메뉴 건너뛰기




Volumn 184, Issue 23, 2002, Pages 6635-6641

Degradation of a Caulobacter soluble cytoplasmic chemoreceptor is ClpX dependent

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ENDOPEPTIDASE CLPX; GENE PRODUCT; UNCLASSIFIED DRUG;

EID: 0036889290     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.23.6635-6642.2002     Document Type: Article
Times cited : (29)

References (34)
  • 1
    • 0034931520 scopus 로고    scopus 로고
    • The highly conserved domain of the Caulobacter McpA chemoreceptor is required for its polar localization
    • Alley, M. R. K. 2001. The highly conserved domain of the Caulobacter McpA chemoreceptor is required for its polar localization. Mol. Microbiol. 40:1335-1343.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1335-1343
    • Alley, M.R.K.1
  • 2
    • 0026009504 scopus 로고
    • Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus
    • Alley, M. R. K., S. L. Gomes, W. Alexander, and L. Shapiro. 1991. Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus. Genetics 129:333-341.
    • (1991) Genetics , vol.129 , pp. 333-341
    • Alley, M.R.K.1    Gomes, S.L.2    Alexander, W.3    Shapiro, L.4
  • 3
    • 0026628961 scopus 로고
    • Polar localization of a bacterial chemoreceptor
    • Alley, M. R. K., J. R. Maddock, and L. Shapiro. 1992. Polar localization of a bacterial chemoreceptor. Genes Dev. 6:825-836.
    • (1992) Genes Dev. , vol.6 , pp. 825-836
    • Alley, M.R.K.1    Maddock, J.R.2    Shapiro, L.3
  • 4
    • 0027409274 scopus 로고
    • Requirement of the carboxyl terminus of a bacterial chemoreceptor for its targeted proteolysis
    • Alley, M. R. K., J. R. Maddock, and L. Shapiro. 1993. Requirement of the carboxyl terminus of a bacterial chemoreceptor for its targeted proteolysis. Science 259:1754-1757.
    • (1993) Science , vol.259 , pp. 1754-1757
    • Alley, M.R.K.1    Maddock, J.R.2    Shapiro, L.3
  • 5
    • 0032875385 scopus 로고    scopus 로고
    • Efficient adaptational demethylation of chemoreceptors requires the same enzymedocking site as efficient methylation
    • Barnakov, A. N., L. A. Barnakova, and G. L. Hazelbauer. 1999. Efficient adaptational demethylation of chemoreceptors requires the same enzymedocking site as efficient methylation. Proc. Natl. Acad. Sci. USA 96:10667-10672.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10667-10672
    • Barnakov, A.N.1    Barnakova, L.A.2    Hazelbauer, G.L.3
  • 6
    • 0018926910 scopus 로고
    • Multiple electrophoretic forms of methyl-accepting chemotaxis proteins generated by stimulus-elicited methylation in Escherichia coli
    • Boyd, A., and M. I. Simon. 1980. Multiple electrophoretic forms of methyl-accepting chemotaxis proteins generated by stimulus-elicited methylation in Escherichia coli. J. Bacteriol. 143:809-815.
    • (1980) J. Bacteriol. , vol.143 , pp. 809-815
    • Boyd, A.1    Simon, M.I.2
  • 7
    • 0034460297 scopus 로고    scopus 로고
    • How signals are heard during bacterial chemotaxis: Protein-protein interactions in sensory signal propagation
    • Bren, A., and M. Eisenbach. 2000. How signals are heard during bacterial chemotaxis: Protein-protein interactions in sensory signal propagation. J. Bacteriol. 182:6865-6873.
    • (2000) J. Bacteriol. , vol.182 , pp. 6865-6873
    • Bren, A.1    Eisenbach, M.2
  • 8
    • 0031944976 scopus 로고    scopus 로고
    • An archaeal aerotaxis transducer combines subunit I core structures of eukaryotic cytochrome c oxidase and eubacterial methyl-accepting chemotaxis proteins
    • Brooun, A., J. Bell, T. Freitas, R. W. Larsen, and M. Alam. 1998. An archaeal aerotaxis transducer combines subunit I core structures of eukaryotic cytochrome c oxidase and eubacterial methyl-accepting chemotaxis proteins. J. Bacteriol. 180:1642-1646.
