메뉴 건너뛰기




Volumn 76, Issue 3, 2010, Pages 659-669

Contributions of the Pre- And Pro-Regions of a Staphylococcus hyicus Lipase to Secretion of a Heterologous Protein by Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BACILLUS SUBTILIS; CELL SURFACES; CELL WALLS; HETEROLOGOUS PROTEINS; HOST CELLS; PLASMA MEMBRANES; SIGNAL PEPTIDE; SUBTILIS; TRANSCRIPTIONAL ANALYSIS;

EID: 75749088555     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01671-09     Document Type: Article
Times cited : (9)

References (64)
  • 3
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • 3. Aslanidis, C., and P. J. de Jong. 1990. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18:6069-6074. (Pubitemid 20364668)
    • (1990) Nucleic Acids Research , vol.18 , Issue.20 , pp. 6069-6074
    • Aslanidis, C.1    De Jong, P.J.2
  • 5
    • 0033609929 scopus 로고    scopus 로고
    • Functional analysis of paralogous thiol-disulfide oxkloreductases in Bacillus subtilis
    • Bolhuis, A., G. Venema, W. J. Quax, S. Bron, and J. M. van Dijl. 1999. Functional analysis of paralogous thiol-disulfide oxkloreductases 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
  • 6
    • 0033179306 scopus 로고    scopus 로고
    • Improving protein secretion by engineering components of the bacterial, translocation machinery
    • Braun, P., G. Gerritse, J. M. van Dijl, and W. J. Quax. 1999. Improving protein secretion by engineering components of the bacterial, translocation machinery. Curr. Opin. Biotechnol. 10:376-381.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 376-381
    • Braun, P.1    Gerritse, G.2    Van Dijl, J.M.3    Quax, W.J.4
  • 7
    • 33748101074 scopus 로고    scopus 로고
    • Systematic screening of all signal, peptides from. Bacillus subtilis: A powerful strategy in optimizing heterologous protein secretion in Grampositive bacteria
    • Brockmeier, U., M. Caspers, R. Freudl, A. Jockwer, T. Noll, and T. Eggert. 2006. Systematic screening of all signal, peptides from. Bacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in Grampositive bacteria. J. Mol. Biol. 362:393-402.
    • (2006) J. Mol. Biol. , vol.362 , pp. 393-402
    • Brockmeier, U.1    Caspers, M.2    Freudl, R.3    Jockwer, A.4    Noll, T.5    Eggert, T.6
  • 8
    • 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., and G. Venema. 1972. 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. 15:1-10.
    • (1972) Mutat. Res. , vol.15 , pp. 1-10
    • Bron, S.1    Venema, G.2
  • 9
    • 0032809376 scopus 로고    scopus 로고
    • A surface-displayed cholera toxin B peptide improves antibody responses using food-grade staphylococci for mucosal subunit vaccine delivery
    • Cano, F., S. Liljeqvist, T. N. Nguyen, P. Samuelson, J. Y. Bonnefoy, S. Stahl, and A. Robert. 1999. A surface-displayed cholera toxin B peptide improves antibody responses using food-grade staphylococci for mucosal subunit vaccine delivery. FEMS Immunol. Med. Microbiol. 25:289-298.
    • (1999) FEMS Immunol. Med. Microbiol. , vol.25 , pp. 289-298
    • Cano, F.1    Liljeqvist, S.2    Nguyen, T.N.3    Samuelson, P.4    Bonnefoy, J.Y.5    Stahl, S.6    Robert, A.7
  • 10
    • 0034213959 scopus 로고    scopus 로고
    • Partial protection to respiratory syncytial virus (RSV) elicited in mice by intranasal immunization using live staphylococci with surface-displayed RSV-peptides
    • PII S0264410X00000633
    • 10. Cano, F., H. Plotnicky-Gilquin, T. N. Nguyen, S. Liljeqvist, P. Samuelson, J. Bonnefoy, S. Stahl, and A. Robert. 2000. Partial protection, to respiratory syncytial virus (RSV) elicited in mice by intranasal immunization using live staphylococci with surface-displayed RSV-peptides. Vaccine 18:2743-2752. (Pubitemid 30211583)
    • (2000) Vaccine , vol.18 , Issue.24 , pp. 2743-2752
    • Cano, F.1    Plotnicky-Gilquin, H.2    Nguyen, T.N.3    Liljeqvist, S.4    Samuelson, P.5    Bonnefoy, J.-Y.6    Stahl, S.7    Robert, A.8
  • 11
    • 0036307635 scopus 로고    scopus 로고
    • Defining the Bacillus subtilis sigma(W) regulon: A comparative analysis of promoter consensus search, run-off transcription/macroarray analysis (ROMA), and transcriptional, profiling approaches
    • Cao, M., P. A. Kobel, M. M. Morshedi, M. F. Wu, C. Paddon, and J. D. Helmann. 2002. Defining the Bacillus subtilis sigma(W) regulon: a comparative analysis of promoter consensus search, run-off transcription/macroarray analysis (ROMA), and transcriptional, profiling approaches. J. Mol. Biol. 316:443-457.
