메뉴 건너뛰기




Volumn 82, Issue 5, 2011, Pages 1110-1128

cAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A SYNTHETASE; ACYLTRANSFERASE; C REACTIVE PROTEIN; CYCLIC AMP; HISTONE ACETYLTRANSFERASE GCN5; HISTONE DEACETYLASE;

EID: 82155175630     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07873.x     Document Type: Article
Times cited : (72)

References (47)
  • 1
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection
    • Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., etal. (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2: 2006.0008.
    • (2006) Mol Syst Biol , vol.2 , pp. 20060008
    • Baba, T.1    Ara, T.2    Hasegawa, M.3    Takai, Y.4    Okumura, Y.5    Baba, M.6
  • 2
    • 71149118041 scopus 로고    scopus 로고
    • An insight into the role of phosphotransacetylase (pta) and the acetate/acetyl-CoA node in Escherichia coli
    • Castaño-Cerezo, S., Pastor, J., Renilla, S., Bernal, V., Iborra, J., and Canovas, M. (2009) An insight into the role of phosphotransacetylase (pta) and the acetate/acetyl-CoA node in Escherichia coli. Microb Cell Fact 8: 54.
    • (2009) Microb Cell Fact , vol.8 , pp. 54
    • Castaño-Cerezo, S.1    Pastor, J.2    Renilla, S.3    Bernal, V.4    Iborra, J.5    Canovas, M.6
  • 3
    • 79953058855 scopus 로고    scopus 로고
    • In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate
    • Chan, C.H., Garrity, J., Crosby, H.A., and Escalante-Semerena, J.C. (2011) In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate. Mol Microbiol 80: 168-183.
    • (2011) Mol Microbiol , vol.80 , pp. 168-183
    • Chan, C.H.1    Garrity, J.2    Crosby, H.A.3    Escalante-Semerena, J.C.4
  • 4
    • 77952222270 scopus 로고    scopus 로고
    • Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris
    • Crosby, H.A., Heiniger, E.K., Harwood, C.S., and Escalante-Semerena, J.C. (2010) Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris. Mol Microbiol 76: 874-888.
    • (2010) Mol Microbiol , vol.76 , pp. 874-888
    • Crosby, H.A.1    Heiniger, E.K.2    Harwood, C.S.3    Escalante-Semerena, J.C.4
  • 5
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 6
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel, T., Deng, C.-X., and Mostoslavsky, R. (2009) Recent progress in the biology and physiology of sirtuins. Nature 460: 587-591.
    • (2009) Nature , vol.460 , pp. 587-591
    • Finkel, T.1    Deng, C.-X.2    Mostoslavsky, R.3
  • 7
    • 65249173472 scopus 로고    scopus 로고
    • Carbon catabolite control of the metabolic network in Bacillus subtilis
    • Fujita, Y. (2009) Carbon catabolite control of the metabolic network in Bacillus subtilis. Biosci Biotechnol Biochem 73: 245-259.
    • (2009) Biosci Biotechnol Biochem , vol.73 , pp. 245-259
    • Fujita, Y.1
  • 8
    • 78651299341 scopus 로고    scopus 로고
    • RegulonDB version 7.0: transcriptional regulation of Escherichia coli K-12 integrated within genetic sensory response units (Gensor Units)
    • Gama-Castro, S., Salgado, H., Peralta-Gil, M., Santos-Zavaleta, A., Muñiz-Rascado, L., Solano-Lira, H., etal. (2011) RegulonDB version 7.0: transcriptional regulation of Escherichia coli K-12 integrated within genetic sensory response units (Gensor Units). Nucleic Acids Res 39: D98-D105.
    • (2011) Nucleic Acids Res , vol.39
    • Gama-Castro, S.1    Salgado, H.2    Peralta-Gil, M.3    Santos-Zavaleta, A.4    Muñiz-Rascado, L.5    Solano-Lira, H.6
  • 9
    • 47249127304 scopus 로고    scopus 로고
    • Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme a synthetase (AcsA) in Bacillus subtilis
    • Gardner, J.G., and Escalante-Semerena, J.C. (2008) Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme a synthetase (AcsA) in Bacillus subtilis. J Bacteriol 190: 5132-5136.
    • (2008) J Bacteriol , vol.190 , pp. 5132-5136
    • Gardner, J.G.1    Escalante-Semerena, J.C.2
  • 10
    • 63049137277 scopus 로고    scopus 로고
    • In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN gene (formerly yhdZ), and functions encoded by the acuABC genes control the activity of acetyl coenzyme A synthetase
    • Gardner, J.G., and Escalante-Semerena, J.C. (2009) In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN gene (formerly yhdZ), and functions encoded by the acuABC genes control the activity of acetyl coenzyme A synthetase. J Bacteriol 191: 1749-1755.
