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Volumn 128, Issue , 2015, Pages 352-364

Lysine acetylation is a common post-translational modification of key metabolic pathway enzymes of the anaerobe Porphyromonas gingivalis

Author keywords

Anaerobe; Catabolism; Immune affinity enrichment; Lysine acetylation; Mass spectrometry

Indexed keywords

LYSINE; ACYLTRANSFERASE;

EID: 84941085139     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2015.08.015     Document Type: Article
Times cited : (31)

References (62)
  • 1
    • 0033873462 scopus 로고    scopus 로고
    • Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis
    • Takahashi N., Sato T., Yamada T. Metabolic pathways for cytotoxic end product formation from glutamate- and aspartate-containing peptides by Porphyromonas gingivalis. J. Bacteriol. 2000, 182:4704-4710.
    • (2000) J. Bacteriol. , vol.182 , pp. 4704-4710
    • Takahashi, N.1    Sato, T.2    Yamada, T.3
  • 2
    • 0024058673 scopus 로고
    • Relationship of subgingival microbial complexes to clinical features at the sampled sites
    • Socransky S., Haffajee A., Dzink J. Relationship of subgingival microbial complexes to clinical features at the sampled sites. J. Clin. Periodontol. 1988, 15:440-444.
    • (1988) J. Clin. Periodontol. , vol.15 , pp. 440-444
    • Socransky, S.1    Haffajee, A.2    Dzink, J.3
  • 3
    • 81755166205 scopus 로고    scopus 로고
    • Low-abundance biofilm species orchestrates inflammatory periodontal disease through the commensal microbiota and complement
    • Hajishengallis G., Liang S., Payne Mark A., Hashim A., Jotwani R., Eskan Mehmet A., et al. Low-abundance biofilm species orchestrates inflammatory periodontal disease through the commensal microbiota and complement. Cell Host Microbe 2011, 10:497-506.
    • (2011) Cell Host Microbe , vol.10 , pp. 497-506
    • Hajishengallis, G.1    Liang, S.2    Payne Mark, A.3    Hashim, A.4    Jotwani, R.5    Eskan Mehmet, A.6
  • 5
    • 0034692543 scopus 로고    scopus 로고
    • Periodontal disease and coronary heart disease risk
    • (Chicago, Ill)
    • Hujoel P.P. Periodontal disease and coronary heart disease risk. JAMA 2000, 284:1406. (Chicago, Ill).
    • (2000) JAMA , vol.284 , pp. 1406
    • Hujoel, P.P.1
  • 7
    • 1442351870 scopus 로고    scopus 로고
    • Associations between periodontal disease and risk for nosocomial bacterial pneumonia and chronic obstructive pulmonary disease. A systematic review
    • Scannapieco F.A., Bush R.B., Paju S. Associations between periodontal disease and risk for nosocomial bacterial pneumonia and chronic obstructive pulmonary disease. A systematic review. Ann. Periodontol 2003, 8:54-69.
    • (2003) Ann. Periodontol , vol.8 , pp. 54-69
    • Scannapieco, F.A.1    Bush, R.B.2    Paju, S.3
  • 8
    • 64249151247 scopus 로고    scopus 로고
    • Periodontal disease as a risk factor in pre-term low birth weight-an assessment of gynecologists' knowledge: a pilot study
    • Shenoy R., Nayak D., Sequeira P. Periodontal disease as a risk factor in pre-term low birth weight-an assessment of gynecologists' knowledge: a pilot study. Indian J. Dent. Res. 2009, 20:13-16.
    • (2009) Indian J. Dent. Res. , vol.20 , pp. 13-16
    • Shenoy, R.1    Nayak, D.2    Sequeira, P.3
  • 9
    • 55549083867 scopus 로고    scopus 로고
    • The chronicles of Porphyromonas gingivalis: the microbium, the human oral epithelium and their interplay
    • Yilmaz O. The chronicles of Porphyromonas gingivalis: the microbium, the human oral epithelium and their interplay. Microbiology 2008, 154:2897-2903.
