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Volumn 65, Issue 7, 1999, Pages 2934-2941

Evaluation of bottlenecks in the late stages of protein secretion in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; BACTERIAL PROTEIN; BETA LACTAMASE; OXIDOREDUCTASE;

EID: 0032975058     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.65.7.2934-2941.1999     Document Type: Article
Times cited : (90)

References (46)
  • 1
    • 0002474503 scopus 로고
    • Cell wall structure, synthesis, and turnover
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), American Society for Microbiology, Washington, D.C.
    • Archibald, A. R., I. C. Hancock, and C. R. Harwood. 1993. Cell wall structure, synthesis, and turnover, p. 381-410. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria. American Society for Microbiology, Washington, D.C.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 381-410
    • Archibald, A.R.1    Hancock, I.C.2    Harwood, C.R.3
  • 2
    • 0029809574 scopus 로고    scopus 로고
    • Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase I
    • Bolhuis, A., A. Sorokin, V. Azevedo, S. D. Ehrlich, P. G. Braun, A. de Jong, G. Venema, S. Bran, and J. M. van Dijl. 1996. Bacillus subtilis can modulate its capacity and specificity for protein secretion through temporally controlled expression of the sipS gene for signal peptidase I. Mol. Microbiol. 22:605-618.
    • (1996) Mol. Microbiol. , vol.22 , pp. 605-618
    • Bolhuis, A.1    Sorokin, A.2    Azevedo, V.3    Ehrlich, S.D.4    Braun, P.G.5    De Jong, A.6    Venema, G.7    Bran, S.8    Van Dijl, J.M.9
  • 3
    • 0015335342 scopus 로고
    • Ultraviolet inactivation and excision repair in Bacillus subtilis. I. Construction and characterisation of a transformable eightfold auxotrophic strain and two ultraviolet-sensitive derivatives
    • Bron, S., and G. Venema. 1972. Ultraviolet inactivation and excision repair in Bacillus subtilis. I. Construction and characterisation of a transformable eightfold auxotrophic strain and two ultraviolet-sensitive derivatives. Mutat. Res. 15:1-10.
    • (1972) Mutat. Res. , vol.15 , pp. 1-10
    • Bron, S.1    Venema, G.2
  • 4
    • 0025191308 scopus 로고
    • Secretion of Bacillus subtilis levansucrase. Fe(III) could act as a cofactor in an efficient coupling of the folding and translocation processes
    • Chambert, R., F. Benyahia, and M. F. Petit-Glatron. 1990. Secretion of Bacillus subtilis levansucrase. Fe(III) could act as a cofactor in an efficient coupling of the folding and translocation processes. Biochem. J. 265:375-382.
    • (1990) Biochem. J. , vol.265 , pp. 375-382
    • Chambert, R.1    Benyahia, F.2    Petit-Glatron, M.F.3
  • 5
    • 0039281436 scopus 로고    scopus 로고
    • The chemistry and enzymology of the type I signal peptidases
    • Dalbey, R. E., M. O. Lively, S. Bron, and J. M. van Dijl. 1997. The chemistry and enzymology of the type I signal peptidases. Protein Sci. 17:474-478.
    • (1997) Protein Sci. , vol.17 , pp. 474-478
    • Dalbey, R.E.1    Lively, M.O.2    Bron, S.3    Van Dijl, J.M.4
  • 6
    • 0022545127 scopus 로고
    • Potential use of Bacillus subtilis for secretion and production of foreign proteins
    • Doi, R. H., S. L. Wong, and F. Kawamura. 1986. Potential use of Bacillus subtilis for secretion and production of foreign proteins. Trends Biotechnol. 4:232-235.
    • (1986) Trends Biotechnol. , vol.4 , pp. 232-235
    • Doi, R.H.1    Wong, S.L.2    Kawamura, F.3
  • 7
    • 0027967844 scopus 로고
    • How proteins cross the bacterial cytoplasmic membrane
    • Driessen, A. J. M. 1994. How proteins cross the bacterial cytoplasmic membrane. J. Membr. Biol. 142:145-159.
    • (1994) J. Membr. Biol. , vol.142 , pp. 145-159
    • Driessen, A.J.M.1
  • 8
    • 85069248282 scopus 로고    scopus 로고
    • Translocation of proteins across the bacterial membrane
    • W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Elsevier Science, Amsterdam, The Netherlands
    • Driessen, A. J. M. 1996. Translocation of proteins across the bacterial membrane, p. 759-790. In W. N. Konings, H. R. Kaback, and J. S. Lolkema (ed.), Handbook of biological physics. Transport processes in eukaryotic and prokaryotic membranes. Elsevier Science, Amsterdam, The Netherlands.
