin deacetylase
    • North B.J., Marshall B.L., Borra M.T., Denu J.M., Verdin E. The human Sir2 ortholog, SIRT2, is an NAD(+)-dependent tubulin deacetylase. Mol Cell. 11:2003;437-444.
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 10
    • 0037023326 scopus 로고    scopus 로고
    • The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation
    • Bell S.D., Botting C.H., Wardleworth B.N., Jackson S.P., White M.F. The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation. Science. 296:2002;148-151.
    • (2002) Science , vol.296 , pp. 148-151
    • Bell, S.D.1    Botting, C.H.2    Wardleworth, B.N.3    Jackson, S.P.4    White, M.F.5
  • 11
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • First report of a central metabolism enzyme whose activity is under sirtuin control. Mass fingerprinting was used to determine the precise location of the acetyl moiety on the protein. Acetylated enzyme was inactive, and its reactivation required NAD-dependent Sir2 deacetylase activity.
    • Starai V.J., Celic I., Cole R.N., Boeke J.D., Escalante-Semerena J.C. Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science. 298:2002;2390-2392 First report of a central metabolism enzyme whose activity is under sirtuin control. Mass fingerprinting was used to determine the precise location of the acetyl moiety on the protein. Acetylated enzyme was inactive, and its reactivation required NAD-dependent Sir2 deacetylase activity.
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 12
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • Lin S.J., Guarente L. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr Opin Cell Biol. 15:2003;241-246.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 13
    • 0346435109 scopus 로고    scopus 로고
    • Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
    • Jackson M.D., Schmidt M.T., Oppenheimer N.J., Denu J.M. Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J Biol Chem. 278:2003;50985-50998.
    • (2003) J Biol Chem , vol.278 , pp. 50985-50998
    • Jackson, M.D.1    Schmidt, M.T.2    Oppenheimer, N.J.3    Denu, J.M.4
  • 14
    • 0041571570 scopus 로고    scopus 로고
    • Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
    • Sauve A.A., Schramm V.L. Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry. Biochemistry. 42:2003;9249-9256.
    • (2003) Biochemistry , vol.42 , pp. 9249-9256
    • Sauve, A.A.1    Schramm, V.L.2
  • 15
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman K.J., Anderson R.M., Cohen H.Y., Latorre-Esteves M., Sinclair D.A. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem. 277:2002;45099-45107.
    • (2002) J Biol Chem , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 17
    • 0141677687 scopus 로고    scopus 로고
    • Longevity regulation in Saccharomyces cerevisiae: Linking metabolism, genome stability, and heterochromatin
    • Bitterman K.J., Medvedik O., Sinclair D.A. Longevity regulation in Saccharomyces cerevisiae: linking metabolism, genome stability, and heterochromatin. Microbiol Mol Biol Rev. 67:2003;376-399.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 376-399
    • Bitterman, K.J.1    Medvedik, O.2    Sinclair, D.A.3
  • 18
    • 0141781063 scopus 로고    scopus 로고
    • NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in Saccharomyces cerevisiae
    • Bedalov A., Hirao M., Posakony J., Nelson M., Simon J.A. NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+ levels in Saccharomyces cerevisiae. Mol Cell Biol. 23:2003;7044-7054.
    • (2003) Mol Cell Biol , vol.23 , pp. 7044-7054
    • Bedalov, A.1    Hirao, M.2    Posakony, J.3    Nelson, M.4    Simon, J.A.5
  • 19
    • 0037452897 scopus 로고    scopus 로고
    • The 1.75Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme a
    • This work provides insights into the conformational changes Ac-CoA synthetase undergoes during catalysis. The structure of the complex shows the acetylation site exposed during thioester bond formation.
    • Gulick A.M., Starai V.J., Horswill A.R., Homick K.M., Escalante-Semerena J.C. The 1.75Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A. Biochemistry. 42:2003;2866-2873 This work provides insights into the conformational changes Ac-CoA synthetase undergoes during catalysis. The structure of the complex shows the acetylation site exposed during thioester bond formation.
