메뉴 건너뛰기




Volumn 289, Issue 39, 2014, Pages 27034-27045

Allosteric regulation of a protein acetyltransferase in micromonospora aurantiaca by the amino acids cysteine and Arginine

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; ARGININE; BACTERIA;

EID: 84907588701     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.579078     Document Type: Article
Times cited : (23)

References (38)
  • 1
    • 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., and Escalante-Semerena, J. C. (2002) Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298, 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
  • 2
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase
    • Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S., and Verdin, E. (2006) Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase. Proc. Natl. Acad. Sci. U.S.A. 103, 10224-10229
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 3
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows, W. C., Lee, S., and Denu, J. M. (2006) Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. U.S.A. 103, 10230-10235
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 4
    • 82155175630 scopus 로고    scopus 로고
    • CAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli
    • Castaño-Cerezo, S., Bernal, V., Blanco-Catalá, J., Iborra, J. L., and Cánovas, M. (2011) cAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli. Mol. Microbiol. 82, 1110-1128
    • (2011) Mol. Microbiol , vol.82 , pp. 1110-1128
    • Castaño-Cerezo, S.1    Bernal, V.2    Blanco-Catalá, J.3    Iborra, J.L.4    Cánovas, M.5
  • 5
    • 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
  • 6
    • 79959791094 scopus 로고    scopus 로고
    • Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP
    • Xu, H., Hegde, S. S., and Blanchard, J. S. (2011) Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP. Biochemistry 50, 5883-5892
    • (2011) Biochemistry , vol.50 , pp. 5883-5892
    • Xu, H.1    Hegde, S.S.2    Blanchard, J.S.3
  • 7
    • 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
  • 8
    • 33845944628 scopus 로고    scopus 로고
    • The ACT Domain: A small molecule binding domain and its role as a common regulatory element
    • Grant, G. A. (2006) The ACT Domain: A small molecule binding domain and its role as a common regulatory element. J. Biol. Chem. 281, 33825-33829
    • (2006) J. Biol. Chem , vol.281 , pp. 33825-33829
    • Grant, G.A.1
  • 9
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database search
    • Aravind, L., and Koonin, E. V. (1999) Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database search. J. Mol. Biol. 287, 1023-1040
    • (1999) J. Mol. Biol , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 10
    • 77149155971 scopus 로고    scopus 로고
    • Micromonospora: An important microbe for biomedicine and potentially for biocontrol and biofuels
    • Hirsch, A. M., and Valdés, M. (2010) Micromonospora: an important microbe for biomedicine and potentially for biocontrol and biofuels. Soil Biol. Biochem. 42, 536-542
    • (2010) Soil Biol. Biochem , vol.42 , pp. 536-542
    • Hirsch, A.M.1    Valdés, M.2
  • 11
    • 84883555849 scopus 로고    scopus 로고
    • Quantitative monitoring of 2-oxoglutarate in Escherichia coli cells by a fluorescence resonance energy transfer-based biosensor
    • Zhang, C., Wei, Z. H., and Ye, B. C. (2013) Quantitative monitoring of 2-oxoglutarate in Escherichia coli cells by a fluorescence resonance energy transfer-based biosensor. Appl. Microbiol. Biotechnol. 97, 8307-8316
    • (2013) Appl. Microbiol. Biotechnol , vol.97 , pp. 8307-8316
    • Zhang, C.1    Wei, Z.H.2    Ye, B.C.3
  • 12
    • 23944525341 scopus 로고    scopus 로고
    • Assays for mechanistic investigations of protein/histone acetyltransferases
    • Berndsen, C. E., and Denu, J. M. (2005) Assays for mechanistic investigations of protein/histone acetyltransferases. Methods 36, 321-331
    • (2005) Methods , vol.36 , pp. 321-331
    • Berndsen, C.E.1    Denu, J.M.2
  • 13
    • 0034194489 scopus 로고    scopus 로고
    • A continuous, nonradioac-tive assay for histone acetyltransferases
    • Kim, Y., Tanner, K. G., and Denu, J. M. (2000) A continuous, nonradioac-tive assay for histone acetyltransferases. Anal. Biochem. 280, 308-314
    • (2000) Anal. Biochem , vol.280 , pp. 308-314
    • Kim, Y.1    Tanner, K.G.2    Denu, J.M.3
