메뉴 건너뛰기




Volumn 9, Issue 4, 2009, Pages 1018-1032

Overflow of a hyper-produced secretory protein from the Bacillus sec pathway into the Tat pathway for protein secretion as revealed by proteogenomics

Author keywords

Bacillus subtilis; Lipa; Secretion; Secretome; Tat

Indexed keywords

ESTERASE; PROTEIN LIPA; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

EID: 61349200775     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800580     Document Type: Article
Times cited : (22)

References (69)
  • 1
    • 33745218504 scopus 로고    scopus 로고
    • Protein secretion in the Archaea: Multiple paths towards a unique cell surface
    • Albers, S. V., Szabo, Z., Driessen, A. J., Protein secretion in the Archaea: Multiple paths towards a unique cell surface. Nat. Rev. Microbiol. 2006, 4, 537-547.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 537-547
    • Albers, S.V.1    Szabo, Z.2    Driessen, A.J.3
  • 3
    • 33749247804 scopus 로고    scopus 로고
    • Mapping the pathways to staphylococcal pathogenesis by comparative secretomics
    • Sibbald, M. J., Ziebandt, A. K., Engelmann, S., Hecker, M. et al., Mapping the pathways to staphylococcal pathogenesis by comparative secretomics. Microbiol. Mol. Biol. Rev. 2006, 70, 755-788.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 755-788
    • Sibbald, M.J.1    Ziebandt, A.K.2    Engelmann, S.3    Hecker, M.4
  • 4
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus sub-tilis: A genome-based survey of the secretome
    • Tjalsma, H., Bolhuis, A., Jongbloed, J. D., Bron, S. et al., Signal peptide-dependent protein transport in Bacillus sub-tilis: A genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 2000, 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
  • 5
    • 2942561968 scopus 로고    scopus 로고
    • Proteomics of protein secretion by Bacillus subtilis: Separating the "secrets" of the secretome
    • Tjalsma, H., Antelmann, H., Jongbloed, J. D., Braun, P. G. et al., Proteomics of protein secretion by Bacillus subtilis: Separating the "secrets" of the secretome. Microbiol. Mol. Biol. Rev. 2004, 68, 207-233.
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 207-233
    • Tjalsma, H.1    Antelmann, H.2    Jongbloed, J.D.3    Braun, P.G.4
  • 6
    • 0034891203 scopus 로고    scopus 로고
    • Translocation of proteins across the cell envelope of Gram-positive bacteria
    • van Wely, K. H., Swaving, J., Freudl, R., Driessen, A. J., Translocation of proteins across the cell envelope of Gram-positive bacteria. FEMS Microbiol. Rev. 2001, 25, 437-454.
    • (2001) FEMS Microbiol. Rev , vol.25 , pp. 437-454
    • van Wely, K.H.1    Swaving, J.2    Freudl, R.3    Driessen, A.J.4
  • 7
    • 0034821694 scopus 로고    scopus 로고
    • A proteomic view on genome-based signal peptide predictions
    • Antelmann, H., Tjalsma, H., Voigt, B., Ohlmeier, S. et al.,A proteomic view on genome-based signal peptide predictions. Genome Res. 2001, 11, 1484-1502.
    • (2001) Genome Res , vol.11 , pp. 1484-1502
    • Antelmann, H.1    Tjalsma, H.2    Voigt, B.3    Ohlmeier, S.4
  • 8
    • 0033895238 scopus 로고    scopus 로고
    • Phosphate starvation-inducible proteins of Bacillus subtilis: Proteomics and tran-scriptional analysis
    • Antelmann, H., Scharf, C., Hecker, M., Phosphate starvation-inducible proteins of Bacillus subtilis: Proteomics and tran-scriptional analysis. J. Bacteriol. 2000, 182, 4478-4490.
    • (2000) J. Bacteriol , vol.182 , pp. 4478-4490
    • Antelmann, H.1    Scharf, C.2    Hecker, M.3
  • 9
    • 10744222163 scopus 로고    scopus 로고
    • The extracellular proteome of Bacillus subtilis under secretion stress conditions
    • Antelmann, H., Darmon, E., Noone, D., Veening, J. W. et al., The extracellular proteome of Bacillus subtilis under secretion stress conditions. Mol. Microbiol. 2003, 49, 143-156.
