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Volumn 189, Issue 1, 2007, Pages 272-275

Proteolytic adaptor for transfer-messenger RNA-tagged proteins from α-proteobacteria

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; BACTERIAL PROTEIN; MESSENGER RNA; PROTEIN SSPB; TRANSFER MESSENGER RNA; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 33845916549     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01387-06     Document Type: Article
Times cited : (25)

References (32)
  • 2
    • 0031596298 scopus 로고    scopus 로고
    • MglA and MglB are required for the intramacrophage growth of Francisella novieida
    • Baron, G. S., and F. E. Nano. 1998. MglA and MglB are required for the intramacrophage growth of Francisella novieida. Mol. Microbiol. 29:247-259.
    • (1998) Mol. Microbiol , vol.29 , pp. 247-259
    • Baron, G.S.1    Nano, F.E.2
  • 3
    • 0028215784 scopus 로고
    • Salmonella typhimurium loci involved in survival within macrophages
    • Baumler, A. J., J. G. Kusters, I. Stojiljkovic, and F. Heffron. 1994. Salmonella typhimurium loci involved in survival within macrophages. Infect. Immun. 62:1623-1630.
    • (1994) Infect. Immun , vol.62 , pp. 1623-1630
    • Baumler, A.J.1    Kusters, J.G.2    Stojiljkovic, I.3    Heffron, F.4
  • 5
    • 0036210995 scopus 로고    scopus 로고
    • ClpS, a substrate modulator of the ClpAP machine
    • Dougan, D. A., B. G. Reid, A. L. Horwich, and B. Bukau. 2002. ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 9:673-683.
    • (2002) Mol. Cell , vol.9 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 6
    • 0026079941 scopus 로고
    • Discovery of a rhizobial RNA that is essential for symbiotic root nodule development
    • Ebeling, S., C. Kundig, and H. Hennecke. 1991. Discovery of a rhizobial RNA that is essential for symbiotic root nodule development. J. Bacteriol. 173:6373-6382.
    • (1991) J. Bacteriol , vol.173 , pp. 6373-6382
    • Ebeling, S.1    Kundig, C.2    Hennecke, H.3
  • 7
    • 0017740506 scopus 로고
    • Envelope-associated nucleoid from Caulobacter crescentus stalked and swarmer cells
    • Evinger, M., and N. Agabian. 1977. Envelope-associated nucleoid from Caulobacter crescentus stalked and swarmer cells. J. Bacteriol. 132:294-301.
    • (1977) J. Bacteriol , vol.132 , pp. 294-301
    • Evinger, M.1    Agabian, N.2
  • 8
    • 25144452838 scopus 로고    scopus 로고
    • Cytoplasmic degradation of ssrA-tagged proteins
    • Farrell, C. M., A. D. Grossman, and R. T. Sauer. 2005. Cytoplasmic degradation of ssrA-tagged proteins. Mol. Microbiol. 57:1750-1761.
    • (2005) Mol. Microbiol , vol.57 , pp. 1750-1761
    • Farrell, C.M.1    Grossman, A.D.2    Sauer, R.T.3
  • 9
    • 4444377383 scopus 로고    scopus 로고
    • Modulating substrate choice: The SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation
    • Flynn, J. M., I. Levchenko, R. T. Sauer, and T. A. Baker. 2004. Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. Genes Dev. 18:2292-2301.
    • (2004) Genes Dev , vol.18 , pp. 2292-2301
    • Flynn, J.M.1    Levchenko, I.2    Sauer, R.T.3    Baker, T.A.4
  • 10
    • 0035845498 scopus 로고    scopus 로고
    • Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis
    • Flynn, J. M., I. Levchenko, M. Seidel, S. H. Wickner, R. T. Sauer, and T. A. Baker. 2001. Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis. Proc. Natl. Acad. Sci. USA 98:10584-10589.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10584-10589
    • Flynn, J.M.1    Levchenko, I.2    Seidel, M.3    Wickner, S.H.4    Sauer, R.T.5    Baker, T.A.6
  • 11
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn, J. M., S. B. Neher, Y. I. Kim, R. T. Sauer, and T. A. Baker. 2003. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11:671-683.
    • (2003) Mol. Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 12
    • 0022351923 scopus 로고
    • Positive selection procedure for entrapment of insertion sequence elements in gram-negative bacteria
    • Gay, P., D. Le Coq, M. Steinmetz, T. Berkelman, and C. I. Kado. 1985. Positive selection procedure for entrapment of insertion sequence elements in gram-negative bacteria. J. Bacteriol. 164:918-921.