    • (1996) Handbook of Biological Physics. Transport Processes in Eukaryotic and Prokaryotic Membranes , pp. 759-790
    • Driessen, A.J.M.1
  • 9
    • 0022445340 scopus 로고
    • Expression of the staphylococcal protein A gene in Bacillus subtilis by gene fusions utilizing the promoter from a Bacillus amyloliquefaciens α-amylase gene
    • Fahnestock, S. R., and K. E. Fisher. 1986. Expression of the staphylococcal protein A gene in Bacillus subtilis by gene fusions utilizing the promoter from a Bacillus amyloliquefaciens α-amylase gene. J. Bacteriol. 165:796-804.
    • (1986) J. Bacteriol. , vol.165 , pp. 796-804
    • Fahnestock, S.R.1    Fisher, K.E.2
  • 10
    • 0024385258 scopus 로고
    • A protein of unusual composition from Enterococcus faecium
    • Furst, P., H. U. Mosch, and M. Solioz. 1989. A protein of unusual composition from Enterococcus faecium. Nucleic Acids Res. 17:6724.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6724
    • Furst, P.1    Mosch, H.U.2    Solioz, M.3
  • 12
    • 85069249362 scopus 로고    scopus 로고
    • Institut Pasteur. 11 June revision date. 1 February last date accessed
    • Institut Pasteur. 11 June 1998, revision date. Bacillus subtilis genome sequencing project. [Online.] http://www.pasteur.fr/Bio/SubtiList.html. [1 February 1999, last date accessed.]
    • (1998) Bacillus Subtilis Genome Sequencing Project. [Online.]
  • 13
    • 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-sequences
    • Jacobs, M., J. B. Andersen, V. Kontinen, and M. Sarvas. 1993. Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized either with or without pro-sequences Mol. Microbiol. 8:957-966.
    • (1993) Mol. Microbiol. , vol.8 , pp. 957-966
    • Jacobs, M.1    Andersen, J.B.2    Kontinen, V.3    Sarvas, M.4
  • 14
    • 0021193861 scopus 로고
    • Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neutral protease
    • Kawamura, F., and R. H. Doi. 1984. Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neutral protease. J. Bacteriol. 160:442-444.
    • (1984) J. Bacteriol. , vol.160 , pp. 442-444
    • Kawamura, F.1    Doi, R.H.2
  • 15
    • 0023227614 scopus 로고
    • A general method for the construction of Escherichia coli mutants by homologous recombination and plasmid segregation
    • Kiel, J. A., J. P. van der Vossen, and G. Venema. 1987. A general method for the construction of Escherichia coli mutants by homologous recombination and plasmid segregation. Mol. Gen. Genet. 207:294-301.
    • (1987) Mol. Gen. Genet. , vol.207 , pp. 294-301
    • Kiel, J.A.1    Van Der Vossen, J.P.2    Venema, G.3
  • 16
    • 0028173018 scopus 로고
    • Isolation and characterization of a Bacillus subtilis secA mutant allele conferring resistance to sodium azide
    • Klein, M., B. Hofmann, M. Klose, and R. Freudl. 1994. Isolation and characterization of a Bacillus subtilis secA mutant allele conferring resistance to sodium azide. FEMS Microbiol. Lett. 124:393-397.
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 393-397
    • Klein, M.1    Hofmann, B.2    Klose, M.3    Freudl, R.4
  • 17
    • 0025906712 scopus 로고
    • A gene (prsA) of Bacillus subtilis involved in a novel, late stage of protein export
    • Kantinen, V. P., P. Saris, and M. Sarvas. 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
    • Kantinen, V.P.1    Saris, P.2    Sarvas, M.3
  • 18
    • 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 M. Sarvas. 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
  • 20
    • 0030831592 scopus 로고    scopus 로고
    • Characterization of the rate-limiting step of the secretion of Bacillus subtilis alpha-amylase overproduced during the exponential phase of growth
    • Leloup, L., A. el Haddaoui, R. Chambert, and M. F. Petit-Glatron. 1997. Characterization of the rate-limiting step of the secretion of Bacillus subtilis alpha-amylase overproduced during the exponential phase of growth. Microbiology 143:3295-3303.
    • (1997) Microbiology , vol.143 , pp. 3295-3303
    • Leloup, L.1    El Haddaoui, A.2    Chambert, R.3    Petit-Glatron, M.F.4
  • 21
    • 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 D. Karamata. 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
  • 22
    • 0030841644 scopus 로고    scopus 로고
    • Use of the pre-pro part of Staphylococcus hyicus lipase as a carrier for secretion of Escherichia coli outer membrane protein A (OmpA) prevents proteolytic degradation of OmpA by a cell-associated protease(s) in two different gram-positive bacteria
    • Meens, J., M. Herbert, M. Klein, and R. Freudl. 1997. Use of the pre-pro part of Staphylococcus hyicus lipase as a carrier for secretion of Escherichia coli outer membrane protein A (OmpA) prevents proteolytic degradation of OmpA by a cell-associated protease(s) in two different gram-positive bacteria. Appl. Environ. Microbiol. 63:2814-2820.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2814-2820
    • Meens, J.1    Herbert, M.2    Klein, M.3    Freudl, R.4
  • 23
    • 0001914212 scopus 로고
    • Protein secretion
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), American Society for Microbiology, Washington, D.C.
