메뉴 건너뛰기




Volumn 41, Issue 5, 2001, Pages 1159-1172

A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE;

EID: 0035788801     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2001.02576.x     Document Type: Article
Times cited : (143)

References (44)
  • 2
    • 0033609929 scopus 로고    scopus 로고
    • Functional analysis of paralogous thioldisulfide oxidoreductases in Bacillus subtilis
    • Bolhuis, A., Venema, G., Quax, W.J., Bron, S., and van Dijl, J.M. (1999a) Functional analysis of paralogous thioldisulfide oxidoreductases in Bacillus subtilis. J Biol Chem 274: 24531-24538.
    • (1999) J Biol Chem , vol.274 , pp. 24531-24538
    • Bolhuis, A.1    Venema, G.2    Quax, W.J.3    Bron, S.4    Van Dijl, J.M.5
  • 3
    • 0032975058 scopus 로고    scopus 로고
    • Evaluation of bottlenecks in the late stages of protein secretion in Bacillus subtilis
    • Bolhuis, A., Tjalsma, H., Smith, H.E., de Jong, A., Meima, R., Venema, G., et al. (1999b) Evaluation of bottlenecks in the late stages of protein secretion in Bacillus subtilis. Appl Environ Microbiol 65: 2934-2941.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2934-2941
    • Bolhuis, A.1    Tjalsma, H.2    Smith, H.E.3    De Jong, A.4    Meima, R.5    Venema, G.6
  • 4
    • 0033024029 scopus 로고    scopus 로고
    • Different mechanisms for thermal inactivation of Bacillus subtilis signal peptidase mutants
    • Bolhuis, A., Tjalsma, H., Stephenson, K., Harwood, C.R., Venema, G., Bron, S., and van Dijl, J.M. (1999c) Different mechanisms for thermal inactivation of Bacillus subtilis signal peptidase mutants. J Biol Chem 274: 15865-15868.
    • (1999) J Biol Chem , vol.274 , pp. 15865-15868
    • Bolhuis, A.1    Tjalsma, H.2    Stephenson, K.3    Harwood, C.R.4    Venema, G.5    Bron, S.6    Van Dijl, J.M.7
  • 5
    • 0033609854 scopus 로고    scopus 로고
    • Signal peptide peptidase- and ClpP-like proteins of Bacillus subtilis required for efficient translocation and processing of secretory proteins
    • Bolhuis, A., Matzen, A., Hyyryläinen, H.-L., Kontinen, V.P., Meima, R., Chapuis, J., et al. (1999d) Signal peptide peptidase- and ClpP-like proteins of Bacillus subtilis required for efficient translocation and processing of secretory proteins. J Biol Chem 274: 24585-24592.
    • (1999) J Biol Chem , vol.274 , pp. 24585-24592
    • Bolhuis, A.1    Matzen, A.2    Hyyryläinen, H.-L.3    Kontinen, V.P.4    Meima, R.5    Chapuis, J.6
  • 6
    • 0030763077 scopus 로고    scopus 로고
    • The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways
    • Connolly, L., De Las Peñas, A., Alba, B.M., and Gross, C.A. (1997) The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways. Genes Dev 11: 2012-2021.
    • (1997) Genes Dev , vol.11 , pp. 2012-2021
    • Connolly, L.1    De Las Peñas, A.2    Alba, B.M.3    Gross, C.A.4
  • 7
    • 0030998321 scopus 로고    scopus 로고
    • E and the Cpx signal transduction system control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • E and the Cpx signal transduction system control the synthesis of periplasmic protein-folding enzymes in Escherichia coli. Genes Dev 11: 1183-1193.
    • (1997) Genes Dev , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 8
    • 0032527831 scopus 로고    scopus 로고
    • A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
    • Dartigalongue, C., and Raina, S. (1998) A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J 17: 3968-3980.
    • (1998) EMBO J , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 10
    • 0032728835 scopus 로고    scopus 로고
    • The CpxRA signal transduction system of Escherichia coli: Growth-related autoactivation and control of unanticipated target operons
    • De Wulf, P., Kwon, O., and Lin, E.C. (1999) The CpxRA signal transduction system of Escherichia coli: growth-related autoactivation and control of unanticipated target operons. J Bacteriol 181: 6772-6778.
    • (1999) J Bacteriol , vol.181 , pp. 6772-6778
    • De Wulf, P.1    Kwon, O.2    Lin, E.C.3
  • 11
    • 0028966094 scopus 로고
    • Identification of the potential active site of the signal peptidase SipS of Bacillus subtilis
    • 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. 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
  • 12
    • 0029590029 scopus 로고
    • Antibiotic-resistance cassettes for Bacillus subtilis
    • Guérout-Fleury, A.M., Shazand, K., Frandsen, N., and Stragier, P. (1995) Antibiotic-resistance cassettes for Bacillus subtilis. Gene 167: 335-336.
