메뉴 건너뛰기




Volumn 49, Issue 1, 2003, Pages 143-156

The extracellular proteome of Bacillus subtilis under secretion stress conditions

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; HTRA PROTEASE; PROTEIN YQXL; PROTEINASE; PROTEOME; UNCLASSIFIED DRUG;

EID: 10744222163     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03565.x     Document Type: Article
Times cited : (96)

References (39)
  • 2
    • 0036244046 scopus 로고    scopus 로고
    • Stabilization of cell wall proteins in Bacillus subtilis: A proteomic approach
    • Antelmann, H., Yamamoto, H., Sekiguchi, J., and Hecker, M. (2002) Stabilization of cell wall proteins in Bacillus subtilis: a proteomic approach. Proteomics 2: 591-602.
    • (2002) Proteomics , vol.2 , pp. 591-602
    • Antelmann, H.1    Yamamoto, H.2    Sekiguchi, J.3    Hecker, M.4
  • 3
    • 84988074679 scopus 로고
    • Improved silver-staining of plant proteins, RNA and DNA polyacrylamide gels
    • Blum, H., Beier, H., and Gross, H.J. (1987) Improved silver-staining of plant proteins, RNA and DNA polyacrylamide gels. Electrophoresis 8: 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 4
    • 0032516913 scopus 로고    scopus 로고
    • SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins
    • Bolhuis, A., Broekhuizen, C.P., Sorokin, A., van Roosmalen, M.L., Venema, G., Bron, S., et al. (1998) SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins. J Biol Chem 273: 21217-21224.
    • (1998) J Biol Chem , vol.273 , pp. 21217-21224
    • Bolhuis, A.1    Broekhuizen, C.P.2    Sorokin, A.3    Van Roosmalen, M.L.4    Venema, G.5    Bron, S.6
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0034837018 scopus 로고    scopus 로고
    • A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis
    • Buttner, K., Bernhardt, J., Scharf, C., Schmid, R., Mader, U., Eymann, C., et al. (2001) A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis. Electrophoresis 22: 2908-2935.
    • (2001) Electrophoresis , vol.22 , pp. 2908-2935
    • Buttner, K.1    Bernhardt, J.2    Scharf, C.3    Schmid, R.4    Mader, U.5    Eymann, C.6
  • 7
    • 17744415288 scopus 로고    scopus 로고
    • Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element
    • Chong, S., Mersha, F.B., Comb, D.G., Scott, M.E., Landry, D., Vence, L.M., et al. (1997) Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene 192: 271-281.
    • (1997) Gene , vol.192 , pp. 271-281
    • Chong, S.1    Mersha, F.B.2    Comb, D.G.3    Scott, M.E.4    Landry, D.5    Vence, L.M.6
  • 8
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: Implications for protein composition cell fate
    • Clausen, T., Southan, C., and Ehrmann, M. (2002) The HtrA family of proteases: implications for protein composition cell fate. Mol Cell 10: 443-455.
    • (2002) Mol Cell , vol.10 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrmann, M.3
  • 9
    • 0036786262 scopus 로고    scopus 로고
    • A novel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of Bacillus subtilis
    • Darmon, E., Noone, D., Masson, A., Bron, S., Kuipers, O.P., Devine, K.M., and Van Dijl, J.M. (2002) A novel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of Bacillus subtilis. J Bacteriol 184: 5661-5671.
    • (2002) J Bacteriol , vol.184 , pp. 5661-5671
    • Darmon, E.1    Noone, D.2    Masson, A.3    Bron, S.4    Kuipers, O.P.5    Devine, K.M.6    Van Dijl, J.M.7
  • 10
    • 0028966094 scopus 로고
    • Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases
    • van Dijl, J.M., de Jong, A., Venema, G., and Bron, S. (1995) Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis. Structural and functional similarities with LexA-like proteases. J Biol Chem 270: 3611-3618.
    • (1995) J Biol Chem , vol.270 , pp. 3611-3618
    • Van Dijl, J.M.1    De Jong, A.2    Venema, G.3    Bron, S.4
  • 11
    • 0002317159 scopus 로고    scopus 로고
    • Protein transport pathways in Bacillus subtilis: A genome-based road map
    • Sonenshein, A.L., Hoch, J.A and Losick, R., (eds). Washington, DC: American Society for Microbiology Press
    • van Dijl, J.M., Bolhuis, A., Tjalsma, H., Jongbloed, J.D.H., de Jong, A., and Bron, S. (2001) Protein transport pathways in Bacillus subtilis: a genome-based road map. In Bacillus Subtilis and its Closest Relatvies: from Genes to Cells. Sonenshein, A.L., Hoch, J.A and Losick, R., (eds). Washington, DC: American Society for Microbiology Press, pp. 337-355.
    • (2001) Bacillus Subtilis and Its Closest Relatvies: From Genes to Cells , pp. 337-355
    • Van Dijl, J.M.1    Bolhuis, A.2    Tjalsma, H.3    Jongbloed, J.D.H.4    De Jong, A.5    Bron, S.6
  • 12