    • (1998) J. Bacteriol. , vol.180 , pp. 1642-1646
    • Brooun, A.1    Bell, J.2    Freitas, T.3    Larsen, R.W.4    Alam, M.5
  • 9
  • 10
    • 0030272406 scopus 로고    scopus 로고
    • The control of temporal and spatial organization during the Caulobacter cell cycle
    • Domian, I. J., K. C. Quon, and L. Shapiro. 1996. The control of temporal and spatial organization during the Caulobacter cell cycle. Curr. Opin. Genet. Dev. 6:538-544.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 538-544
    • Domian, I.J.1    Quon, K.C.2    Shapiro, L.3
  • 11
    • 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
  • 12
    • 0033765068 scopus 로고    scopus 로고
    • Evolutionary conservation of methyl-accepting chemotaxis protein location in Bacteria and Archaea
    • Gestwicki, J. E., A. C. Lamanna, R. M. Harshey, L. L. McCarter, L. L. Kiessling, and J. Adler. 2000. Evolutionary conservation of methyl-accepting chemotaxis protein location in Bacteria and Archaea. J. Bacteriol. 182:6499-6502.
    • (2000) J. Bacteriol. , vol.182 , pp. 6499-6502
    • Gestwicki, J.E.1    Lamanna, A.C.2    Harshey, R.M.3    McCarter, L.L.4    Kiessling, L.L.5    Adler, J.6
  • 13
    • 0026236990 scopus 로고
    • Positional information during Caulobacter cell differentiation
    • Gober, J. W., M. R. K. Alley, and L. Shapiro. 1991. Positional information during Caulobacter cell differentiation. Curr. Opin. Genet. Dev. 1:324-329.
    • (1991) Curr. Opin. Genet. Dev. , vol.1 , pp. 324-329
    • Gober, J.W.1    Alley, M.R.K.2    Shapiro, L.3
  • 15
    • 0032958359 scopus 로고    scopus 로고
    • Localization and environmental regulation of MCP-like proteins in Rhodobacter sphaeroides
    • Harrison, D. M., J. Skidmore, J. P. Armitage, and J. R. Maddock. 1999. Localization and environmental regulation of MCP-like proteins in Rhodobacter sphaeroides. Mol. Microbiol. 31:885-892.
    • (1999) Mol. Microbiol. , vol.31 , pp. 885-892
    • Harrison, D.M.1    Skidmore, J.2    Armitage, J.P.3    Maddock, J.R.4
  • 18
    • 0032189273 scopus 로고    scopus 로고
    • An essential protease involved in bacterial cell-cycle control
    • Jenal, U., and T. Fuchs. 1998. An essential protease involved in bacterial cell-cycle control. EMBO J. 17:5658-5669.
    • (1998) EMBO J. , vol.17 , pp. 5658-5669
    • Jenal, U.1    Fuchs, T.2
  • 19
    • 0029936883 scopus 로고    scopus 로고
    • Cell cycle-controlled proteolysis of a flagellar motor protein that is asymmetrically distributed in the Caulobacter predivisional cell
    • Jenal, U., and L. Shapiro. 1996. Cell cycle-controlled proteolysis of a flagellar motor protein that is asymmetrically distributed in the Caulobacter predivisional cell. EMBO J. 15:2393-2406.
    • (1996) EMBO J. , vol.15 , pp. 2393-2406
    • Jenal, U.1    Shapiro, L.2
  • 20
    • 0001690764 scopus 로고    scopus 로고
    • Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
    • Kim, K. K., H. Yokota, and S. H. Kim. 1999. Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor. Nature 400:787-792.
    • (1999) Nature , vol.400 , pp. 787-792
    • Kim, K.K.1    Yokota, H.2    Kim, S.H.3
  • 21
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • Kim, Y. I., R. E. Burton, B. M. Burton, R. T. Sauer, and T. A. Baker. 2000. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell 5:639-648.
    • (2000) Mol. Cell , vol.5 , pp. 639-648
    • Kim, Y.I.1    Burton, R.E.2    Burton, B.M.3    Sauer, R.T.4    Baker, T.A.5
  • 22
    • 0021762876 scopus 로고
    • Caulobacter crescentus flagellar filament has a right-handed helical form
    • Koyasu, S., and Y. Shirakihara. 1984. Caulobacter crescentus flagellar filament has a right-handed helical form. J. Mol. Biol. 173:125-130.
    • (1984) J. Mol. Biol. , vol.173 , pp. 125-130