    • (2003) Mol. Microbiol , vol.49 , pp. 143-156
    • Antelmann, H.1    Darmon, E.2    Noone, D.3    Veening, J.W.4
  • 10
    • 0033972848 scopus 로고    scopus 로고
    • Proteome analysis of Bacillus subtilis extracellular proteins: A two-dimensional protein electrophoretic study
    • Hirose, I., Sano, K., Shioda, I., Kumano, M. et al., Proteome analysis of Bacillus subtilis extracellular proteins: A two-dimensional protein electrophoretic study. Microbiology 2000, 146, 65-75.
    • (2000) Microbiology , vol.146 , pp. 65-75
    • Hirose, I.1    Sano, K.2    Shioda, I.3    Kumano, M.4
  • 11
    • 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. et al., The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 1997, 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4
  • 13
    • 57449107189 scopus 로고    scopus 로고
    • Bacillus
    • Goldman, E, Green, L, Eds, 2nd Edn, CRC Press, Boca Raton, FL
    • Zeigler, D. R., Perkins, J. B., Bacillus. in: Goldman, E., Green, L. (Eds.), Practical Handbook of Microbiology, 2nd Edn., CRC Press, Boca Raton, FL 2008.
    • (2008) Practical Handbook of Microbiology
    • Zeigler, D.R.1    Perkins, J.B.2
  • 14
    • 61349122924 scopus 로고    scopus 로고
    • Bron, S., Meima, R., van Dijl, J. M., Wipat, A., Harwood, C. R., Molecular biology and genetics of Bacillus species.in: Demain, A. L., Davies, J. E. (Eds.), The Manual of Industrial Microbiology andBiotechnology, 2nd Edn., ASM Press,USA 1999, pp. 392-416.
    • Bron, S., Meima, R., van Dijl, J. M., Wipat, A., Harwood, C. R., Molecular biology and genetics of Bacillus species.in: Demain, A. L., Davies, J. E. (Eds.), The Manual of Industrial Microbiology andBiotechnology, 2nd Edn., ASM Press,USA 1999, pp. 392-416.
  • 16
    • 33846611391 scopus 로고    scopus 로고
    • Feature-based reappraisal of the Bacillus sub-tilis exoproteome
    • Tjalsma, H., Feature-based reappraisal of the Bacillus sub-tilis exoproteome. Proteomics 2007, 7, 73-81.
    • (2007) Proteomics , vol.7 , pp. 73-81
    • Tjalsma, H.1
  • 17
    • 0025183758 scopus 로고
    • Protein targeting signals
    • von Heijne, G., Protein targeting signals. Curr. Opin. Cell Biol. 1990, 2, 604-608.
    • (1990) Curr. Opin. Cell Biol , vol.2 , pp. 604-608
    • von Heijne, G.1
  • 18
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne, G., The signal peptide. J. Membr. Biol. 1990, 115, 195-201.
    • (1990) J. Membr. Biol , vol.115 , pp. 195-201
    • von Heijne, G.1
  • 19
    • 33646837543 scopus 로고    scopus 로고
    • Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
    • Dabney-Smith, C., Mori, H., Cline, K., Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J. Biol. Chem. 2006, 281, 5476-5483.
    • (2006) J. Biol. Chem , vol.281 , pp. 5476-5483
    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
  • 20
    • 0035852327 scopus 로고    scopus 로고
    • Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways
    • Mori, H., Cline, K., Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways. Biochim. Biophys. Acta 2001, 1541, 80-90.
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 80-90
    • Mori, H.1    Cline, K.2
  • 21
    • 18844442890 scopus 로고    scopus 로고
    • The Tat pathway in bacteria and chloroplasts (review)
    • Muller, M., Klosgen, R. B., The Tat pathway in bacteria and chloroplasts (review). Mol. Membr. Biol. 2005, 22, 113-121.