    • (2008) Microbiology , vol.154 , pp. 2897-2903
    • Yilmaz, O.1
  • 10
    • 84903538710 scopus 로고    scopus 로고
    • Porphyromonas gingivalis peptidylarginine deiminase, a key contributor in the pathogenesis of experimental periodontal disease and experimental arthritis
    • Gully N., Bright R., Marino V., Marchant C., Cantley M., Haynes D., et al. Porphyromonas gingivalis peptidylarginine deiminase, a key contributor in the pathogenesis of experimental periodontal disease and experimental arthritis. PLoS One 2014, 9.
    • (2014) PLoS One , vol.9
    • Gully, N.1    Bright, R.2    Marino, V.3    Marchant, C.4    Cantley, M.5    Haynes, D.6
  • 11
    • 84863826834 scopus 로고    scopus 로고
    • Porphyromonas gingivalis: an invasive and evasive opportunistic oral pathogen
    • Bostanci N., Belibasakis G.N. Porphyromonas gingivalis: an invasive and evasive opportunistic oral pathogen. FEMS Microbiol. Lett. 2012, 333:1-9.
    • (2012) FEMS Microbiol. Lett. , vol.333 , pp. 1-9
    • Bostanci, N.1    Belibasakis, G.N.2
  • 13
    • 0031766801 scopus 로고    scopus 로고
    • Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis
    • Lamont R.J., Jenkinson H.F. Life below the gum line: pathogenic mechanisms of Porphyromonas gingivalis. Microbiol. Mol. Biol. Rev. 1998, 62:1244-1263.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1244-1263
    • Lamont, R.J.1    Jenkinson, H.F.2
  • 14
    • 9344261804 scopus 로고    scopus 로고
    • Stress and how bacteria cope with death and survival
    • Aertsen A. Stress and how bacteria cope with death and survival. Crit. Rev. Microbiol. 2004, 30:263-273.
    • (2004) Crit. Rev. Microbiol. , vol.30 , pp. 263-273
    • Aertsen, A.1
  • 15
    • 31144471322 scopus 로고    scopus 로고
    • Bacterial stress responses: what doesn't kill them can make them stronger
    • Boor K.J. Bacterial stress responses: what doesn't kill them can make them stronger. PLoS Biol. 2006, 4.
    • (2006) PLoS Biol. , vol.4
    • Boor, K.J.1
  • 16
    • 3342953960 scopus 로고    scopus 로고
    • Bacterial linguistic communication and social intelligence
    • Jacob E.B. Bacterial linguistic communication and social intelligence. Trends Microbiol. 2004, 12:366.
    • (2004) Trends Microbiol. , vol.12 , pp. 366
    • Jacob, E.B.1
  • 18
    • 58049217240 scopus 로고    scopus 로고
    • Riboswitch RNAs: using RNA to sense cellular metabolism
    • Henkin T.M. Riboswitch RNAs: using RNA to sense cellular metabolism. Genes Dev. 2008, 22:3383-3390.
    • (2008) Genes Dev. , vol.22 , pp. 3383-3390
    • Henkin, T.M.1
  • 19
    • 0026511987 scopus 로고
    • Environmental signals controlling expression of virulence determinants in bacteria
    • Mekalanos J.J. Environmental signals controlling expression of virulence determinants in bacteria. J. Bacteriol. 1992, 174:1-7.
    • (1992) J. Bacteriol. , vol.174 , pp. 1-7
    • Mekalanos, J.J.1
  • 20
    • 73449104573 scopus 로고    scopus 로고
    • Compensatory evolution of gene regulation in response to stress by Escherichia coli lacking RpoS
    • Stoebel D.M., Hokamp K., Last M.S., Dorman C.J. Compensatory evolution of gene regulation in response to stress by Escherichia coli lacking RpoS. PLoS Genet. 2009, 5.
    • (2009) PLoS Genet. , vol.5
    • Stoebel, D.M.1    Hokamp, K.2    Last, M.S.3    Dorman, C.J.4
  • 21
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim S., Sprung R., Chen Y., Xu Y., Ball H., Pei J., et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol. Cell 2006, 23:607-618.