  • 14
    • 15244344475 scopus 로고    scopus 로고
    • Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism
    • Liberles, J. S., Thórólfsson, M., and Martínez, A. (2005) Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism. Amino Acids 28, 1-12
    • (2005) Amino Acids , vol.28 , pp. 1-12
    • Liberles, J.S.1    Thórólfsson, M.2    Martínez, A.3
  • 15
    • 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. (2004) 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
  • 16
    • 84860868848 scopus 로고    scopus 로고
    • System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases
    • Crosby, H. A., Pelletier, D. A., Hurst, G. B., and Escalante-Semerena, J. C. (2012) System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. J. Biol. Chem. 287, 15590-15601
    • (2012) J. Biol. Chem , vol.287 , pp. 15590-15601
    • Crosby, H.A.1    Pelletier, D.A.2    Hurst, G.B.3    Escalante-Semerena, J.C.4
  • 17
    • 84871407978 scopus 로고    scopus 로고
    • Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans
    • Tucker, A. C., and Escalante-Semerena, J. C. (2013) Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans. Mol. Microbiol. 87, 152-167
    • (2013) Mol. Microbiol , vol.87 , pp. 152-167
    • Tucker, A.C.1    Escalante-Semerena, J.C.2
  • 18
    • 0034698085 scopus 로고    scopus 로고
    • Kinetic mechanism of the histone acetyltransferase GCN5 from yeast
    • Tanner, K. G., Langer, M. R., Kim, Y., and Denu, J. M. (2000) Kinetic mechanism of the histone acetyltransferase GCN5 from yeast. J. Biol. Chem. 275, 22048-22055
    • (2000) J. Biol. Chem , vol.275 , pp. 22048-22055
    • Tanner, K.G.1    Langer, M.R.2    Kim, Y.3    Denu, J.M.4
  • 19
    • 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
  • 20
    • 0035996735 scopus 로고    scopus 로고
    • Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana
    • Paris, S., Wessel, P. M., and Dumas, R. (2002) Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana. Protein Expression Purif. 24, 105-110
    • (2002) Protein Expression Purif , vol.24 , pp. 105-110
    • Paris, S.1    Wessel, P.M.2    Dumas, R.3
  • 21
    • 0038475950 scopus 로고    scopus 로고
    • Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine
    • Paris, S., Viemon, C., Curien, G., and Dumas, R. (2003) Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine. J. Biol. Chem. 278, 5361-5366
    • (2003) J. Biol. Chem , vol.278 , pp. 5361-5366
    • Paris, S.1    Viemon, C.2    Curien, G.3    Dumas, R.4
  • 22
    • 29244471699 scopus 로고    scopus 로고
    • Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms
    • Curien, G., Ravanel, S., Robert, M., and Dumas, R. (2005) Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. J. Biol. Chem. 280, 41178-41183
    • (2005) J. Biol. Chem , vol.280 , pp. 41178-41183
    • Curien, G.1    Ravanel, S.2    Robert, M.3    Dumas, R.4
  • 23
    • 33745803816 scopus 로고    scopus 로고
    • A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase
    • Mas-Droux, C., Curien, G., Robert-Genthon, M., Laurencin, M., Ferrer, J.-L., and Dumas, R. (2006) A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase. Plant Cell 18, 1681-1692
    • (2006) Plant Cell , vol.18 , pp. 1681-1692
    • Mas-Droux, C.1    Curien, G.2    Robert-Genthon, M.3    Laurencin, M.4    Ferrer, J.-L.5    Dumas, R.6
  • 24
    • 33845651790 scopus 로고    scopus 로고
    • Allosteric monofunctional aspartate kinases from Arabidopsis
    • Curien, G., Laurencin, M., Robert-Genthon, M., and Dumas, R. (2007) Allosteric monofunctional aspartate kinases from Arabidopsis. FEBS J. 274, 164-176
    • (2007) FEBS J , vol.274 , pp. 164-176
    • Curien, G.1    Laurencin, M.2    Robert-Genthon, M.3    Dumas, R.4
  • 25
    • 0028923757 scopus 로고
    • Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli
    • Nagy, P. L., Marolewski, A., Benkovic, S. J., and Zalkin, H. (1995) Formyltetrahydrofolate hydrolase, a regulatory enzyme that functions to balance pools of tetrahydrofolate and one-carbon tetrahydrofolate adducts in Escherichia coli. J. Bacteriol. 177, 1292-1298
    • (1995) J. Bacteriol , vol.177 , pp. 1292-1298
    • Nagy, P.L.1    Marolewski, A.2    Benkovic, S.J.3    Zalkin, H.4
  • 26
    • 0017711171 scopus 로고
    • Threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12 kinetic and spectroscopic effects upon binding of serine and threonine