    • (2005) Mol. Membr. Biol , vol.22 , pp. 113-121
    • Muller, M.1    Klosgen, R.B.2
  • 22
    • 8844280791 scopus 로고    scopus 로고
    • Tat-dependent protein targeting in prokaryotes and chloroplasts
    • Robinson, C., Bolhuis, A., Tat-dependent protein targeting in prokaryotes and chloroplasts. Biochim. Biophys. Acta 2004, 1694, 135-147.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 135-147
    • Robinson, C.1    Bolhuis, A.2
  • 23
    • 33644856642 scopus 로고    scopus 로고
    • Pathfinders and trail-blazers: A prokaryotic targeting system for transport of folded proteins
    • Sargent, F., Berks, B. C., Palmer, T., Pathfinders and trail-blazers: A prokaryotic targeting system for transport of folded proteins. FEMS Microbiol. Lett. 2006, 254, 198-207.
    • (2006) FEMS Microbiol. Lett , vol.254 , pp. 198-207
    • Sargent, F.1    Berks, B.C.2    Palmer, T.3
  • 24
    • 33845199230 scopus 로고    scopus 로고
    • The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor
    • Widdick, D. A., Dilks, K., Chandra, G., Bottrill, A. et al., The twin-arginine translocation pathway is a major route of protein export in Streptomyces coelicolor. Proc. Natl. Acad. Sci. USA 2006, 103, 17927-17932.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17927-17932
    • Widdick, D.A.1    Dilks, K.2    Chandra, G.3    Bottrill, A.4
  • 25
    • 0036276602 scopus 로고    scopus 로고
    • Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system
    • Yen, M. R., Tseng, Y. H., Nguyen, E. H., Wu, L. F. et al., Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system. Arch. Microbiol. 2002, 177, 441-450.
    • (2002) Arch. Microbiol , vol.177 , pp. 441-450
    • Yen, M.R.1    Tseng, Y.H.2    Nguyen, E.H.3    Wu, L.F.4
  • 26
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: Moving folded proteins across membranes
    • Sargent, F., The twin-arginine transport system: Moving folded proteins across membranes. Biochem. Soc. Trans. 2007, 35, 835-847.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 835-847
    • Sargent, F.1
  • 27
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors?
    • Berks, B. C., A common export pathway for proteins binding complex redox cofactors? Mol. Microbiol. 1996, 22, 393-404.
    • (1996) Mol. Microbiol , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 28
    • 0029079118 scopus 로고
    • A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the delta pH-dependent thyla-koidal protein translocase
    • Chaddock, A. M., Mant, A., Karnauchov, I., Brink, S. et al.,A new type of signal peptide: Central role of a twin-arginine motif in transfer signals for the delta pH-dependent thyla-koidal protein translocase. EMBO J. 1995, 14, 2715-2722.
    • (1995) EMBO J , vol.14 , pp. 2715-2722
    • Chaddock, A.M.1    Mant, A.2    Karnauchov, I.3    Brink, S.4
  • 29
    • 0034697156 scopus 로고    scopus 로고
    • The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli
    • Stanley, N. R., Palmer, T., Berks, B. C., The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli. J. Biol. Chem. 2000, 275, 11591-11596.
    • (2000) J. Biol. Chem , vol.275 , pp. 11591-11596
    • Stanley, N.R.1    Palmer, T.2    Berks, B.C.3
  • 30
    • 0040537042 scopus 로고    scopus 로고
    • Competition between Sec- and TAT-dependent protein translocation in Escherichia coli
    • Cristobal, S., de Gier, J. W., Nielsen, H., von Heijne, G., Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 1999, 18, 2982-2990.
    • (1999) EMBO J , vol.18 , pp. 2982-2990
    • Cristobal, S.1    de Gier, J.W.2    Nielsen, H.3    von Heijne, G.4
  • 31
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alami, M., Luke, I., Deitermann, S., Eisner, G. et al., Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 2003, 12, 937-946.
    • (2003) Mol. Cell , vol.12 , pp. 937-946
    • Alami, M.1    Luke, I.2    Deitermann, S.3    Eisner, G.4
  • 32
    • 9644273939 scopus 로고    scopus 로고
    • The core TatABC complex of the twin-arginine translocase in Escher-ichia coli: TatC drives assembly whereas TatA is essential for stability
    • Mangels, D., Mathers, J., Bolhuis, A., Robinson, C., The core TatABC complex of the twin-arginine translocase in Escher-ichia coli: TatC drives assembly whereas TatA is essential for stability. J. Mol. Biol. 2005, 345, 415-423.