    • (2002) J. Mol. Biol. , vol.316 , pp. 443-457
    • Cao, M.1    Kobel, P.A.2    Morshedi, M.M.3    Wu, M.F.4    Paddon, C.5    Helmann, J.D.6
  • 12
    • 0036046191 scopus 로고    scopus 로고
    • Antibiotics that inhibit cell wall biosynthesis induce expression of the Bacillus subtilis sigma(W) and sigma(M) regulons
    • Cao, M., T. Wang, R. Ye, and J. D. Helmann. 2002. Antibiotics that inhibit cell wall biosynthesis induce expression of the Bacillus subtilis sigma(W) and sigma(M) regulons. Mol. Microbiol. 45:1267-1276.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1267-1276
    • Cao, M.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 14
    • 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., D. Noone, A. Masson, S. Bron, O. P. Kuipers, K. M. Devine, and J. M. van Dijl. 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
  • 15
    • 0027969299 scopus 로고
    • Evidence for importance of the Staphylococcus hyicus lipase pro-peptide in lipase secretion, stability and activity
    • Demleitner, G., and F. Gotz. 1994. Evidence for importance of the Staphylococcus hyicus lipase pro-peptide in lipase secretion, stability and activity. FEMS Microbiol. Lett. 121:189-197.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 189-197
    • Demleitner, G.1    Gotz, F.2
  • 16
    • 0032904233 scopus 로고    scopus 로고
    • ClpE, a novel type of HSPl00 ATPase, is part of the CtsR heat shock regulon of Bacillus subtilis
    • Derre, I., G. Rapoport, K. Devine, M. Rose, and T. Msadek. 1999. ClpE, a novel type of HSPl00 ATPase, is part of the CtsR heat shock regulon of Bacillus subtilis. Mol. Microbiol. 32:581-593.
    • (1999) Mol. Microbiol. , vol.32 , pp. 581-593
    • Derre, I.1    Rapoport, G.2    Devine, K.3    Rose, M.4    Msadek, T.5
  • 18
    • 0032103863 scopus 로고    scopus 로고
    • Staphylococcal lipases: Molecular characterisation, secretion, and processing
    • Gotz, F., H. M. Verheij, and R.- Rosenstein. 1998. Staphylococcal lipases: molecular characterisation, secretion, and processing. Chem. Phys. Lipids 93:15-25.
    • (1998) Chem. Phys. Lipids , vol.93 , pp. 15-25
    • Gotz, F.1    Verheij, H.M.2    Rosenstein, R.3
  • 19
    • 0029924013 scopus 로고    scopus 로고
    • Surface display of a functional single-chain Fv antibody on staphylococci
    • 19. Gunneriusson, E., P. Samuelson, M. Uhlen, P. A. Nygren, and S. Stahl. 1996. Surface display of a functional single-chain Fv antibody on staphylococci. J. Bacteriol. 178:1341-1346. (Pubitemid 26073391)
    • (1996) Journal of Bacteriology , vol.178 , Issue.5 , pp. 1341-1346
    • Gunneriusson, E.1    Samuelson, P.2    Uhlen, M.3    Nygren, P.-A.4    Stahl, S.5
  • 20
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: An unfolding story
    • Harwood, C. R., and R. Cranenburgh. 2008. Bacillus protein secretion: an unfolding story. Trends Microbiol. 16:73-79.