    • (1985) J. Bacteriol , vol.164 , pp. 918-921
    • Gay, P.1    Le Coq, D.2    Steinmetz, M.3    Berkelman, T.4    Kado, C.I.5
  • 13
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • Gottesman, S. 2003. Proteolysis in bacterial regulatory circuits. Annu. Rev. Cell Dev. Biol. 19:565-587.
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 14
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman, S., E. Roche, Y. Zhou, and R. T. Sauer. 1998. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12:1338-1347.
    • (1998) Genes Dev , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 15
    • 0346494971 scopus 로고    scopus 로고
    • The tmRNA website: Reductive evolution of tmRNA in plastids and other endosymbionts
    • Gueneau de Novoa, P., and K. P. Williams. 2004. The tmRNA website: reductive evolution of tmRNA in plastids and other endosymbionts. Nucleic Acids Res. 32:D104-D108.
    • (2004) Nucleic Acids Res , vol.32
    • Gueneau de Novoa, P.1    Williams, K.P.2
  • 16
    • 22144462503 scopus 로고    scopus 로고
    • Cell cycle-regulated degradation of tmRNA is controlled by RNase R. and SnapB
    • Hong, S.-J., Q. A. Tran, and K. C. Keiler. 2005. Cell cycle-regulated degradation of tmRNA is controlled by RNase R. and SnapB. Mol. Microbiol. 57:565-575.
    • (2005) Mol. Microbiol , vol.57 , pp. 565-575
    • Hong, S.-J.1    Tran, Q.A.2    Keiler, K.C.3
  • 17
    • 25644435672 scopus 로고    scopus 로고
    • Signature proteins that are distinctive of alpha proteobacteria
    • Kainth, P., and R. S. Gupta. 2005. Signature proteins that are distinctive of alpha proteobacteria. BMC Genomics 6:94.
    • (2005) BMC Genomics , vol.6 , pp. 94
    • Kainth, P.1    Gupta, R.S.2
  • 18
    • 0034046020 scopus 로고    scopus 로고
    • The SsrA-SmpB system for protein tagging, directed degradation, and ribosome rescue
    • Karzai, A. W., E. D. Roche, and R. T. Sauer. 2000. The SsrA-SmpB system for protein tagging, directed degradation, and ribosome rescue. Nat. Struct. Biol. 7:449-455.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 449-455
    • Karzai, A.W.1    Roche, E.D.2    Sauer, R.T.3
  • 19
    • 0037336119 scopus 로고    scopus 로고
    • tmRNA in Caulobacter crescentus is cell cycle regulated by temporally controlled transcription and RNA degradation
    • Keiler, K. C., and L. Shapiro. 2003. tmRNA in Caulobacter crescentus is cell cycle regulated by temporally controlled transcription and RNA degradation. J. Bacteriol. 185:1825-1830.
    • (2003) J. Bacteriol , vol.185 , pp. 1825-1830
    • Keiler, K.C.1    Shapiro, L.2
  • 20
    • 0037227964 scopus 로고    scopus 로고
    • tmRNA is required for correct timing of DNA replication in Caulobacter crescentus
    • Keiler, K. C., and L. Shapiro. 2003. tmRNA is required for correct timing of DNA replication in Caulobacter crescentus. J. Bacteriol. 185:573-580.
    • (2003) J. Bacteriol , vol.185 , pp. 573-580
    • Keiler, K.C.1    Shapiro, L.2
  • 21
    • 0034608854 scopus 로고    scopus 로고
    • tmRNAs that encode proteolysis-inducing tags are found in all known bacterial genomes: A two-piece tmRNA functions in Caulobacter
    • Keiler, K. C., L. Shapiro, and K. P. Williams. 2000. tmRNAs that encode proteolysis-inducing tags are found in all known bacterial genomes: a two-piece tmRNA functions in Caulobacter. Proc. Natl. Acad. Sci. USA 97:7778-7783.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7778-7783
    • Keiler, K.C.1    Shapiro, L.2    Williams, K.P.3
  • 22
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler, K. C., P. R. Waller, and R. T. Sauer. 1996. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271:990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 23
    • 0034671792 scopus 로고    scopus 로고
    • Global analysis of the genetic network controlling a bacterial cell cycle
    • Laub, M. T., H. H. McAdams, T. Feldblyum, C. Fraser, and L. Shapiro. 2000. Global analysis of the genetic network controlling a bacterial cell cycle. Science 290:2144-2148.
