메뉴 건너뛰기




Volumn 13, Issue 15, 2013, Pages 2278-2282

Proteomic analysis of acetylation in thermophilic Geobacillus kaustophilus

Author keywords

Acetylation; Geobacillus kaustophilus; Microbiology; Posttranslational modification; Proteome; Thermophile

Indexed keywords

BACTERIAL PROTEIN; CELL PROTEIN; LYSINE;

EID: 84881243155     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201200072     Document Type: Article
Times cited : (61)

References (31)
  • 1
    • 0014409959 scopus 로고
    • Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone
    • Gershey, E. L., Vidali, G., Allfrey, V. G., Chemical studies of histone acetylation. The occurrence of epsilon-N-acetyllysine in the f2a1 histone. J. Biol. Chem. 1968, 243, 5018-5022.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5018-5022
    • Gershey, E.L.1    Vidali, G.2    Allfrey, V.G.3
  • 2
    • 0007852927 scopus 로고
    • The presence of acetyl groups of histones
    • Phillips, D. M., The presence of acetyl groups of histones. Biochem. J. 1963, 87, 258-263.
    • (1963) Biochem. J. , vol.87 , pp. 258-263
    • Phillips, D.M.1
  • 4
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V. G., Faulkner, R., Mirsky, A. E., Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. USA 1964, 51, 786-794.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 5
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G., Guarente, L., The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 2004, 73, 417-435.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 6
    • 0024151129 scopus 로고
    • Structure and utilization of tubulin isotypes
    • Sullivan, K. F., Structure and utilization of tubulin isotypes. Annu. Rev. Cell. Biol. 1988, 4, 687-716.
    • (1988) Annu. Rev. Cell. Biol. , vol.4 , pp. 687-716
    • Sullivan, K.F.1
  • 7
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao, S., Xu, W., Jiang, W., Yu, W. et al., Regulation of cellular metabolism by protein lysine acetylation. Science 2010, 327, 1000-1004.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3    Yu, W.4
  • 8
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel, T., Deng, C. X., Mostoslavsky, R., Recent progress in the biology and physiology of sirtuins. Nature 2009, 460, 587-591.
    • (2009) Nature , vol.460 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 9
    • 48749114997 scopus 로고    scopus 로고
    • A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation
    • Lin, Y. Y., Qi, Y., Lu, J. Y., Pan, X. et al., A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation. Genes Dev. 2008, 22, 2062-2074.
    • (2008) Genes Dev. , vol.22 , pp. 2062-2074
    • Lin, Y.Y.1    Qi, Y.2    Lu, J.Y.3    Pan, X.4
  • 10
    • 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
  • 11
    • 38649123072 scopus 로고    scopus 로고
    • Conserved metabolic regulatory functions of sirtuins
    • Schwer, B., Verdin, E., Conserved metabolic regulatory functions of sirtuins. Cell Metab. 2008, 7, 104-112.
    • (2008) Cell Metab. , vol.7 , pp. 104-112
    • Schwer, B.1    Verdin, E.2
  • 12
    • 53649086367 scopus 로고    scopus 로고
    • Mechanisms and molecular probes of sirtuins
    • Smith, B. C., Hallows, W. C., Denu, J. M., Mechanisms and molecular probes of sirtuins. Chem. Biol. 2008, 15, 1002-1013.
    • (2008) Chem. Biol. , vol.15 , pp. 1002-1013
    • Smith, B.C.1    Hallows, W.C.2    Denu, J.M.3
  • 13
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., Horikawa, I., Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol. Biol. Cell. 2005, 16, 4623-4635.
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 14
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F. R., Plunkett, G., 3rd, Bloch, C. A., Perna, N. T. et al., The complete genome sequence of Escherichia coli K-12. Science 1997, 277, 1453-1462.
    • (1997) Science , vol.277 , pp. 1453-1462
    • Blattner, F.R.1    Plunkett 3rd, G.2    Bloch, C.A.3    Perna, N.T.4
  • 15
    • 0035950182 scopus 로고    scopus 로고
    • Complete genome sequence of Salmonella enterica serovar Typhimurium LT2
    • McClelland, M., Sanderson, K. E., Spieth, J., Clifton, S. W. et al., Complete genome sequence of Salmonella enterica serovar Typhimurium LT2. Nature 2001, 413, 852-856.
    • (2001) Nature , vol.413 , pp. 852-856
    • McClelland, M.1    Sanderson, K.E.2    Spieth, J.3    Clifton, S.W.4
  • 16
    • 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 2002, 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
  • 17
    • 77957836421 scopus 로고    scopus 로고
    • Protein acetylation in archaea, bacteria, and eukaryotes
    • 820681
    • Soppa, J., Protein acetylation in archaea, bacteria, and eukaryotes. Archaea 2010, 820681, 1-9.
    • (2010) Archaea , pp. 1-9
    • Soppa, J.1
  • 18
    • 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 2002, 296, 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
  • 19
