메뉴 건너뛰기




Volumn 340, Issue 5, 2004, Pages 1005-1012

Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica

Author keywords

Ac CoA, acetyl CoA; acetyl AMP, acetyl adenosine monophosphate; Acs, acetyl CoA synthetase; enzyme activity control; gene silencing; Pat, protein acetyltransferase; post translational modification; protein acetyltransferase; sirtuins

Indexed keywords

ACETYL COENZYME A SYNTHETASE; ACYLTRANSFERASE; ENZYME; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; REGULATOR PROTEIN; SILENT INFORMATION REGULATOR PROTEIN 2; SIRTUIN; STRUCTURAL PROTEIN;

EID: 3242788065     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.010     Document Type: Article
Times cited : (229)

References (25)
  • 1
    • 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
  • 2
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • Fulco M., Schiltz R.L., Iezzi S., King M.T., Zhao P., Kashiwaya Y., et al. Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol. Cell. 12:2003;51-62
    • (2003) Mol. Cell , vol.12 , pp. 51-62
    • Fulco, M.1    Schiltz, R.L.2    Iezzi, S.3    King, M.T.4    Zhao, P.5    Kashiwaya, Y.6
  • 3
    • 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
  • 4
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • 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
    • (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
  • 5
    • 0037452897 scopus 로고    scopus 로고
    • The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme a
    • Gulick A.M., Starai V.J., Horswill A.R., Homick K.M., Escalante-Semerena J.C. The 1.75 Å crystal structure of acetyl-CoA synthetase bound to adenosine-5′-propylphosphate and coenzyme A. Biochemistry. 42:2003;2866-2873
    • (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
  • 6
    • 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
    • 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
    • (2003) Genetics , vol.163 , pp. 545-555
    • Starai, V.J.1    Takahashi, H.2    Boeke, J.D.3    Escalante-Semerena, J.C.4
  • 7
    • 0021681568 scopus 로고
    • New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition
    • Way J.C., Davis M.A., Morisato D., Roberts D.E., Kleckner N. New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene. 32:1984;369-379
    • (1984) Gene , vol.32 , pp. 369-379
    • Way, J.C.1    Davis, M.A.2    Morisato, D.3    Roberts, D.E.4    Kleckner, N.5
  • 8
    • 0015856129 scopus 로고
    • Phosphotransacetylase from Bacillus subtilis: Purification and physiological studies
    • Rado T.A., Hoch J.A. Phosphotransacetylase from Bacillus subtilis: purification and physiological studies. Biochim. Biophys. Acta. 321:1973;114-125
    • (1973) Biochim. Biophys. Acta , vol.321 , pp. 114-125
    • Rado, T.A.1    Hoch, J.A.2
  • 9
    • 0039445025 scopus 로고    scopus 로고
    • Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming) gene from the amitochondriate protist, Giardia lamblia
    • Sánchez L.B., Morrison H.G., Sogin M.L., Müller M. Cloning and sequencing of an acetyl-CoA synthetase (ADP-forming) gene from the amitochondriate protist, Giardia lamblia. Gene. 233:1999;225-321
    • (1999) Gene , vol.233 , pp. 225-321
    • Sánchez, L.B.1    Morrison, H.G.2    Sogin, M.L.3    Müller, M.4
  • 10
    • 0031039802 scopus 로고    scopus 로고
    • Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus
    • Glasemacher J., Bock A.K., Schmid R., Schönheit P. Purification and properties of acetyl-CoA synthetase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus. Eur. J. Biochem. 244:1997;561-567
    • (1997) Eur. J. Biochem. , vol.244 , pp. 561-567
    • Glasemacher, J.1    Bock, A.K.2    Schmid, R.3    Schönheit, P.4
  • 11
    • 0039765216 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase from the amitochondriate eukaryote Giardia lamblia belongs to the newly recognized superfamily of acyl-CoA synthetases (Nucleoside diphosphate-forming)
    • Sánchez L.B., Galperin M.Y., Müller M. Acetyl-CoA synthetase from the amitochondriate eukaryote Giardia lamblia belongs to the newly recognized superfamily of acyl-CoA synthetases (Nucleoside diphosphate-forming). J. Biol. Chem. 275:2000;5794-5803
    • (2000) J. Biol. Chem. , vol.275 , pp. 5794-5803