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman, S. (1996) Proteases and their targets in Escherichia coli. Annu Rev Genet 30: 465-506.
    • (1996) Annu Rev Genet , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 13
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman, S., Wickner, S., and Maurizi, M.R. (1997) Protein quality control: triage by chaperones and proteases. Genes Dev 11: 815-823.
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 14
    • 0034118606 scopus 로고    scopus 로고
    • Proteomics, DNA arrays and the analysis of still unknown regulons and unknown proteins of Bacillus subtilis and pathogenic Gram-positive bacteria
    • Hecker, M., and Engelmann, S. (2000) Proteomics, DNA arrays and the analysis of still unknown regulons and unknown proteins of Bacillus subtilis and pathogenic Gram-positive bacteria. Int J Medical Microbiol 290: 123-134.
    • (2000) Int J Medical Microbiol , vol.290 , pp. 123-134
    • Hecker, M.1    Engelmann, S.2
  • 15
    • 0035788801 scopus 로고    scopus 로고
    • A novel two-component regulatory system of Bacillus subtilis for the survival of severe secretion stress
    • Hyyrylänen, H.K., Bolhuis, A., Darmon, E., Muukkonen, L., Koski, P., Vitikainen, M., et al. (2001) A novel two-component regulatory system of Bacillus subtilis for the survival of severe secretion stress. Mol Microbiol 41: 1159-1172.
    • (2001) Mol Microbiol , vol.41 , pp. 1159-1172
    • Hyyrylänen, H.K.1    Bolhuis, A.2    Darmon, E.3    Muukkonen, L.4    Koski, P.5    Vitikainen, M.6
  • 16
    • 0030605248 scopus 로고    scopus 로고
    • A xylose-inducible Bacillus subtilis integration vector and its application
    • Kim, L., Mogk, A., and Schumann, W. (1996) A xylose-inducible Bacillus subtilis integration vector and its application. Gene 181: 71-76.
    • (1996) Gene , vol.181 , pp. 71-76
    • Kim, L.1    Mogk, A.2    Schumann, W.3
  • 17
    • 0037458675 scopus 로고    scopus 로고
    • Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima
    • Kim, D.Y., Kim, D.R., Ha, S.C., Lokanath, N.K., Lee, C.J., Hwang, H.Y., and Kim, K.K. (2003) Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima. J Biol Chem 278: 6543-6551.
    • (2003) J Biol Chem , vol.278 , pp. 6543-6551
    • Kim, D.Y.1    Kim, D.R.2    Ha, S.C.3    Lokanath, N.K.4    Lee, C.J.5    Hwang, H.Y.6    Kim, K.K.7
  • 18
    • 0035212494 scopus 로고    scopus 로고
    • Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems
    • Kobayashi, K., Ogura, M., Yamaguchi, H., Yoshida, K., Ogasawara, N., Tanaka, T., and Fujita, Y. (2001) Comprehensive DNA microarray analysis of Bacillus subtilis two-component regulatory systems. J Bacteriol 183: 7365-7370.
    • (2001) J Bacteriol , vol.183 , pp. 7365-7370
    • Kobayashi, K.1    Ogura, M.2    Yamaguchi, H.3    Yoshida, K.4    Ogasawara, N.5    Tanaka, T.6    Fujita, Y.7
  • 19
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M., and Clausen, T. (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416: 455-459.
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 20
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst, F., Ogasawara, N., Moszer, I., Albertini, A.M., Alloni, G., Azevedo, V., et al. (1997) The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 390: 246-256.
    • (1997) Nature , vol.390 , pp. 246-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5    Azevedo, V.6
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0030031254 scopus 로고    scopus 로고
    • Molecular analysis of an operon in Bacillus subtilis encoding a novel ABC transporter with a role in exoprotein production, sporulation and competence
    • Leskela, S., Kontinen, V.P., and Sarvas, M. (1996) Molecular analysis of an operon in Bacillus subtilis encoding a novel ABC transporter with a role in exoprotein production, sporulation and competence. Microbiology 142: 71-77.
    • (1996) Microbiology , vol.142 , pp. 71-77
    • Leskela, S.1    Kontinen, V.P.2    Sarvas, M.3
  • 23
    • 0036263973 scopus 로고    scopus 로고
    • Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi
    • Li, W., Srinivasula, S.M., Chai, J., Li, P., Wu, J.W., Zhang, Z., et al. (2002) Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. Nature Struct Biol 9: 436-441.
    • (2002) Nature Struct Biol , vol.9 , pp. 436-441
    • Li, W.1    Srinivasula, S.M.2    Chai, J.3    Li, P.4    Wu, J.W.5    Zhang, Z.6
  • 24
    • 0025784662 scopus 로고
    • Simultaneous and rapid isolation of bacterial and eukaryotic DNA and RNA: A new approach for isolating DNA
    • Majumdar, D., Avissar, Y.J., and Wyche, J.H. (1991) Simultaneous and rapid isolation of bacterial and eukaryotic DNA and RNA: a new approach for isolating DNA. Biotechniques 11: 94-101.