    • (2006) Mol. Cell , vol.23 , pp. 607-618
    • Kim, S.1    Sprung, R.2    Chen, Y.3    Xu, Y.4    Ball, H.5    Pei, J.6
  • 22
    • 79954582107 scopus 로고    scopus 로고
    • Control of protein function by reversible N≈-lysine acetylation in bacteria
    • Thao S., Escalante S.J. Control of protein function by reversible NΕ-lysine acetylation in bacteria. Curr. Opin. Microbiol. 2011, 14:200-204.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 200-204
    • Thao, S.1    Escalante, S.J.2
  • 23
    • 56649114286 scopus 로고    scopus 로고
    • The diversity of lysine-acetylated proteins in Escherichia coli
    • Yu B., Kim J., Moon J., Ryu S., Pan J.-G. The diversity of lysine-acetylated proteins in Escherichia coli. J. Microbiol. Biotechnol. 2008, 18:1529-1536.
    • (2008) J. Microbiol. Biotechnol. , vol.18 , pp. 1529-1536
    • Yu, B.1    Kim, J.2    Moon, J.3    Ryu, S.4    Pan, J.-G.5
  • 24
    • 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., et al. Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol. Cell. Proteomics 2009, 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
  • 27
    • 77954013335 scopus 로고    scopus 로고
    • Bacterial protein acetylation: the dawning of a new age
    • Hu L.I., Lima B.P., Wolfe A.J. Bacterial protein acetylation: the dawning of a new age. Mol. Microbiol. 2010, 77:15-21.
    • (2010) Mol. Microbiol. , vol.77 , pp. 15-21
    • Hu, L.I.1    Lima, B.P.2    Wolfe, A.J.3
  • 28
    • 84863621527 scopus 로고    scopus 로고
    • Cancer epigenetics: from mechanism to therapy
    • Dawson Mark A., Kouzarides T. Cancer epigenetics: from mechanism to therapy. Cell 2012, 150:12-27.
    • (2012) Cell , vol.150 , pp. 12-27
    • Dawson Mark, A.1    Kouzarides, T.2
  • 29
    • 33644946604 scopus 로고    scopus 로고
    • HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis
    • Saha R.N., Pahan K. HATs and HDACs in neurodegeneration: a tale of disconcerted acetylation homeostasis. Cell Death Differ. 2006, 13:539-550.
    • (2006) Cell Death Differ. , vol.13 , pp. 539-550
    • Saha, R.N.1    Pahan, K.2
  • 30
    • 84896289692 scopus 로고    scopus 로고
    • Dysregulation of histone acetyltransferases and deacetylases in cardiovascular diseases
    • Wang Y., Miao X., Liu Y., Li F., Liu Q., Sun J., et al. Dysregulation of histone acetyltransferases and deacetylases in cardiovascular diseases. Oxidative Med. Cell. Longev. 2014, 2014.
    • (2014) Oxidative Med. Cell. Longev. , pp. 2014
    • Wang, Y.1    Miao, X.2    Liu, Y.3    Li, F.4    Liu, Q.5    Sun, J.6
  • 31
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. U. S. A. 2006, 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
  • 32
    • 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., et al. Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux. Science 2010, 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
  • 33
    • 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., Escalante-Semerena J.C. In Salmonella enterica, the sirtuin-dependent protein acylation/deacylation system (SDPADS) maintains energy homeostasis during growth on low concentrations of acetate. Mol. Microbiol. 2011, 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
  • 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., et al. Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus. Proteomics 2013, 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.6
  • 36
    • 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., Escalante-Semerena J.C. System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. J. Biol. Chem. 2012, 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
  • 37
    • 84883772266 scopus 로고    scopus 로고
    • Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus
    • Okanishi H., Kim K., Masui R., Kuramitsu S. Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus. J. Proteome Res. 2013, 12:3952-3968.