    • Nagarajan, V. 1993. Protein secretion, p. 713-726. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria. American Society for Microbiology, Washington, D.C.
    • (1993) Bacillus Subtilis and Other Gram-positive Bacteria , pp. 713-726
    • Nagarajan, V.1
  • 24
    • 0020438726 scopus 로고
    • Molecular cloning of α-amylase gene from Bacillus amyloliquefaciens and its expression in B. subtilis
    • Palva, I. 1982. Molecular cloning of α-amylase gene from Bacillus amyloliquefaciens and its expression in B. subtilis. Gene 19:81-87.
    • (1982) Gene , vol.19 , pp. 81-87
    • Palva, I.1
  • 26
    • 0027297013 scopus 로고
    • The contribution of the cell wall to a transmembrane calcium gradient could play a key role in Bacillus subtilis protein secretion
    • Petit-Glatron, M. F., L. Grajcar, A. Munz, and R. Chambert. 1993. The contribution of the cell wall to a transmembrane calcium gradient could play a key role in Bacillus subtilis protein secretion. Mol. Microbiol. 9:1097-1106.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1097-1106
    • Petit-Glatron, M.F.1    Grajcar, L.2    Munz, A.3    Chambert, R.4
  • 27
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A, P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 29
  • 30
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and B. Dobberstein. 1996. Common principles of protein translocation across membranes. Science 271:1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 31
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simonen, M., and I. Palva. 1993. Protein secretion in Bacillus species. Microbiol. Rev. 57:109-137.
    • (1993) Microbiol. Rev. , vol.57 , pp. 109-137
    • Simonen, M.1    Palva, I.2
  • 32
    • 0023191360 scopus 로고
    • Construction and use of signal sequence selection vectors in Escherichia coli and Bacillus subtilis
    • Smith, H., S. Bron, J. van Ee, and G. Venema. 1987. Construction and use of signal sequence selection vectors in Escherichia coli and Bacillus subtilis. J. Bacteriol. 169:3321-3328.
    • (1987) J. Bacteriol. , vol.169 , pp. 3321-3328
    • Smith, H.1    Bron, S.2    Van Ee, J.3    Venema, G.4
  • 33
    • 0023823396 scopus 로고
    • Characterisation of signal-sequence-coding regions selected from the Bacillus subtilis chromosome
    • Smith, H., A. de Jong, S. Bron, and G. Venema. 1988. Characterisation of signal-sequence-coding regions selected from the Bacillus subtilis chromosome. Gene 70:351-361.
    • (1988) Gene , vol.70 , pp. 351-361
    • Smith, H.1    De Jong, A.2    Bron, S.3    Venema, G.4
  • 34
    • 0024344169 scopus 로고
    • Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers
    • Stanssens, P., C. Opsomer, Y. M. McKeown, W. Kramer, M. Zabeau, and H. J. Fritz. 1989. Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers. Nucleic Acids Res. 17:4441-4454.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4441-4454
    • Stanssens, P.1    Opsomer, C.2    McKeown, Y.M.3    Kramer, W.4    Zabeau, M.5    Fritz, H.J.6
  • 35
    • 0031926846 scopus 로고    scopus 로고
    • Influence of a cell-wall-associated protease on production of alpha-amylase by Bacillus subtilis
    • Stephenson, K., and C. R. Harwood. 1998. Influence of a cell-wall-associated protease on production of alpha-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
  • 36
    • 0030868265 scopus 로고    scopus 로고
    • Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities. Constitutive and temporally controlled expression of different sip genes
    • Tjalsma, H., M. A. Noback, S. Bron, G. Venema, K. Yamane, and J. M. van Dijl. 1997. Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities. Constitutive and temporally controlled expression of different sip genes. J. Biol. Chem. 272:25983-25992.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25983-25992
    • Tjalsma, H.1    Noback, M.A.2    Bron, S.3    Venema, G.4    Yamane, K.5    Van Dijl, J.M.6
  • 37
    • 0032146073 scopus 로고    scopus 로고
    • Functional analysis of the secretory precursor processing machinery of Bacillus subtilis; identification of a eubacterial homologue of archaeal and eukaryotic signal peptidases
    • Tjalsma, H., A. Bolhuis, M. L. van Roosmalen, T. Wiegert, W. Schumann, C. P. Broekhuizen, W. J. Quax, G. Venema, S. Bron, and J. M. van Dijl. 1998. Functional analysis of the secretory precursor processing machinery of Bacillus subtilis; identification of a eubacterial homologue of archaeal and eukaryotic signal peptidases. Genes Dev. 12:2318-2331.