    • (1991) Biotechniques , vol.11 , pp. 94-101
    • Majumdar, D.1    Avissar, Y.J.2    Wyche, J.H.3
  • 25
    • 0036260673 scopus 로고    scopus 로고
    • Love it or cleave it: Tough choices in protein quality control
    • Maurizi, M.R. (2002) Love it or cleave it: tough choices in protein quality control. Nature Struct Biol 9: 410-412.
    • (2002) Nature Struct Biol , vol.9 , pp. 410-412
    • Maurizi, M.R.1
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1982) Experiments in Molecular Genetics. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
    • (1982) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 27
    • 0034049557 scopus 로고    scopus 로고
    • Expression of ykdA, encoding a Bacillus subtilis homologue of HtrA, is heat shock inducible and negatively autoregulated
    • Noone, D., Howell, A., and Devine, K.M. (2000) Expression of ykdA, encoding a Bacillus subtilis homologue of HtrA, is heat shock inducible and negatively autoregulated. J Bacteriol 182: 1592-1599.
    • (2000) J Bacteriol , vol.182 , pp. 1592-1599
    • Noone, D.1    Howell, A.2    Devine, K.M.3
  • 28
    • 0035156736 scopus 로고    scopus 로고
    • YkdA and YvtA, HtrA-like serine proteases in Bacillus subtilis, engage in negative autoregulation and reciprocal cross-regulation of ykdA and yvtA gene expression
    • Noone, D., Howell, A., Collery, R., and Devine, K.M. (2001) YkdA and YvtA, HtrA-like serine proteases in Bacillus subtilis, engage in negative autoregulation and reciprocal cross-regulation of ykdA and yvtA gene expression. J Bacteriol 183: 654-663.
    • (2001) J Bacteriol , vol.183 , pp. 654-663
    • Noone, D.1    Howell, A.2    Collery, R.3    Devine, K.M.4
  • 29
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J.S., and Kofoid, E.C. (1992) Communication modules in bacterial signaling proteins. Annu Rev Genet 26: 71-112.
    • (1992) Annu Rev Genet , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 31
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., Beil, A., and Ehrmann, M. (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97: 339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 32
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock, J.B., Ninfa, A.J., and Stock, A.M. (1989) Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol Rev 53: 450-490.
    • (1989) Microbiol Rev , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 34
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma, H., Bolhuis, A., Jongbloed, J.D., Bron, S., and van Dijl, J.M. (2000) Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol Mol Biol Rev 64: 515-547.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    Van Dijl, J.M.5
  • 35
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner, V., Dervyn, E., and Ehrlich, S.D. (1998) A vector for systematic gene inactivation in Bacillus subtilis. Microbiol 144: 3097-3104.
    • (1998) Microbiol , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 36
    • 0022917641 scopus 로고
    • Host/vector interactions which affect the viability of recombinant phage lambda clones
    • Wertman, K.F., Wyman, A.R., and Botstein, D. (1986) Host/vector interactions which affect the viability of recombinant phage lambda clones. Gene 49: 253-262.
    • (1986) Gene , vol.49 , pp. 253-262
    • Wertman, K.F.1    Wyman, A.R.2    Botstein, D.3
  • 37
    • 0026750167 scopus 로고
    • Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis
    • Wetzstein, M., Volker, U., Dedio, J., Lobau, S., Zuber, U., Schiesswohl, M., et al. (1992) Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis. J Bacteriol 174: 3300-3310.
    • (1992) J Bacteriol , vol.174 , pp. 3300-3310
    • Wetzstein, M.1    Volker, U.2    Dedio, J.3    Lobau, S.4    Zuber, U.5    Schiesswohl, M.6
  • 38
    • 0033520987 scopus 로고    scopus 로고
    • Post-translational quality control: Folding, refolding, and degrading proteins
    • Wickner, S., Maurizi, M.R., and Gottesman, S. (1999) Post-translational quality control: folding, refolding, and degrading proteins. Science 286: 1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 39
    • 0033524383 scopus 로고    scopus 로고
    • High-level secretory production of intact, biologically active staphylokinase from Bacillus subtilis
    • Ye, R., Kim, J.H., Kim, B.G., Szarka, S., Sihota, E., and Wong, S.L. (1999) High-level secretory production of intact, biologically active staphylokinase from Bacillus subtilis. Biotechnol Bioeng 62: 87-96.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 87-96
    • Ye, R.1    Kim, J.H.2    Kim, B.G.3    Szarka, S.4    Sihota, E.5    Wong, S.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.