    • (2000) Science , vol.290 , pp. 2144-2148
    • Laub, M.T.1    McAdams, H.H.2    Feldblyum, T.3    Fraser, C.4    Shapiro, L.5
  • 25
    • 0141992126 scopus 로고    scopus 로고
    • Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag
    • Levchenko, I., R. A. Grant, D. A. Wah, R. T. Sauer, and T. A. Baker. 2003. Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag. Mol. Cell 12:365-372.
    • (2003) Mol. Cell , vol.12 , pp. 365-372
    • Levchenko, I.1    Grant, R.A.2    Wah, D.A.3    Sauer, R.T.4    Baker, T.A.5
  • 26
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko, I., M. Seidel, R. T. Sauer, and T. A. Baker. 2000. A specificity-enhancing factor for the ClpXP degradation machine. Science 289:2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 27
    • 0037082125 scopus 로고    scopus 로고
    • Degradation of L-glutamate dehydrogenase from Escherichia coli: Allosteric regulation of enzyme stability
    • Maurizi, M. R., and F. Rasulova. 2002. Degradation of L-glutamate dehydrogenase from Escherichia coli: allosteric regulation of enzyme stability. Arch. Biochem. Biophys. 397:206-216.
    • (2002) Arch. Biochem. Biophys , vol.397 , pp. 206-216
    • Maurizi, M.R.1    Rasulova, F.2
  • 28
    • 13444282474 scopus 로고    scopus 로고
    • Mulder, N. J., R. Apweiler, T. K. Attwood, A. Bairoch, A. Bateman, D. Binns, P. Bradley, P. Bork, P. Bucher, L. Cerutti, R. Copley, E. Courcelle, U. Das, R. Durbin, W. Fleischmann, J. Cough, D. Haft, N. Harte, N. Hulo, D. Kahn, A. Kanapin, M. Krestyaninova, D. Lonsdale, R. Lopez, I. Letunic, M. Madera, J. Maslen, J. McDowall, A. Mitchell, A. N. Nikolskaya, S. Orchard, M. Pagni, C. P. Ponting, E. Quevillon, J. Selengut, C. J. Sigrist, V. Silventoinen, D. J. Studholme, R. Vaughan, and C. H. Wu. 2005. InterPro, progress and status in 2005. Nucleic Acids Res. 33:D201-D205.
    • Mulder, N. J., R. Apweiler, T. K. Attwood, A. Bairoch, A. Bateman, D. Binns, P. Bradley, P. Bork, P. Bucher, L. Cerutti, R. Copley, E. Courcelle, U. Das, R. Durbin, W. Fleischmann, J. Cough, D. Haft, N. Harte, N. Hulo, D. Kahn, A. Kanapin, M. Krestyaninova, D. Lonsdale, R. Lopez, I. Letunic, M. Madera, J. Maslen, J. McDowall, A. Mitchell, A. N. Nikolskaya, S. Orchard, M. Pagni, C. P. Ponting, E. Quevillon, J. Selengut, C. J. Sigrist, V. Silventoinen, D. J. Studholme, R. Vaughan, and C. H. Wu. 2005. InterPro, progress and status in 2005. Nucleic Acids Res. 33:D201-D205.
  • 29
    • 0043128700 scopus 로고    scopus 로고
    • Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine
    • Song, H. K., and M. J. Eck. 2003. Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine. Mol. Cell 12:75-86.
    • (2003) Mol. Cell , vol.12 , pp. 75-86
    • Song, H.K.1    Eck, M.J.2
  • 30
    • 0036848756 scopus 로고    scopus 로고
    • Characterization of a specificity factor for an AAA+ ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer
    • Wah, D. A., I. Levchenko, T. A. Baker, and R. T. Sauer. 2002. Characterization of a specificity factor for an AAA+ ATPase: assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chem. Biol. 9:1237-1245.
    • (2002) Chem. Biol , vol.9 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 31
    • 0032986721 scopus 로고    scopus 로고
    • Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium
    • Wang, L., M. Elliott, and T. Elliott. 1999. Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium. J. Bacteriol. 181:1211-1219.
    • (1999) J. Bacteriol , vol.181 , pp. 1211-1219
    • Wang, L.1    Elliott, M.2    Elliott, T.3
  • 32
    • 0035281566 scopus 로고    scopus 로고
    • The RssB response regulator directly targets sigma(S) for degradation by ClpXP
    • Zhou, Y., S. Gottesman, J. R. Hoskins, M. R. Maurizi, and S. Wickner. 2001. The RssB response regulator directly targets sigma(S) for degradation by ClpXP. Genes Dev. 15:627-637.
    • (2001) Genes Dev , vol.15 , pp. 627-637
    • Zhou, Y.1    Gottesman, S.2    Hoskins, J.R.3    Maurizi, M.R.4    Wickner, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.