    • (2005) J. Mol. Biol , vol.345 , pp. 415-423
    • Mangels, D.1    Mathers, J.2    Bolhuis, A.3    Robinson, C.4
  • 33
    • 34547683366 scopus 로고    scopus 로고
    • TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli
    • Orriss, G. L., Tarry, M. J., Ize, B., Sargent, F. et al., TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli. FEBS Lett. 2007, 581, 4091-4097.
    • (2007) FEBS Lett , vol.581 , pp. 4091-4097
    • Orriss, G.L.1    Tarry, M.J.2    Ize, B.3    Sargent, F.4
  • 34
    • 0034731394 scopus 로고    scopus 로고
    • TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway
    • Jongbloed, J. D., Martin, U., Antelmann, H., Hecker, M. et al., TatC is a specificity determinant for protein secretion via the twin-arginine translocation pathway. J. Biol. Chem. 2000, 275, 41350-41357.
    • (2000) J. Biol. Chem , vol.275 , pp. 41350-41357
    • Jongbloed, J.D.1    Martin, U.2    Antelmann, H.3    Hecker, M.4
  • 36
    • 0036479116 scopus 로고    scopus 로고
    • The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system
    • Pop, O., Martin, U., Abel, C., Muller, J. P., The twin-arginine signal peptide of PhoD and the TatAd/Cd proteins of Bacillus subtilis form an autonomous Tat translocation system. J. Biol. Chem. 2002, 277, 3268-3273.
    • (2002) J. Biol. Chem , vol.277 , pp. 3268-3273
    • Pop, O.1    Martin, U.2    Abel, C.3    Muller, J.P.4
  • 37
    • 30344440093 scopus 로고    scopus 로고
    • Bifunctional TatA subunits in minimal Tat protein translocases
    • Jongbloed, J. D., van der, P. R., van Dijl, J. M., Bifunctional TatA subunits in minimal Tat protein translocases. Trends Microbiol. 2006, 14, 2-4.
    • (2006) Trends Microbiol , vol.14 , pp. 2-4
    • Jongbloed, J.D.1    van der, P.R.2    van Dijl, J.M.3
  • 38
    • 41449118764 scopus 로고    scopus 로고
    • A minimal Tat system from a gram-positive organism: A bifunctional TatA subunit participates in discrete TatAC and TatA complexes
    • Barnett, J. P., Eijlander, R. T., Kuipers, O. P., Robinson, C., A minimal Tat system from a gram-positive organism: A bifunctional TatA subunit participates in discrete TatAC and TatA complexes. J. Biol. Chem. 2008, 283, 2534-2542.
    • (2008) J. Biol. Chem , vol.283 , pp. 2534-2542
    • Barnett, J.P.1    Eijlander, R.T.2    Kuipers, O.P.3    Robinson, C.4
  • 39
    • 0348150717 scopus 로고    scopus 로고
    • Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis
    • Jongbloed, J. D., Antelmann, H., Hecker, M., Nijland, R. et al., Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis. J. Biol. Chem. 2002, 277, 44068-44078.
    • (2002) J. Biol. Chem , vol.277 , pp. 44068-44078
    • Jongbloed, J.D.1    Antelmann, H.2    Hecker, M.3    Nijland, R.4
  • 40
    • 37349115561 scopus 로고    scopus 로고
    • A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life
    • Widdick, D. A., Eijlander, R. T.,van Dijl, J. M., Kuipers, O. P. et al., A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life. J. Mol. Biol. 2008, 375, 595-603.
    • (2008) J. Mol. Biol , vol.375 , pp. 595-603
    • Widdick, D.A.1    Eijlander, R.T.2    van Dijl, J.M.3    Kuipers, O.P.4
  • 41
    • 34248332082 scopus 로고    scopus 로고
    • Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria
    • Kouwen, T. R., van der Goot, A., Dorenbos, R., Winter, T. et al., Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria. Mol. Microbiol. 2007, 64, 984-999.
    • (2007) Mol. Microbiol , vol.64 , pp. 984-999
    • Kouwen, T.R.1    van der Goot, A.2    Dorenbos, R.3    Winter, T.4
  • 42
    • 0021073779 scopus 로고
    • Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis
    • Norrander, J., Kempe, T., Messing, J., Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene 1983, 26, 101-106.