    • Costrejean, J. M., and Truffa-Bachi, P. (1977) Threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12 kinetic and spectroscopic effects upon binding of serine and threonine. J. Biol. Chem. 252, 5332-5336
    • (1977) J. Biol. Chem , vol.252 , pp. 5332-5336
    • Costrejean, J.M.1    Truffa-Bachi, P.2
  • 28
    • 0037336269 scopus 로고    scopus 로고
    • High levels of intracellular cysteine promote oxidative DNA damage by driving the fenton reaction
    • Park, S., and Imlay, J. A. (2003) High levels of intracellular cysteine promote oxidative DNA damage by driving the fenton reaction. J. Bacteriol. 185, 1942-1950
    • (2003) J. Bacteriol , vol.185 , pp. 1942-1950
    • Park, S.1    Imlay, J.A.2
  • 29
    • 44449126770 scopus 로고    scopus 로고
    • Arginine biosynthesis in Escherichia coli: Experimental perturbation and mathematical modeling
    • Caldara, M., Dupont, G., Leroy, F., Goldbeter, A., De Vuyst, L., and Cunin, R. (2008) Arginine biosynthesis in Escherichia coli: experimental perturbation and mathematical modeling. J. Biol. Chem. 283, 6347-6358
    • (2008) J. Biol. Chem , vol.283 , pp. 6347-6358
    • Caldara, M.1    Dupont, G.2    Leroy, F.3    Goldbeter, A.4    De Vuyst, L.5    Cunin, R.6
  • 30
    • 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., Liu, C. F., Grishin, N. V., and Zhao, Y. (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    Liu, C.F.7    Grishin, N.V.8    Zhao, Y.9
  • 31
    • 84873343462 scopus 로고    scopus 로고
    • Comprehensive profiling of protein lysine acetylation in Escherichia coli
    • Zhang, K., Zheng, S., Yang, J. S., Chen, Y., and Cheng, Z. (2013) Comprehensive profiling of protein lysine acetylation in Escherichia coli. J. Proteome Res. 12, 844-851
    • (2013) J. Proteome Res , vol.12 , pp. 844-851
    • Zhang, K.1    Zheng, S.2    Yang, J.S.3    Chen, Y.4    Cheng, Z.5
  • 33
    • 84878629096 scopus 로고    scopus 로고
    • The acetylproteome of Gram-positive model bacterium Bacillus subtilis
    • Kim, D., Yu, B. J., Kim, J. A., Lee, Y. J., Choi, S. G., Kang, S., and Pan, J. G. (2013) The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Proteomics 13, 1726-1736
    • (2013) Proteomics , vol.13 , pp. 1726-1736
    • Kim, D.1    Yu, B.J.2    Kim, J.A.3    Lee, Y.J.4    Choi, S.G.5    Kang, S.6    Pan, J.G.7
  • 34
    • 84881243155 scopus 로고    scopus 로고
    • Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus
    • Lee, D. W., Kim, D., Lee, Y. J., Kim, J. A., Choi, J. Y., Kang, S. H., and Pan, J. G. (2013) Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus. Proteomics 13, 2278-2282
    • (2013) Proteomics , vol.13 , pp. 2278-2282
    • Lee, D.W.1    Kim, D.2    Lee, Y.J.3    Kim, J.A.4    Choi, J.Y.5    Kang, S.H.6    Pan, J.G.7
  • 35
    • 84883772266 scopus 로고    scopus 로고
    • Acetylome with structure mapping reveals the significance of lysine acetylation in Thermus thermophiles
    • Okanishi, H., Kim, K., Masui, R., and Kuramitsu, S. (2013) Acetylome with structure mapping reveals the significance of lysine acetylation in Thermus thermophiles. J. Proteome Res. 12, 3952-3968
    • (2013) J. Proteome Res , vol.12 , pp. 3952-3968
    • Okanishi, H.1    Kim, K.2    Masui, R.3    Kuramitsu, S.4
  • 36
    • 84905454949 scopus 로고    scopus 로고
    • Acetyl coenzyme A synthetase is acetylated on multiple lysine residues by a protein acetyltransferase with a single Gcn5-typeN-acetyltransferase (GNAT) domain in Saccharopolyspora erythraea
    • You, D., Yao, L. L., Huang, D., Escalante-Semerena, J. C., and Ye, B. C. (2014) Acetyl coenzyme A synthetase is acetylated on multiple lysine residues by a protein acetyltransferase with a single Gcn5-typeN-acetyltransferase (GNAT) domain in Saccharopolyspora erythraea. J. Bacteriol. 196, 3169-3178
    • (2014) J. Bacteriol , vol.196 , pp. 3169-3178
    • You, D.1    Yao, L.L.2    Huang, D.3    Escalante-Semerena, J.C.4    Ye, B.C.5
  • 38
    • 84886599617 scopus 로고    scopus 로고
    • Structure and mechanism of non-histone protein acetyltransferase enzymes
    • Friedmann, D. R., and Marmorstein, R. (2013) Structure and mechanism of non-histone protein acetyltransferase enzymes. FEBS J. 280, 5570-5581
    • (2013) FEBS J , vol.280 , pp. 5570-5581
    • Friedmann, D.R.1    Marmorstein, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.