    • (2009) J Bacteriol , vol.191 , pp. 1749-1755
    • Gardner, J.G.1    Escalante-Semerena, J.C.2
  • 11
    • 33746620532 scopus 로고    scopus 로고
    • Control of acetyl-coenzyme A synthetase (AcsA) activity by acetylation/deacetylation without NAD(+) involvement in Bacillus subtilis
    • Gardner, J.G., Grundy, F.J., Henkin, T.M., and Escalante-Semerena, J.C. (2006) Control of acetyl-coenzyme A synthetase (AcsA) activity by acetylation/deacetylation without NAD(+) involvement in Bacillus subtilis. J Bacteriol 188: 5460-5468.
    • (2006) J Bacteriol , vol.188 , pp. 5460-5468
    • Gardner, J.G.1    Grundy, F.J.2    Henkin, T.M.3    Escalante-Semerena, J.C.4
  • 12
    • 0028136632 scopus 로고
    • Catabolite regulation of Bacillus subtilis acetate and acetoin utilization genes by CcpA
    • Grundy, F.J., Turinsky, A.J., and Henkin, T.M. (1994) Catabolite regulation of Bacillus subtilis acetate and acetoin utilization genes by CcpA. J Bacteriol 176: 4527-4533.
    • (1994) J Bacteriol , vol.176 , pp. 4527-4533
    • Grundy, F.J.1    Turinsky, A.J.2    Henkin, T.M.3
  • 13
    • 0030057004 scopus 로고    scopus 로고
    • The role of the CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis
    • Henkin, T.M. (1996) The role of the CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis. FEMS Microbiol Lett 135: 9-15.
    • (1996) FEMS Microbiol Lett , vol.135 , pp. 9-15
    • Henkin, T.M.1
  • 14
    • 0032826179 scopus 로고    scopus 로고
    • Identifying DNA and protein patterns with statistically significant alignments of multiple sequences
    • Hertz, G.Z., and Stormo, G.D. (1999) Identifying DNA and protein patterns with statistically significant alignments of multiple sequences. Bioinformatics 15: 563-577.
    • (1999) Bioinformatics , vol.15 , pp. 563-577
    • Hertz, G.Z.1    Stormo, G.D.2
  • 15
    • 77954013335 scopus 로고    scopus 로고
    • Bacterial protein acetylation: the dawning of a new age
    • Hu, L.I., Lima, B.P., and Wolfe, A.J. (2010) Bacterial protein acetylation: the dawning of a new age. Mol Microbiol 77: 15-21.
    • (2010) Mol Microbiol , vol.77 , pp. 15-21
    • Hu, L.I.1    Lima, B.P.2    Wolfe, A.J.3
  • 16
    • 0141758085 scopus 로고    scopus 로고
    • Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals
    • Huerta, A.M., and Collado-Vides, J. (2003) Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals. J Mol Biol 333: 261-278.
    • (2003) J Mol Biol , vol.333 , pp. 261-278
    • Huerta, A.M.1    Collado-Vides, J.2
  • 18
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim, S.C., Sprung, R., Chen, Y., Xu, Y., Ball, H., Pei, J., etal. (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 23: 607-618.
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5    Pei, J.6
  • 20
    • 0033621553 scopus 로고    scopus 로고
    • 70 is the principal sigma factor responsible for transcription of acs, which encodes acetyl coenzyme A synthetase in Escherichia coli
    • 70 is the principal sigma factor responsible for transcription of acs, which encodes acetyl coenzyme A synthetase in Escherichia coli. J Bacteriol 182: 551-554.
    • (2000) J Bacteriol , vol.182 , pp. 551-554
    • Kumari, S.1    Simel, E.J.2    Wolfe, A.J.3
  • 21
    • 0020355238 scopus 로고
    • A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle
    • LaPorte, D.C., and Koshland, D.E. (1982) A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycle. Nature 300: 458-460.
    • (1982) Nature , vol.300 , pp. 458-460
    • LaPorte, D.C.1    Koshland, D.E.2
  • 22
    • 77952826169 scopus 로고    scopus 로고
    • CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY
    • Li, R., Gu, J., Chen, Y.-Y., Xiao, C.-L., Wang, L.-W., Zhang, Z.-P., etal. (2010) CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY. Mol Microbiol 76: 1162-1174.