    • (2003) Biochemistry , vol.42 , pp. 2866-2873
    • Gulick, A.M.1    Starai, V.J.2    Horswill, A.R.3    Homick, K.M.4    Escalante-Semerena, J.C.5
  • 20
    • 0037133231 scopus 로고    scopus 로고
    • Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: Residue Lys592 is required for propionyl-AMP synthesis
    • Horswill A.R., Escalante-Semerena J.C. Characterization of the propionyl-CoA synthetase (PrpE) enzyme of Salmonella enterica: residue Lys592 is required for propionyl-AMP synthesis. Biochemistry. 41:2002;2379-2387.
    • (2002) Biochemistry , vol.41 , pp. 2379-2387
    • Horswill, A.R.1    Escalante-Semerena, J.C.2
  • 21
    • 0037297590 scopus 로고    scopus 로고
    • Short-chain fatty acid activation by acyl-coenzyme a synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae
    • Results of in vivo analysis of mutants supports the conclusion that sirtuins control acetyl-CoA synthetase activity in yeast and bacteria. Sir2 homologs Hst3 and Hst4 are predominantly responsible for controlling the activity of this enzyme in S. cerevisiae.
    • Starai V.J., Takahashi H., Boeke J.D., Escalante-Semerena J.C. Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae. Genetics. 163:2003;545-555 Results of in vivo analysis of mutants supports the conclusion that sirtuins control acetyl-CoA synthetase activity in yeast and bacteria. Sir2 homologs Hst3 and Hst4 are predominantly responsible for controlling the activity of this enzyme in S. cerevisiae.
    • (2003) Genetics , vol.163 , pp. 545-555
    • Starai, V.J.1    Takahashi, H.2    Boeke, J.D.3    Escalante-Semerena, J.C.4
  • 22
    • 0029134555 scopus 로고
    • ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme a synthetase, essential for growth on glucose
    • Van den Berg M.A., Steensma H.Y. ACS2, a Saccharomyces cerevisiae gene encoding acetyl-coenzyme A synthetase, essential for growth on glucose. Eur J Biochem. 231:1995;704-713.
    • (1995) Eur J Biochem , vol.231 , pp. 704-713
    • Van Den Berg, M.A.1    Steensma, H.Y.2
  • 23
    • 0027062806 scopus 로고
    • Cloning and disruption of a gene required for growth on acetate but not on ethanol: The acetyl-coenzyme a synthetase gene of Saccharomyces cerevisiae
    • De Virgilio C., Burckert N., Barth G., Neuhaus J.M., Boller T., Wiemken A. Cloning and disruption of a gene required for growth on acetate but not on ethanol: the acetyl-coenzyme A synthetase gene of Saccharomyces cerevisiae. Yeast. 8:1992;1043-1051.
    • (1992) Yeast , vol.8 , pp. 1043-1051
    • De Virgilio, C.1    Burckert, N.2    Barth, G.3    Neuhaus, J.M.4    Boller, T.5    Wiemken, A.6
  • 25
    • 0035819933 scopus 로고    scopus 로고
    • Molecular evolution of the AMP-forming acetyl-CoA synthetase
    • Karan D., David J.R., Capy P. Molecular evolution of the AMP-forming acetyl-CoA synthetase. Gene. 265:2001;95-101.
    • (2001) Gene , vol.265 , pp. 95-101
    • Karan, D.1    David, J.R.2    Capy, P.3
  • 26
    • 0035815751 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate
    • Fujino T., Kondo J., Ishikawa M., Morikawa K., Yamamoto T.T. Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate. J Biol Chem. 276:2001;11420-11426.
    • (2001) J Biol Chem , vol.276 , pp. 11420-11426
    • Fujino, T.1    Kondo, J.2    Ishikawa, M.3    Morikawa, K.4    Yamamoto, T.T.5
  • 27
    • 0034714382 scopus 로고    scopus 로고
    • Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins
    • Luong A., Hannah V.C., Brown M.S., Goldstein J.L. Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins. J Biol Chem. 275:2000;26458-26466.