    • Sánchez, L.B.1    Galperin, M.Y.2    Müller, M.3
  • 12
    • 0025977083 scopus 로고
    • Functional consequences of substitution of the active site (phospho)histidine residue of Escherichia coli succinyl-CoA synthetase
    • Majumdar R., Guest J.R., Bridger W.A. Functional consequences of substitution of the active site (phospho)histidine residue of Escherichia coli succinyl-CoA synthetase. Biochim. Biophys. Acta. 1076:1991;86-90
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 86-90
    • Majumdar, R.1    Guest, J.R.2    Bridger, W.A.3
  • 13
    • 0343290301 scopus 로고    scopus 로고
    • Purification and characterization of the acetate forming enzyme, acetyl-CoA synthetase (ADP-forming) from the amitochondriate protist, Giardia lamblia
    • Sanchez L.B., Muller M. Purification and characterization of the acetate forming enzyme, acetyl-CoA synthetase (ADP-forming) from the amitochondriate protist, Giardia lamblia. FEBS Letters. 378:1996;240-244
    • (1996) FEBS Letters , vol.378 , pp. 240-244
    • Sanchez, L.B.1    Muller, M.2
  • 16
    • 0014992845 scopus 로고
    • A method for detection of phage mutants with altered transduction ability
    • Schmieger H. A method for detection of phage mutants with altered transduction ability. Mol. Gen. Genet. 100:1971;378-381
    • (1971) Mol. Gen. Genet. , vol.100 , pp. 378-381
    • Schmieger, H.1
  • 17
    • 0015934081 scopus 로고
    • The origin of DNA in transducing particles of P22 mutants with increased transduction frequencies (HT-mutants)
    • Schmieger H., Bakhaus H. The origin of DNA in transducing particles of P22 mutants with increased transduction frequencies (HT-mutants). Mol. Gen. Genet. 120:1973;181-190
    • (1973) Mol. Gen. Genet. , vol.120 , pp. 181-190
    • Schmieger, H.1    Bakhaus, H.2
  • 18
    • 0015445137 scopus 로고
    • Specialized transduction of tetracycline resistance by phage P22 in Salmonella typhimurium. II. Properties of a high transducing lysate
    • Chan R.K., Botstein D., Watanabe T., Ogata Y. Specialized transduction of tetracycline resistance by phage P22 in Salmonella typhimurium. II. Properties of a high transducing lysate. Virology. 50:1972;883-898
    • (1972) Virology , vol.50 , pp. 883-898
    • Chan, R.K.1    Botstein, D.2    Watanabe, T.3    Ogata, Y.4
  • 19
    • 0027137711 scopus 로고
    • Amplifying DNA with arbitrary oligonucleotide primers
    • Caetano-Annoles G. Amplifying DNA with arbitrary oligonucleotide primers. PCR Methods Appl. 3:1993;85-92
    • (1993) PCR Methods Appl. , vol.3 , pp. 85-92
    • Caetano-Annoles, G.1
  • 20
    • 0031970701 scopus 로고    scopus 로고
    • Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: A genetic analysis
    • O'Toole G.A., Kolter R. Initiation of biofilm formation in Pseudomonas fluorescens WCS365 proceeds via multiple, convergent signalling pathways: a genetic analysis. Mol. Microbiol. 28:1998;449-461
    • (1998) Mol. Microbiol. , vol.28 , pp. 449-461
    • O'Toole, G.A.1    Kolter, R.2
  • 21
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage and structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage and structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0001870287 scopus 로고
    • Detection of proteins
    • F.A. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, & K. Struhl. New York: Wiley Interscience. 2 vols
    • Sasse J. Detection of proteins. Ausubel F.A., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Struhl K. Current Protocols in Molecular Biology. Current Protocols in Molecular Biology. vol. 1:1991;10.6.1-10.6.8 Wiley Interscience, New York. 2 vols
    • (1991) Current Protocols in Molecular Biology. Current Protocols in Molecular Biology , vol.1 , pp. 1061-1068
    • Sasse, J.1
  • 24
    • 77957001185 scopus 로고
    • Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods
    • J.M. Lowenstein. New York: Academic Press
    • Williamson J.R., Corkey B.E. Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods. Lowenstein J.M. Methods in Enzymology. Methods in Enzymology. vol. XIII:1969;494-497 Academic Press, New York
    • (1969) Methods in Enzymology. Methods in Enzymology , vol.13 , pp. 494-497
    • Williamson, J.R.1    Corkey, B.E.2
  • 25
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.