    • (1998) Genes Dev. , vol.12 , pp. 2318-2331
    • Tjalsma, H.1    Bolhuis, A.2    Van Roosmalen, M.L.3    Wiegert, T.4    Schumann, W.5    Broekhuizen, C.P.6    Quax, W.J.7    Venema, G.8    Bron, S.9    Van Dijl, J.M.10
  • 38
    • 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
  • 39
    • 85069253098 scopus 로고
    • Signal peptidase I overproduction results in increased efficiencies of export and maturation of hybrid secretory proteins in Escherichia coli
    • van Dijl, J. M., A. de Jong, H. Smith, S. Bron, and G. Venema: 1991. Signal peptidase I overproduction results in increased efficiencies of export and maturation of hybrid secretory proteins in Escherichia coli. Mol. Gen. Genet. 223:233-240.
    • (1991) Mol. Gen. Genet. , vol.223 , pp. 233-240
    • Van Dijl, J.M.1    De Jong, A.2    Smith, H.3    Bron, S.4    Venema, G.5
  • 40
    • 0345512324 scopus 로고
    • Protein export in Bacillus subtilis and Escherichia coli
    • H. Heslot, J. Davies, J. Florent, L. Bobichen, G. Durand, and L. Penasse (ed.), Société Française de Microbiologie, Strasbourg, France
    • van Dijl, J. M., S. Bron, G. Venema, A. de Jong, and H. Smith. 1991. Protein export in Bacillus subtilis and Escherichia coli, p. 679-690. In H. Heslot, J. Davies, J. Florent, L. Bobichen, G. Durand, and L. Penasse (ed.), Proceedings of the 6th international Symposium on Genetics of Industrial Microorganisms. Société Française de Microbiologie, Strasbourg, France.
    • (1991) Proceedings of the 6th International Symposium on Genetics of Industrial Microorganisms , pp. 679-690
    • Van Dijl, J.M.1    Bron, S.2    Venema, G.3    De Jong, A.4    Smith, H.5
  • 41
    • 0026772152 scopus 로고
    • Signal peptidase I of Bacillus subtilis: Patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases
    • van Dijl, J. M., A. de Jong, J. Vehmaanperä, G. Venema, and S. Bron. 1992. Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases. EMBO J. 11:2819-2828.
    • (1992) EMBO J. , vol.11 , pp. 2819-2828
    • Van Dijl, J.M.1    De Jong, A.2    Vehmaanperä, J.3    Venema, G.4    Bron, S.5
  • 42
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne, G. 1990. The signal peptide. J. Membr. Biol. 115:195-201.
    • (1990) J. Membr. Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 44
    • 0032460995 scopus 로고    scopus 로고
    • Enhanced secretory production of a single-chain antibody fragment from Bacillus subtilis by coproduction of molecular chaperones
    • Wu, S. C., R. Ye, X. C. Wu, S. C. Ng, and S. L. Wong. 1998. Enhanced secretory production of a single-chain antibody fragment from Bacillus subtilis by coproduction of molecular chaperones. J. Bacteriol. 180:2830-2835.
    • (1998) J. Bacteriol. , vol.180 , pp. 2830-2835
    • Wu, S.C.1    Ye, R.2    Wu, X.C.3    Ng, S.C.4    Wong, S.L.5
  • 45
    • 0026338822 scopus 로고
    • Engineering a Bacillus subtilis expression-secretion system with a strain deficient in six extracellular proteases
    • Wu, X. C., W. Lee, L. Tran, and S. L. Wong. 1991. Engineering a Bacillus subtilis expression-secretion system with a strain deficient in six extracellular proteases. J. Bacteriol. 173:4952-4958.
    • (1991) J. Bacteriol. , vol.173 , pp. 4952-4958
    • Wu, X.C.1    Lee, W.2    Tran, L.3    Wong, S.L.4
  • 46
    • 14744300958 scopus 로고
    • Efficient production of a functional single-chain antidigoxin antibody via an engineered Bacillus subtilis expression-secretion system
    • Wu, X. C., S. C. Ng, R. I. Near, and S. L. Wong. 1993. Efficient production of a functional single-chain antidigoxin antibody via an engineered Bacillus subtilis expression-secretion system. Biotechnology 11:71-76.
    • (1993) Biotechnology , vol.11 , pp. 71-76
    • Wu, X.C.1    Ng, S.C.2    Near, R.I.3    Wong, S.L.4


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