    • (2010) Mol Microbiol , vol.76 , pp. 1162-1174
    • Li, R.1    Gu, J.2    Chen, Y.-Y.3    Xiao, C.-L.4    Wang, L.-W.5    Zhang, Z.-P.6
  • 23
    • 33746718715 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase overexpression in Escherichia coli demonstrates more efficient acetate assimilation and lower acetate accumulation: a potential tool in metabolic engineering
    • Lin, H., Castro, N.M., Bennett, G.N., and San, K.Y. (2006) Acetyl-CoA synthetase overexpression in Escherichia coli demonstrates more efficient acetate assimilation and lower acetate accumulation: a potential tool in metabolic engineering. Appl Microbiol Biotechnol 71: 870-874.
    • (2006) Appl Microbiol Biotechnol , vol.71 , pp. 870-874
    • Lin, H.1    Castro, N.M.2    Bennett, G.N.3    San, K.Y.4
  • 25
    • 39749166860 scopus 로고    scopus 로고
    • Phosphoproteome analysis of E.coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation
    • Macek, B., Gnad, F., Soufi, B., Kumar, C., Olsen, J.V., Mijakovic, I., and Mann, M. (2008) Phosphoproteome analysis of E.coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol Cell Proteomics 7: 299-307.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 299-307
    • Macek, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4    Olsen, J.V.5    Mijakovic, I.6    Mann, M.7
  • 26
    • 70449380939 scopus 로고    scopus 로고
    • Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E.coli
    • Mendoza-Vargas, A., Olvera, L., Olvera, M., Grande, R., Vega-Alvarado, L., Taboada, B., etal. (2009) Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E.coli. PLoS ONE 4: e7526.
    • (2009) PLoS ONE , vol.4
    • Mendoza-Vargas, A.1    Olvera, L.2    Olvera, M.3    Grande, R.4    Vega-Alvarado, L.5    Taboada, B.6
  • 27
    • 77955285819 scopus 로고    scopus 로고
    • cAMP-regulated protein lysine acetylases in mycobacteria
    • Nambi, S., Basu, N., and Visweswariah, S.S. (2010) cAMP-regulated protein lysine acetylases in mycobacteria. J Biol Chem 285: 24313-24323.
    • (2010) J Biol Chem , vol.285 , pp. 24313-24323
    • Nambi, S.1    Basu, N.2    Visweswariah, S.S.3
  • 28
    • 77449116892 scopus 로고    scopus 로고
    • Acetylation goes global: the emergence of acetylation biology
    • Norris, K., Lee, J., and Yao, T. (2009) Acetylation goes global: the emergence of acetylation biology. Sci Signal 2: 1-7.
    • (2009) Sci Signal , vol.2 , pp. 1-7
    • Norris, K.1    Lee, J.2    Yao, T.3
  • 29
    • 0030960672 scopus 로고    scopus 로고
    • Transcriptional activation by recruitment
    • Ptashne, M., and Gann, A. (1997) Transcriptional activation by recruitment. Nature 386: 569-577.
    • (1997) Nature , vol.386 , pp. 569-577
    • Ptashne, M.1    Gann, A.2
  • 31
    • 0029039486 scopus 로고
    • Protein phosphorylation and regulation of carbon metabolism in Gram-negative versus Gram-positive bacteria
    • Saier, M.H., Jr, Chauvaux, S., Deutscher, J., Reizer, J., and Ye, J.-J. (1995) Protein phosphorylation and regulation of carbon metabolism in Gram-negative versus Gram-positive bacteria. Trends Biochem Sci 20: 267-271.
    • (1995) Trends Biochem Sci , vol.20 , pp. 267-271
    • Saier Jr, M.H.1    Chauvaux, S.2    Deutscher, J.3    Reizer, J.4    Ye, J.-J.5
  • 33
    • 50149103440 scopus 로고    scopus 로고
    • Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
    • Schlicker, C., Gertz, M., Papatheodorou, P., Kachholz, B., Becker, C.F.W., and Steegborn, C. (2008) Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J Mol Biol 382: 790-801.
    • (2008) J Mol Biol , vol.382 , pp. 790-801
    • Schlicker, C.1    Gertz, M.2    Papatheodorou, P.3    Kachholz, B.4    Becker, C.F.W.5    Steegborn, C.6
  • 34
    • 34447326690 scopus 로고    scopus 로고
    • The multiple roles of CRP at the complex acs promoter depend on activation region 2 and IHF
    • Sclavi, B., Beatty, C.M., Thach, D.S., Fredericks, C.E., Buckle, M., and Wolfe, A.J. (2007) The multiple roles of CRP at the complex acs promoter depend on activation region 2 and IHF. Mol Microbiol 65: 425-440.