    • Koyasu, S.1    Shirakihara, Y.2
  • 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. M. 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.M.4    Shapiro, L.5
  • 24
    • 0031457264 scopus 로고    scopus 로고
    • PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits
    • Levchenko, I., C. K. Smith, N. P. Walsh, R. T. Sauer, and T. A. Baker. 1997. PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell 91:939-947.
    • (1997) Cell , vol.91 , pp. 939-947
    • Levchenko, I.1    Smith, C.K.2    Walsh, N.P.3    Sauer, R.T.4    Baker, T.A.5
  • 25
    • 0027476771 scopus 로고
    • Polar location of the chemoreceptor complex in the Escherichia coli cell
    • Maddock, J. R., and L. Shapiro. 1993. Polar location of the chemoreceptor complex in the Escherichia coli cell. Science 259:1717-1723.
    • (1993) Science , vol.259 , pp. 1717-1723
    • Maddock, J.R.1    Shapiro, L.2
  • 26
    • 0031016796 scopus 로고    scopus 로고
    • Isolation and characterization of a xylose-dependent promoter from Caulobacter crescentus
    • Meisenzahl, A. C., L. Shapiro, and U. Jenal. 1997. Isolation and characterization of a xylose-dependent promoter from Caulobacter crescentus. J. Bacteriol. 179:592-600.
    • (1997) J. Bacteriol. , vol.179 , pp. 592-600
    • Meisenzahl, A.C.1    Shapiro, L.2    Jenal, U.3
  • 28
    • 0031945269 scopus 로고    scopus 로고
    • Chemotactic adaptation is altered by changes in the carboxy-terminal sequence conserved among the major methyl-accepting chemoreceptors
    • Okumura, H., S. Nishiyama, A. Sasaki, M. Homma, and I. Kawagishi. 1998. Chemotactic adaptation is altered by changes in the carboxy-terminal sequence conserved among the major methyl-accepting chemoreceptors. J. Bacteriol. 180:1862-1868.
    • (1998) J. Bacteriol. , vol.180 , pp. 1862-1868
    • Okumura, H.1    Nishiyama, S.2    Sasaki, A.3    Homma, M.4    Kawagishi, I.5
  • 29
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease
    • Ortega, J., S. K. Singh, T. Ishikawa, M. R. Maurizi, and A. C. Steven. 2000. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell 6:1515-1521.
    • (2000) ClpXP. Mol. Cell , vol.6 , pp. 1515-1521
    • Ortega, J.1    Singh, S.K.2    Ishikawa, T.3    Maurizi, M.R.4    Steven, A.C.5
  • 30
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 31
    • 0030886946 scopus 로고    scopus 로고
    • Identification of the fliI and fliJ components of the Caulobacter flagellar type III protein secretion system
    • Stephens, C., C. Mohr, C. Boyd, J. Maddock, J. Gober, and L. Shapiro. 1997. Identification of the fliI and fliJ components of the Caulobacter flagellar type III protein secretion system. J. Bacteriol. 179:5355-5365.
    • (1997) J. Bacteriol. , vol.179 , pp. 5355-5365
    • Stephens, C.1    Mohr, C.2    Boyd, C.3    Maddock, J.4    Gober, J.5    Shapiro, L.6
  • 32
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 33
    • 0034884131 scopus 로고    scopus 로고
    • Proteolysis of the Caulobacter McpA chemoreceptor is cell cycle regulated by a ClpX-dependent pathway
    • Tsai, J. W., and M. R. K. Alley. 2001. Proteolysis of the Caulobacter McpA chemoreceptor is cell cycle regulated by a ClpX-dependent pathway. J. Bacteriol, 183:5001-5007.
    • (2001) J. Bacteriol. , vol.183 , pp. 5001-5007
    • Tsai, J.W.1    Alley, M.R.K.2
  • 34
    • 0033989004 scopus 로고    scopus 로고
    • Proteolysis of the McpA chemoreceptor does not require the Caulobacter major chemotaxis operon
    • Tsai, J. W., and M. R. K. Alley. 2000. Proteolysis of the McpA chemoreceptor does not require the Caulobacter major chemotaxis operon. J. Bacteriol. 182:504-507.
    • (2000) J. Bacteriol. , vol.182 , pp. 504-507
    • Tsai, J.W.1    Alley, M.R.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.