    • 62649172737 scopus 로고    scopus 로고
    • Genetic evidence for the importance of protein acetylation and protein deacetylation in the halophilic archaeon Haloferax volcanii
    • Altman-Price, N., Mevarech, M., Genetic evidence for the importance of protein acetylation and protein deacetylation in the halophilic archaeon Haloferax volcanii. J. Bacteriol. 2009, 191, 1610-1617.
    • (2009) J. Bacteriol. , vol.191 , pp. 1610-1617
    • Altman-Price, N.1    Mevarech, M.2
  • 20
    • 77149120797 scopus 로고    scopus 로고
    • Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux
    • Wang, Q., Zhang, Y., Yang, C., Xiong, H. 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
  • 21
    • 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. 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
  • 22
    • 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., 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.J.1    Kim, J.A.2    Moon, J.H.3    Ryu, S.E.4    Pan, J.G.5
  • 23
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • Eichler, J., Adams, M. W., Posttranslational protein modification in Archaea. Microbiol. Mol. Biol. Rev. 2005, 69, 393-425.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 393-425
    • Eichler, J.1    Adams, M.W.2
  • 24
    • 0037009516 scopus 로고    scopus 로고
    • Structure of Alba: an archaeal chromatin protein modulated by acetylation
    • Wardleworth, B. N., Russell, R. J., Bell, S. D., Taylor, G. L., White, M. F., Structure of Alba: an archaeal chromatin protein modulated by acetylation. EMBO J. 2002, 21, 4654-4662.
    • (2002) EMBO J. , vol.21 , pp. 4654-4662
    • Wardleworth, B.N.1    Russell, R.J.2    Bell, S.D.3    Taylor, G.L.4    White, M.F.5
  • 25
    • 0035064602 scopus 로고    scopus 로고
    • Taxonomic study of aerobic thermophilic bacilli: descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovolans, Bacillus kaustophilus, Bacillus thermoglusidasius and Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. thermocatenulatus, G. thermoleovolans, G. kaustophilus, G. thermoglusidasius and G. thermodenitrificans
    • Nazina, T. N., Tourova, T. P., Poltaraus, A. B., Novikova, E. V. et al., Taxonomic study of aerobic thermophilic bacilli: descriptions of Geobacillus subterraneus gen. nov., sp. nov. and Geobacillus uzenensis sp. nov. from petroleum reservoirs and transfer of Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus thermoleovolans, Bacillus kaustophilus, Bacillus thermoglusidasius and Bacillus thermodenitrificans to Geobacillus as the new combinations G. stearothermophilus, G. thermocatenulatus, G. thermoleovolans, G. kaustophilus, G. thermoglusidasius and G. thermodenitrificans. Int. J. Syst. Evol. Microbiol. 2001, 51, 433-446.
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 433-446
    • Nazina, T.N.1    Tourova, T.P.2    Poltaraus, A.B.3    Novikova, E.V.4
  • 26
    • 12744268746 scopus 로고    scopus 로고
    • Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus
    • Takami, H., Takaki, Y., Chee, G. J., Nishi, S. et al., Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus. Nucleic Acids Res. 2004, 32, 6292-6303.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6292-6303
    • Takami, H.1    Takaki, Y.2    Chee, G.J.3    Nishi, S.4
  • 27
    • 33847352051 scopus 로고    scopus 로고
    • Use of an integrated MS-multiplexed MS/MS data acquisition strategy for high-coverage peptide mapping studies
    • Chakraborty, A. B., Berger, S. J., Gebler, J. C., Use of an integrated MS-multiplexed MS/MS data acquisition strategy for high-coverage peptide mapping studies. Rapid Commun. Mass Spectrom. 2007, 21, 730-744.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 730-744
    • Chakraborty, A.B.1    Berger, S.J.2    Gebler, J.C.3
  • 28
    • 33645725976 scopus 로고    scopus 로고
    • Simultaneous qualitative and quantitative analysis of the Escherichia coli proteome: a sweet tale
    • Silva, J. C., Denny, R., Dorschel, C., Gorenstein, M. V. et al., Simultaneous qualitative and quantitative analysis of the Escherichia coli proteome: a sweet tale. Mol. Cell. Proteomics 2006, 5, 589-607.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 589-607
    • Silva, J.C.1    Denny, R.2    Dorschel, C.3    Gorenstein, M.V.4
  • 29
    • 20144388265 scopus 로고    scopus 로고
    • Quantitative proteomic analysis by accurate mass retention time pairs
    • Silva, J. C., Denny, R., Dorschel, C. A., Gorenstein, M. et al., Quantitative proteomic analysis by accurate mass retention time pairs. Anal. Chem. 2005, 77, 2187-2200.
    • (2005) Anal. Chem. , vol.77 , pp. 2187-2200
    • Silva, J.C.1    Denny, R.2    Dorschel, C.A.3    Gorenstein, M.4
  • 31
    • 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. et al., The acetylproteome of gram-positive model bacterium Bacillus subtilis. Proteomics 2013, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.