    • (2013) J. Proteome Res. , vol.12 , pp. 3952-3968
    • Okanishi, H.1    Kim, K.2    Masui, R.3    Kuramitsu, S.4
  • 38
  • 39
    • 79551584971 scopus 로고    scopus 로고
    • Regulation of intermediary metabolism by protein acetylation
    • Guan K.L., Xiong Y. Regulation of intermediary metabolism by protein acetylation. Trends Biochem. Sci. 2011, 36:108-116.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 108-116
    • Guan, K.L.1    Xiong, Y.2
  • 40
    • 80051937249 scopus 로고    scopus 로고
    • Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter
    • Lima B.P., Antelmann H., Gronau K., Chi B.K., Becher D., Brinsmade S.R., et al. Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter. Mol. Microbiol. 2011, 81:1190-1204.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1190-1204
    • Lima, B.P.1    Antelmann, H.2    Gronau, K.3    Chi, B.K.4    Becher, D.5    Brinsmade, S.R.6
  • 41
    • 84899668522 scopus 로고    scopus 로고
    • Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation
    • Kuhn M.L., Zemaitaitis B., Hu L.I., Sahu A., Sorensen D., Minasov G., et al. Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation. PLoS One 2014, 9.
    • (2014) PLoS One , vol.9
    • Kuhn, M.L.1    Zemaitaitis, B.2    Hu, L.I.3    Sahu, A.4    Sorensen, D.5    Minasov, G.6
  • 44
    • 84899842537 scopus 로고    scopus 로고
    • Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors
    • Veith P.D., Chen Y.Y., Gorasia D.G., Chen D., Glew M.D., O'Brien-Simpson N.M., et al. Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors. J. Proteome Res. 2014, 13:2420-2432.
    • (2014) J. Proteome Res. , vol.13 , pp. 2420-2432
    • Veith, P.D.1    Chen, Y.Y.2    Gorasia, D.G.3    Chen, D.4    Glew, M.D.5    O'Brien-Simpson, N.M.6
  • 45
    • 2942568222 scopus 로고    scopus 로고
    • Unimod: protein modifications for mass spectrometry
    • Creasy D.M., Cottrell J.S. Unimod: protein modifications for mass spectrometry. Proteomics 2004, 4:1534-1536.
    • (2004) Proteomics , vol.4 , pp. 1534-1536
    • Creasy, D.M.1    Cottrell, J.S.2
  • 46
    • 0041335299 scopus 로고    scopus 로고
    • Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83
    • Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E., Eisen J.A., et al. Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83. J. Bacteriol. 2003, 185:5591-5601.
    • (2003) J. Bacteriol. , vol.185 , pp. 5591-5601
    • Nelson, K.E.1    Fleischmann, R.D.2    DeBoy, R.T.3    Paulsen, I.T.4    Fouts, D.E.5    Eisen, J.A.6
  • 47
    • 79954415619 scopus 로고    scopus 로고
    • Comprehensive lysine acetylomes emerging from bacteria to humans
    • Kim G.-W., Yang X.-J. Comprehensive lysine acetylomes emerging from bacteria to humans. Trends Biochem. Sci. 2011, 36:211-220.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 211-220
    • Kim, G.-W.1    Yang, X.-J.2
  • 48
    • 84864996189 scopus 로고    scopus 로고
    • Mechanistic insights into the regulation of metabolic enzymes by acetylation
    • Xiong Y., Guan K.-L. Mechanistic insights into the regulation of metabolic enzymes by acetylation. J. Cell Biol. 2012, 198:155-164.
    • (2012) J. Cell Biol. , vol.198 , pp. 155-164
    • Xiong, Y.1    Guan, K.-L.2
  • 50
    • 84901370340 scopus 로고    scopus 로고
    • Involvement of the Wbp pathway in the biosynthesis of Porphyromonas gingivalis lipopolysaccharide with anionic polysaccharide
    • Shoji M., Sato K., Yukitake H., Naito M., Nakayama K. Involvement of the Wbp pathway in the biosynthesis of Porphyromonas gingivalis lipopolysaccharide with anionic polysaccharide. Sci. Rep. 2014, 4:5056.
    • (2014) Sci. Rep. , vol.4 , pp. 5056
    • Shoji, M.1    Sato, K.2    Yukitake, H.3    Naito, M.4    Nakayama, K.5
  • 52
    • 84910110983 scopus 로고    scopus 로고
    • The Porphyromonas gingivalis ferric uptake regulator orthologue binds hemin and regulates hemin-responsive biofilm development
    • Butler C.A., Dashper S.G., Zhang L., Seers C.A., Mitchell H.L., Catmull D.V., et al. The Porphyromonas gingivalis ferric uptake regulator orthologue binds hemin and regulates hemin-responsive biofilm development. PLoS One 2014, 9.