    • (2000) J Biol Chem , vol.275 , pp. 26458-26466
    • Luong, A.1    Hannah, V.C.2    Brown, M.S.3    Goldstein, J.L.4
  • 28
    • 0035156443 scopus 로고    scopus 로고
    • Exploring the domain structure of modular nonribosomal peptide synthetases
    • Weber T., Marahiel M.A. Exploring the domain structure of modular nonribosomal peptide synthetases. Structure (Camb). 9:2001;R3-R9.
    • (2001) Structure (Camb) , vol.9 , pp. 3-R9
    • Weber, T.1    Marahiel, M.A.2
  • 29
    • 0037453033 scopus 로고    scopus 로고
    • Polyketide and non-ribosomal peptide synthases: Falling together by coming apart
    • Hutchinson C.R. Polyketide and non-ribosomal peptide synthases: falling together by coming apart. Proc Natl Acad Sci U S A. 100:2003;3010-3012.
    • (2003) Proc Natl Acad Sci U S a , vol.100 , pp. 3010-3012
    • Hutchinson, C.R.1
  • 30
    • 0034996629 scopus 로고    scopus 로고
    • Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis
    • Barak R., Eisenbach M. Acetylation of the response regulator, CheY, is involved in bacterial chemotaxis. Mol Microbiol. 40:2001;731-743.
    • (2001) Mol Microbiol , vol.40 , pp. 731-743
    • Barak, R.1    Eisenbach, M.2
  • 31
    • 0035951072 scopus 로고    scopus 로고
    • Chemistry of gene silencing: The mechanism of NAD(+)-dependent deacetylation reactions
    • Sauve A.A., Celic I., Avalos J., Deng H., Boeke J.D., Schramm V.L. Chemistry of gene silencing: the mechanism of NAD(+)-dependent deacetylation reactions. Biochemistry. 40:2001;15456-15463.
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1    Celic, I.2    Avalos, J.3    Deng, H.4    Boeke, J.D.5    Schramm, V.L.6
  • 32
    • 0037066738 scopus 로고    scopus 로고
    • Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD(+)-dependent deacetylases
    • Borra M.T., O'Neill F.J., Jackson M.D., Marshall B., Verdin E., Foltz K.R., Denu J.M. Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD(+)-dependent deacetylases. J Biol Chem. 277:2002;12632-12641.
    • (2002) J Biol Chem , vol.277 , pp. 12632-12641
    • Borra, M.T.1    O'Neill, F.J.2    Jackson, M.D.3    Marshall, B.4    Verdin, E.5    Foltz, K.R.6    Denu, J.M.7
  • 33
    • 0037166269 scopus 로고    scopus 로고
    • Structural identification of 2′- and 3′-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD(+)-dependent histone/protein deacetylases
    • Jackson M.D., Denu J.M. Structural identification of 2′- and 3′-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD(+)-dependent histone/protein deacetylases. J Biol Chem. 277:2002;18535-18544.
    • (2002) J Biol Chem , vol.277 , pp. 18535-18544
    • Jackson, M.D.1    Denu, J.M.2
  • 34
    • 0037033021 scopus 로고    scopus 로고
    • Analysis of O-acetyl-ADP-ribose as a target for nudix ADP-ribose hydrolases
    • Rafty L.A., Schmidt M.T., Perraud A.L., Scharenberg A.M., Denu J.M. Analysis of O-acetyl-ADP-ribose as a target for nudix ADP-ribose hydrolases. J Biol Chem. 277:2002;47114-47122.
    • (2002) J Biol Chem , vol.277 , pp. 47114-47122
    • Rafty, L.A.1    Schmidt, M.T.2    Perraud, A.L.3    Scharenberg, A.M.4    Denu, J.M.5
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.