    • (1995) Gene , vol.167 , pp. 335-336
    • Guérout-Fleury, A.M.1    Shazand, K.2    Frandsen, N.3    Stragier, P.4
  • 13
    • 0003008416 scopus 로고
    • Lethal phenotype conferred by xylose-induced overproduction of April-LacZ fusion protein
    • Zukowski, M.M., Ganesan, A.T., and Hoch, J.A. (eds). San Diego: Academic Press
    • Hastrup, S., and Jacobs, M.F. (1990) Lethal phenotype conferred by xylose-induced overproduction of April-LacZ fusion protein. In Genetics and Biotechnology of Bacilli. Zukowski, M.M., Ganesan, A.T., and Hoch, J.A. (eds). San Diego: Academic Press, pp. 33-41.
    • (1990) Genetics and Biotechnology of Bacilli , pp. 33-41
    • Hastrup, S.1    Jacobs, M.F.2
  • 14
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker, M., Schumann, W., and Volker, U. (1996) Heat-shock and general stress response in Bacillus subtilis. Mol Microbiol 19: 417-428.
    • (1996) Mol Microbiol , vol.19 , pp. 417-428
    • Hecker, M.1    Schumann, W.2    Volker, U.3
  • 15
    • 0034282698 scopus 로고    scopus 로고
    • D-alanine substitution of teichoic acids as a mudulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis
    • Hyyryläinen, H.-L., Vitikainen, M., Thwaite, J., Wu, H., Sarvas, M., Harwood, C.R., et al. (2000) D-alanine substitution of teichoic acids as a mudulator of protein folding and stability at the cytoplasmic membrane/cell wall interface of Bacillus subtilis. J Biol Chem 275: 26696-26703.
    • (2000) J Biol Chem , vol.275 , pp. 26696-26703
    • Hyyryläinen, H.-L.1    Vitikainen, M.2    Thwaite, J.3    Wu, H.4    Sarvas, M.5    Harwood, C.R.6
  • 16
    • 0027264910 scopus 로고
    • Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequence
    • Jacobs, M., Anderssen, J.B., Kontinen, V., and Sarvas, M. (1993) Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequence. Mol Microbiol 8: 957-966.
    • (1993) Mol Microbiol , vol.8 , pp. 957-966
    • Jacobs, M.1    Anderssen, J.B.2    Kontinen, V.3    Sarvas, M.4
  • 17
    • 0027222723 scopus 로고
    • The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion
    • Kontinen, V.P., and Sarvas, M. (1993) The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion. Mol Microbiol 8: 727-737.
    • (1993) Mol Microbiol , vol.8 , pp. 727-737
    • Kontinen, V.P.1    Sarvas, M.2
  • 18
    • 0025906712 scopus 로고
    • A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export
    • Kontinen, V.P., Saris, P., and Sarvas, M. (1991) A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export. Mol Microbiol 5: 1273-1283.
    • (1991) Mol Microbiol , vol.5 , pp. 1273-1283
    • Kontinen, V.P.1    Saris, P.2    Sarvas, M.3
  • 19
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • Kunst, F., and Rapoport, G. (1995) Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis. J Bacteriol 177: 2403-2407.
    • (1995) J Bacteriol , vol.177 , pp. 2403-2407
    • Kunst, F.1    Rapoport, G.2
  • 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: 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5    Azevedo, V.6
  • 21
    • 0033043496 scopus 로고    scopus 로고
    • Lipid modification of prelipoproteins is dispensable for growth but essential for efficient protein secretion in Bacillus subtilis: Characterization of the lgt gene
    • Leskelä, S., Wahlström, E., Kontinen, V.P., and Sarvas, M. (1999a) Lipid modification of prelipoproteins is dispensable for growth but essential for efficient protein secretion in Bacillus subtilis: characterization of the lgt gene. Mol Microbiol 31: 1075-1085.
    • (1999) Mol Microbiol , vol.31 , pp. 1075-1085
    • Leskelä, S.1    Wahlström, E.2    Kontinen, V.P.3    Sarvas, M.4
  • 22
    • 0032956990 scopus 로고    scopus 로고
    • Ecs, an ABC transporter of Bacillus subtilis: Dual signal transduction functions affecting expression of secreted proteins, as well as their secretion
    • Leskelä, S., Wahlström, E., Hyyryläinen, H.-L., Jacobs, M., Palva, A., Sarvas, M., and Kontinen, V.P. (1999b) Ecs, an ABC transporter of Bacillus subtilis: dual signal transduction functions affecting expression of secreted proteins, as well as their secretion. Mol Microbiol 31: 533-543.
    • (1999) Mol Microbiol , vol.31 , pp. 533-543
    • Leskelä, S.1    Wahlström, E.2    Hyyryläinen, H.-L.3    Jacobs, M.4    Palva, A.5    Sarvas, M.6    Kontinen, V.P.7
  • 23
    • 0030444419 scopus 로고    scopus 로고
    • The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease
    • Margot, P., and Karamata, D. (1996) The wprA gene of Bacillus subtilis 168, expressed during exponential growth, encodes a cell-wall-associated protease. Microbiology 142: 3437-3444.