    • (2014) PLoS One , vol.9
    • Butler, C.A.1    Dashper, S.G.2    Zhang, L.3    Seers, C.A.4    Mitchell, H.L.5    Catmull, D.V.6
  • 54
    • 84879369738 scopus 로고    scopus 로고
    • Commensal bacteria at the interface of host metabolism and the immune system
    • Brestoff J.R., Artis D. Commensal bacteria at the interface of host metabolism and the immune system. Nat. Immunol. 2013, 14:676-684.
    • (2013) Nat. Immunol. , vol.14 , pp. 676-684
    • Brestoff, J.R.1    Artis, D.2
  • 55
    • 42549084285 scopus 로고    scopus 로고
    • 18O reverse proteolytic labeling to determine the effect of biofilm culture on the cell envelope proteome of Porphyromonas gingivalis W50
    • 18O reverse proteolytic labeling to determine the effect of biofilm culture on the cell envelope proteome of Porphyromonas gingivalis W50. Proteomics 2008, 8:1645-1660.
    • (2008) Proteomics , vol.8 , pp. 1645-1660
    • Ang, C.S.1    Veith, P.D.2    Dashper, S.G.3    Reynolds, E.C.4
  • 56
    • 70349761672 scopus 로고    scopus 로고
    • Pathway analysis for intracellular Porphyromonas gingivalis using a strain ATCC 33277 specific database
    • Hendrickson E.L., Xia Q., Wang T., Lamont R.J., Hackett M. Pathway analysis for intracellular Porphyromonas gingivalis using a strain ATCC 33277 specific database. BMC Microbiol. 2009, 9:185.
    • (2009) BMC Microbiol. , vol.9 , pp. 185
    • Hendrickson, E.L.1    Xia, Q.2    Wang, T.3    Lamont, R.J.4    Hackett, M.5
  • 57
    • 72249097352 scopus 로고    scopus 로고
    • Growth-rate dependent global effects on gene expression in bacteria
    • Klumpp S., Zhang Z., Hwa T. Growth-rate dependent global effects on gene expression in bacteria. Cell 2009, 139:1366.
    • (2009) Cell , vol.139 , pp. 1366
    • Klumpp, S.1    Zhang, Z.2    Hwa, T.3
  • 59
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y., Oda Y., Tabata T., Sato T., Nagasu T., Rappsilber J., et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol. Cell. Proteomics 2005, 4:1265-1272.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6
  • 60
    • 84869215170 scopus 로고    scopus 로고
    • Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae
    • Henriksen P., Wagner S.A., Weinert B.T., Sharma S., Bačinskaja G., Rehman M., et al. Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Mol. Cell. Proteomics 2012, 11:1510-1522.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1510-1522
    • Henriksen, P.1    Wagner, S.A.2    Weinert, B.T.3    Sharma, S.4    Bačinskaja, G.5    Rehman, M.6
  • 61
    • 84896475873 scopus 로고    scopus 로고
    • The acetylation motif in AMP-forming acyl coenzyme a synthetases contains residues critical for acetylation and recognition by the protein acetyltransferase pat of Rhodopseudomonas palustris
    • Crosby H.A., Escalante-Semerena J.C. The acetylation motif in AMP-forming acyl coenzyme a synthetases contains residues critical for acetylation and recognition by the protein acetyltransferase pat of Rhodopseudomonas palustris. J. Bacteriol. 2014, 196:1496-1504.
    • (2014) J. Bacteriol. , vol.196 , pp. 1496-1504
    • Crosby, H.A.1    Escalante-Semerena, J.C.2
  • 62
    • 84886599617 scopus 로고    scopus 로고
    • Structure and mechanism of non-histone protein acetyltransferase enzymes
    • Friedmann D.R., Marmorstein R. Structure and mechanism of non-histone protein acetyltransferase enzymes. FEBS J. 2013, 280:5570-5581.
    • (2013) FEBS J. , vol.280 , pp. 5570-5581
    • Friedmann, D.R.1    Marmorstein, R.2


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