    • (2007) Mol Microbiol , vol.65 , pp. 425-440
    • Sclavi, B.1    Beatty, C.M.2    Thach, D.S.3    Fredericks, C.E.4    Buckle, M.5    Wolfe, A.J.6
  • 35
    • 3242788065 scopus 로고    scopus 로고
    • Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica
    • Starai, V.J., and Escalante-Semerena, J.C. (2004a) Identification of the protein acetyltransferase (Pat) enzyme that acetylates acetyl-CoA synthetase in Salmonella enterica. J Mol Biol 340: 1005-1012.
    • (2004) J Mol Biol , vol.340 , pp. 1005-1012
    • Starai, V.J.1    Escalante-Semerena, J.C.2
  • 36
  • 38
    • 79954582107 scopus 로고    scopus 로고
    • Control of protein function by reversible Nε-lysine acetylation in bacteria
    • Thao, S., and Escalante-Semerena, J.C. (2011) Control of protein function by reversible Nε-lysine acetylation in bacteria. Curr Opin Microbiol 14: 200-204.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 200-204
    • Thao, S.1    Escalante-Semerena, J.C.2
  • 39
    • 79251477191 scopus 로고    scopus 로고
    • N epsilon lysine acetylation of a bacterial transcription factor inhibits Its DNA-binding activity
    • Thao, S., Chen, C.-S., Zhu, H., and Escalante-Semerena, J.C. (2010) N epsilon lysine acetylation of a bacterial transcription factor inhibits Its DNA-binding activity. PLoS ONE 5: e15123.
    • (2010) PLoS ONE , vol.5
    • Thao, S.1    Chen, C.-S.2    Zhu, H.3    Escalante-Semerena, J.C.4
  • 40
    • 78649369566 scopus 로고    scopus 로고
    • Biologically active isoforms of CobB sirtuin deacetylase in Salmonella enterica and Erwinia amylovora
    • Tucker, A.C., and Escalante-Semerena, J.C. (2010) Biologically active isoforms of CobB sirtuin deacetylase in Salmonella enterica and Erwinia amylovora. J Bacteriol 192: 6200-6208.
    • (2010) J Bacteriol , vol.192 , pp. 6200-6208
    • Tucker, A.C.1    Escalante-Semerena, J.C.2
  • 41
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang, Q., Zhang, Y., Yang, C., Xiong, H., Lin, Y., Yao, J., etal. (2010) Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 327: 1004-1007.
    • (2010) Science , vol.327 , pp. 1004-1007
    • Wang, Q.1    Zhang, Y.2    Yang, C.3    Xiong, H.4    Lin, Y.5    Yao, J.6
  • 42
    • 0348109341 scopus 로고    scopus 로고
    • CcpA-dependent carbon catabolite repression in bacteria
    • Warner, J.B., and Lolkema, J.S. (2003) CcpA-dependent carbon catabolite repression in bacteria. Microbiol Mol Biol Rev 67: 475-490.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 475-490
    • Warner, J.B.1    Lolkema, J.S.2
  • 44
    • 56649114286 scopus 로고    scopus 로고
    • The diversity of lysine-acetylated proteins in Escherichia coli
    • Yu, B.J., Kim, J.A., Moon, J.H., Ryu, S.E., and Pan, J.G. (2008) The diversity of lysine-acetylated proteins in Escherichia coli. J Microbiol Biotechnol 18: 1529-1536.
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 1529-1536
    • Yu, B.J.1    Kim, J.A.2    Moon, J.H.3    Ryu, S.E.4    Pan, J.G.5
  • 45
    • 33746415885 scopus 로고    scopus 로고
    • A comprehensive library of fluorescent transcriptional reporters for Escherichia coli
    • Zaslaver, A., Bren, A., Ronen, M., Itzkovitz, S., Kikoin, I., Shavit, S., etal. (2006) A comprehensive library of fluorescent transcriptional reporters for Escherichia coli. Nat Methods 3: 623-628.
    • (2006) Nat Methods , vol.3 , pp. 623-628
    • Zaslaver, A.1    Bren, A.2    Ronen, M.3    Itzkovitz, S.4    Kikoin, I.5    Shavit, S.6
  • 46
    • 61649089277 scopus 로고    scopus 로고
    • Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli
    • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., etal. (2009) Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics 8: 215-225.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 215-225
    • Zhang, J.1    Sprung, R.2    Pei, J.3    Tan, X.4    Kim, S.5    Zhu, H.6
  • 47
    • 1542298916 scopus 로고    scopus 로고
    • Structure and substrate binding properties of CobB, a Sir2 homolog protein deacetylase from Escherichia coli
    • Zhao, K., Chai, X., and Marmorstein, R. (2004) Structure and substrate binding properties of CobB, a Sir2 homolog protein deacetylase from Escherichia coli. J Mol Biol 337: 731-741.
    • (2004) J Mol Biol , vol.337 , pp. 731-741
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.