    • (1983) Gene , vol.26 , pp. 101-106
    • Norrander, J.1    Kempe, T.2    Messing, J.3
  • 43
    • 33750987671 scopus 로고    scopus 로고
    • A dis-ulfide bond-containing alkaline phosphatase triggers a BdbC-dependent secretion stress response in Bacillus sub-tilis
    • Darmon, E., Dorenbos, R., Meens, J., Freudl, R. et al., A dis-ulfide bond-containing alkaline phosphatase triggers a BdbC-dependent secretion stress response in Bacillus sub-tilis. Appl. Environ. Microbiol. 2006, 72, 6876-6885.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 6876-6885
    • Darmon, E.1    Dorenbos, R.2    Meens, J.3    Freudl, R.4
  • 44
    • 0344457370 scopus 로고    scopus 로고
    • et al.,Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli
    • Bron, S., Bolhuis, A., Tjalsma, H., Holsappel, S. et al.,Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli. J. Biotechnol. 1998, 64,3-13.
    • (1998) J. Biotechnol , vol.64 , pp. 3-13
    • Bron, S.1    Bolhuis, A.2    Tjalsma, H.3    Holsappel, S.4
  • 45
    • 0032146073 scopus 로고    scopus 로고
    • Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: Identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases
    • Tjalsma, H., Bolhuis, A., van Roosmalen, M. L., Wiegert, T. et al., Functional analysis of the secretory precursor processing machinery of Bacillus subtilis: Identification of a eubacterial homolog of archaeal and eukaryotic signal peptidases. Genes Dev. 1998, 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
  • 46
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D., Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 1983, 166, 557-580.
    • (1983) J. Mol. Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 48
    • 0015335342 scopus 로고
    • Ultraviolet inactivation and excision-repair in Bacillus subtilis. I. Construction and characterization of a transformable eightfold auxotrophic strain and two ultraviolet-sensitive derivatives
    • Bron, S., Venema, G., Ultraviolet inactivation and excision-repair in Bacillus subtilis. I. Construction and characterization of a transformable eightfold auxotrophic strain and two ultraviolet-sensitive derivatives. Mutat. Res. 1972, 15, 1-10.
    • (1972) Mutat. Res , vol.15 , pp. 1-10
    • Bron, S.1    Venema, G.2
  • 49
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus sub-tilis
    • Kunst, F., Rapoport, G., Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus sub-tilis. J. Bacteriol. 1995, 177, 2403-2407.
    • (1995) J. Bacteriol , vol.177 , pp. 2403-2407
    • Kunst, F.1    Rapoport, G.2
  • 50
    • 0036223585 scopus 로고    scopus 로고
    • Bacillus subtilis functional genomics: Global characterization of the stringent response by proteome and transcriptome analysis
    • Eymann, C., Homuth, G., Scharf, C., Hecker, M., Bacillus subtilis functional genomics: Global characterization of the stringent response by proteome and transcriptome analysis. J. Bacteriol. 2002, 184, 2500-2520.
    • (2002) J. Bacteriol , vol.184 , pp. 2500-2520
    • Eymann, C.1    Homuth, G.2    Scharf, C.3    Hecker, M.4
  • 51
    • 0031046035 scopus 로고    scopus 로고
    • The dnaK operon of Bacillus subtilis is heptacistronic
    • Homuth, G., Masuda, S., Mogk, A., Kobayashi, Y. et al., The dnaK operon of Bacillus subtilis is heptacistronic. J. Bacter-iol. 1997, 179, 1153-1164.
    • (1997) J. Bacter-iol , vol.179 , pp. 1153-1164
    • Homuth, G.1    Masuda, S.2    Mogk, A.3    Kobayashi, Y.4
  • 52
    • 27744441183 scopus 로고    scopus 로고
    • Global expression profiling of Bacillus subtilis cells during industrial-close fed-batch fermentations with different nitrogen sources
    • Jürgen, B., Tobisch, S., Wumpelmann, M., Gordes, D. et al., Global expression profiling of Bacillus subtilis cells during industrial-close fed-batch fermentations with different nitrogen sources. Biotechnol. Bioeng. 2005, 92, 277-298.