    • (1996) Microbiology , vol.142 , pp. 3437-3444
    • Margot, P.1    Karamata, D.2
  • 24
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY. Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1982) Experiments in Molecular Genetics. Cold Spring Harbor, NY. Cold Spring Harbor Laboratory Press.
    • (1982) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 25
    • 0031081341 scopus 로고    scopus 로고
    • Protein misfolding in the cell envelope of Escherichia coli: New signaling pathways
    • Missiakas, D., and Raina, S. (1997) Protein misfolding in the cell envelope of Escherichia coli: new signaling pathways. Trends Biochem Sci 22: 59-63.
    • (1997) Trends Biochem Sci , vol.22 , pp. 59-63
    • Missiakas, D.1    Raina, S.2
  • 26
    • 0031745718 scopus 로고    scopus 로고
    • The extracytoplasmic function sigma factors: Role and regulation
    • Missiakas, D., and Raina, S. (1998) The extracytoplasmic function sigma factors: role and regulation. Mol Microbiol 28: 1059-1066.
    • (1998) Mol Microbiol , vol.28 , pp. 1059-1066
    • Missiakas, D.1    Raina, S.2
  • 28
    • 0032456890 scopus 로고    scopus 로고
    • Identification of cpxR as a positive regulator essential for expression of the Shigella sonnei virF gene
    • Nakayama, S., and Watanabe, H. (1998) Identification of cpxR as a positive regulator essential for expression of the Shigella sonnei virF gene. J Bacteriol 180: 3522-3528.
    • (1998) J Bacteriol , vol.180 , pp. 3522-3528
    • Nakayama, S.1    Watanabe, H.2
  • 29
    • 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
  • 30
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen, M.J., and Wren, B.W. (1997) The HtrA family of serine proteases. Mol Microbiol 26: 209-221.
    • (1997) Mol Microbiol , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 31
    • 0020438726 scopus 로고
    • Molecular cloning of α-amylase gene from Bacillus amyloliquefaciens and its expression in Bacillus subtilis
    • Palva, I. (1982) Molecular cloning of α-amylase gene from Bacillus amyloliquefaciens and its expression in Bacillus subtilis. Gene 19: 81-87.
    • (1982) Gene , vol.19 , pp. 81-87
    • Palva, I.1
  • 32
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • Pogliano, J., Lynch, A.S., Belin, D., Lin, E.C.C., and Beckwith, J. (1997) Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev 11: 1169-1182.
    • (1997) Genes Dev , vol.11 , pp. 1169-1182
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lin, E.C.C.4    Beckwith, J.5
  • 36
    • 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
  • 37
    • 0031926846 scopus 로고    scopus 로고
    • Influence of a cell-wall-associated protease on production of α-amylase by Bacillus subtilis
    • Stephenson, K., and Harwood, C.R. (1998) Influence of a cell-wall-associated protease on production of α-amylase by Bacillus subtilis. Appl Environ Microbiol 64: 2875-2881.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2875-2881
    • Stephenson, K.1    Harwood, C.R.2
  • 38
    • 0032479216 scopus 로고    scopus 로고
    • The influence of protein folding on late stages of the secretion of α-amylases from Bacillus subtilis
    • Stephenson, K., Carter, N.M., Harwood, C.R., Petit-Glatron, M.F., and Chambert, R. (1998) The influence of protein folding on late stages of the secretion of α-amylases from Bacillus subtilis. FEBS Lett 430: 385-389.
    • (1998) FEBS Lett , vol.430 , pp. 385-389
    • Stephenson, K.1    Carter, N.M.2    Harwood, C.R.3    Petit-Glatron, M.F.4    Chambert, R.5
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 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.H., 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.H.3    Bron, S.4    Van Dijl, J.M.5
  • 41
    • 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. Microbiology 144: 3097-3104.
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 42
    • 0035108399 scopus 로고    scopus 로고
    • Quantitation of the capacity of the secretion apparatus and the requirement for PrsA in the growth and secretion of α-amylase in Bacillus subtilis
    • Vitikainen, M., Pummi, T., Airaksinen, U., Wahlström, E., Wu, H., Sarvas, M., and Kontinen, V.P., (2001) Quantitation of the capacity of the secretion apparatus and the requirement for PrsA in the growth and secretion of α-amylase in Bacillus subtilis. J Bacteriol 183: 1881-1890.
    • (2001) J Bacteriol , vol.183 , pp. 1881-1890
    • Vitikainen, M.1    Pummi, T.2    Airaksinen, U.3    Wahlström, E.4    Wu, H.5    Sarvas, M.6    Kontinen, V.P.7
  • 43
    • 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
  • 44
    • 0033118799 scopus 로고    scopus 로고
    • Regulation of the heat-shock response
    • Yura, T., and Nakahigashi, K. (1999) Regulation of the heat-shock response. Curr Opin Microbiol 2: 153-158.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 153-158
    • Yura, T.1    Nakahigashi, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.