    • (2005) Biotechnol. Bioeng , vol.92 , pp. 277-298
    • Jürgen, B.1    Tobisch, S.2    Wumpelmann, M.3    Gordes, D.4
  • 53
    • 0034948896 scopus 로고    scopus 로고
    • A Bayesian framework for the analysis of microarray expression data: Regularized t-test and statis-tical inferences of gene changes
    • Baldi, P., Long, A. D., A Bayesian framework for the analysis of microarray expression data: Regularized t-test and statis-tical inferences of gene changes. Bioinformatics 2001, 17, 509-519.
    • (2001) Bioinformatics , vol.17 , pp. 509-519
    • Baldi, P.1    Long, A.D.2
  • 54
    • 0030665283 scopus 로고    scopus 로고
    • Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor sigmaB in Bacillus subtilis
    • Antelmann, H., Engelmann, S., Schmid, R., Sorokin, A. et al., Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor sigmaB in Bacillus subtilis. J. Bacteriol. 1997, 179, 7251-7256.
    • (1997) J. Bacteriol , vol.179 , pp. 7251-7256
    • Antelmann, H.1    Engelmann, S.2    Schmid, R.3    Sorokin, A.4
  • 55
    • 0025836134 scopus 로고
    • Nonfunctional expression of Escherichia coli signal peptidase I in Bacillus subtilis
    • van Dijl, J. M., de Jong, A., Smith, H., Bron, S. et al., Nonfunctional expression of Escherichia coli signal peptidase I in Bacillus subtilis. J. Gen. Microbiol. 1991, 137, 2073-2083.
    • (1991) J. Gen. Microbiol , vol.137 , pp. 2073-2083
    • van Dijl, J.M.1    de Jong, A.2    Smith, H.3    Bron, S.4
  • 56
    • 0028173018 scopus 로고
    • Isolation and characterization of a Bacillus subtilis secA mutant allele conferring resistance to sodium azide
    • Klein, M., Hofmann, B., Klose, M., Freudl, R., Isolation and characterization of a Bacillus subtilis secA mutant allele conferring resistance to sodium azide. FEMS Microbiol. Lett. 1994, 124, 393-397.
    • (1994) FEMS Microbiol. Lett , vol.124 , pp. 393-397
    • Klein, M.1    Hofmann, B.2    Klose, M.3    Freudl, R.4
  • 57
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews, D. H., Sabina, J., Zuker, M., Turner, D. H., Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol. 1999, 288, 911-940.
    • (1999) J. Mol. Biol , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 58
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M., Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 2003, 31, 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 59
    • 44649133867 scopus 로고    scopus 로고
    • Ecology and genomics of Bacillus subtilis
    • Earl, A. M., Losick, R., Kolter, R., Ecology and genomics of Bacillus subtilis. Trends Microbiol. 2008, 16, 269-275.
    • (2008) Trends Microbiol , vol.16 , pp. 269-275
    • Earl, A.M.1    Losick, R.2    Kolter, R.3
  • 60
    • 0032567332 scopus 로고    scopus 로고
    • The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane
    • Hynds, P. J., Robinson, D., Robinson, C., The sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane. J. Biol. Chem. 1998, 273, 34868-34874.
    • (1998) J. Biol. Chem , vol.273 , pp. 34868-34874
    • Hynds, P.J.1    Robinson, D.2    Robinson, C.3
  • 61
    • 36348950408 scopus 로고    scopus 로고
    • Functional Tat transport of unstructured, small, hydrophilic proteins
    • Richter, S., Lindenstrauss, U., Lucke, C., Bayliss, R. et al., Functional Tat transport of unstructured, small, hydrophilic proteins. J. Biol. Chem. 2007, 282, 33257-33264.
    • (2007) J. Biol. Chem , vol.282 , pp. 33257-33264
    • Richter, S.1    Lindenstrauss, U.2    Lucke, C.3    Bayliss, R.4
  • 62
    • 0032479216 scopus 로고    scopus 로고
    • The influence of protein folding on late stages of the secretion of alpha-amylases from Bacillus subtilis
    • Stephenson, K., Carter, N. M., Harwood, C. R., Petit-Glatron, M. F. et al., The influence of protein folding on late stages of the secretion of alpha-amylases from Bacillus subtilis. FEBS Lett. 1998, 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
  • 63
    • 0034663718 scopus 로고    scopus 로고
    • The influence of secretory-protein charge on late stages of secretion from the Gram-positive bacterium Bacillus subtilis
    • Stephenson, K., Jensen, C. L., Jorgensen, S. T., Lakey, J. H. et al., The influence of secretory-protein charge on late stages of secretion from the Gram-positive bacterium Bacillus subtilis. Biochem. J. 2000, 350, 31-39.
    • (2000) Biochem. J , vol.350 , pp. 31-39
    • Stephenson, K.1    Jensen, C.L.2    Jorgensen, S.T.3    Lakey, J.H.4
  • 64
    • 0029762898 scopus 로고    scopus 로고
    • Export of the peri-plasmic NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis
    • Wiegert, T., Sahm, H., Sprenger, G. A., Export of the peri-plasmic NADP-containing glucose-fructose oxidoreductase of Zymomonas mobilis. Arch. Microbiol. 1996, 166, 32-41.
    • (1996) Arch. Microbiol , vol.166 , pp. 32-41
    • Wiegert, T.1    Sahm, H.2    Sprenger, G.A.3
  • 65
    • 0001336374 scopus 로고    scopus 로고
    • Identification of a role for an azide-sensitive factor in the thylakoid transport of the 17-kilodalton subunit of the photosynthetic oxygen-evolving complex
    • Leheny, E. A., Teter, S. A., Theg, S. M., Identification of a role for an azide-sensitive factor in the thylakoid transport of the 17-kilodalton subunit of the photosynthetic oxygen-evolving complex. Plant Physiol. 1998, 116, 805-814.
    • (1998) Plant Physiol , vol.116 , pp. 805-814
    • Leheny, E.A.1    Teter, S.A.2    Theg, S.M.3
  • 66
    • 0037407866 scopus 로고    scopus 로고
    • Genetic analysis of pathway specificity during posttransla-tional protein translocation across the Escherichia coli plasma membrane
    • Blaudeck, N., Kreutzenbeck, P., Freudl, R., Sprenger, G. A., Genetic analysis of pathway specificity during posttransla-tional protein translocation across the Escherichia coli plasma membrane. J. Bacteriol. 2003, 185, 2811-2819.
    • (2003) J. Bacteriol , vol.185 , pp. 2811-2819
    • Blaudeck, N.1    Kreutzenbeck, P.2    Freudl, R.3    Sprenger, G.A.4
  • 67
    • 0037609475 scopus 로고    scopus 로고
    • Folding quality control in the export of proteins by the bacterial twin-argi-nine translocation pathway
    • DeLisa, M. P., Tullman, D., Georgiou, G., Folding quality control in the export of proteins by the bacterial twin-argi-nine translocation pathway. Proc. Natl. Acad. Sci. USA 2003, 100, 6115-6120.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6115-6120
    • DeLisa, M.P.1    Tullman, D.2    Georgiou, G.3
  • 68
    • 34247262581 scopus 로고    scopus 로고
    • Export pathway selectivity of Escherichia coli twin ar-ginine translocation signal peptides
    • Tullman-Ercek, D., DeLisa, M. P., Kawarasaki, Y., Iranpour, P. et al., Export pathway selectivity of Escherichia coli twin ar-ginine translocation signal peptides. J. Biol. Chem. 2007, 282, 8309-8316.
    • (2007) J. Biol. Chem , vol.282 , pp. 8309-8316
    • Tullman-Ercek, D.1    DeLisa, M.P.2    Kawarasaki, Y.3    Iranpour, P.4
  • 69
    • 0042490703 scopus 로고    scopus 로고
    • Influence of tat mutations on the ribose-binding protein translocation in Escherichia coli
    • Pradel, N., Santini, C. L., Ye, C. Y., Fevat, L. et al., Influence of tat mutations on the ribose-binding protein translocation in Escherichia coli. Biochem. Biophys. Res. Commun. 2003, 306, 786-791.
    • (2003) Biochem. Biophys. Res. Commun , vol.306 , pp. 786-791
    • Pradel, N.1    Santini, C.L.2    Ye, C.Y.3    Fevat, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.