    • (2008) Trends Microbiol. , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 23
    • 57449089740 scopus 로고    scopus 로고
    • Modulation, of thiol-disulfide oxidoreductases for increased production, of disulfide-bond-containing proteins in Bacillus subtilis
    • Kouwen, T. R., J. Y. Dubois, R. Freudl, W. J. Quax, and J. M. van Dijl. 2008. Modulation, of thiol-disulfide oxidoreductases for increased production, of disulfide-bond-containing proteins in Bacillus subtilis. Appl. Environ. Microbiol. 74:7536-7545.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 7536-7545
    • Kouwen, T.R.1    Dubois, J.Y.2    Freudl, R.3    Quax, W.J.4    Van Dijl, J.M.5
  • 26
    • 0029006115 scopus 로고
    • Salt stress is an environmental signal affecting degradative enzyme synthesis in Bacillus subtilis
    • Kunst, F., and G. Rapoport. 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
  • 27
    • 0043207895 scopus 로고    scopus 로고
    • Nucleotide sequence of the Bacillus subtilis temperate bacteriophage SPβc2
    • 27. Lazarevic, V., A. Dusterhoft, B. Soldo, H. Hilbert, C. Mauel, and D. Karamata. 1999. Nucleotide sequence of the Bacillus subtilis temperate bacteriophage SPbetac2. Microbiology 145:1055-1067. (Pubitemid 29231809)
    • (1999) Microbiology , vol.145 , Issue.5 , pp. 1055-1067
    • Lazarevic, V.1    Dusterhoft, A.2    Soldo, B.3    Hilbert, H.4    Mauel, C.5    Karamata, D.6
  • 28
    • 0035916387 scopus 로고    scopus 로고
    • Directed immobilization of recombinant staphylococci on cotton fibers by functional display of a fungal, cellulose-binding domain
    • Lehtio, J., H. Wernerus, P. Samuelson, T. T. Teeri, and S. Stahl. 2001. Directed immobilization of recombinant staphylococci on cotton fibers by functional display of a fungal, cellulose-binding domain. FEMS Microbiol. Lett. 195:197-204.
    • (2001) FEMS Microbiol. Lett. , vol.195 , pp. 197-204
    • Lehtio, J.1    Wernerus, H.2    Samuelson, P.3    Teeri, T.T.4    Stahl, S.5
  • 29
    • 0033002699 scopus 로고    scopus 로고
    • Surface display of functional fibronectin-binding domains on Staphylococcus carnosus
    • DOI 10.1016/S0014-5793(99)00232-X, PII S001457939900232X
    • 29. Liljeqvist, S., F. Cano, T. N. Nguyen, M. Uhlen, A. Robert, and S. Stahl. 1999. Surface display of functional fibronectin-binding domains on Staphylococcus carnosus. FEBS Lett. 446:299-304. (Pubitemid 29132747)
    • (1999) FEBS Letters , vol.446 , Issue.2-3 , pp. 299-304
    • Liljeqvist, S.1    Cano, F.2    Nguyen, T.N.3    Uhlen, M.4    Robert, A.5    Stahl, S.6
  • 30
    • 0030819834 scopus 로고    scopus 로고
    • Surface display of the cholera toxin B subunit on Staphylococcus xylosus and Staphylococcus carnosus
    • Liljeqvist, S., P. Samuelson, M. Hansson, T. N. Nguyen, H. Binz, and S. Stahl. 1997. Surface display of the cholera toxin B subunit on Staphylococcus xylosus and Staphylococcus carnosus. Appl. Environ. Microbiol. 63:2481-2488.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2481-2488
    • Liljeqvist, S.1    Samuelson, P.2    Hansson, M.3    Nguyen, T.N.4    Binz, H.5    Stahl, S.6
  • 31
    • 34548231707 scopus 로고    scopus 로고
    • Production and secretion stress caused by overexpression of heterologous alpha-amylase leads to inhibition of sporulation and a prolonged motile phase in Bacillus subtilis
    • Lulko, A. T., J. W. Veening, G. Buist, W. K. Smits, E. J. Blom, A. C. Beekman, S. Bron, and O. P. Kuipers. 2007. Production and secretion stress caused by overexpression of heterologous alpha-amylase leads to inhibition of sporulation and a prolonged motile phase in Bacillus subtilis. Appl. Environ. Microbiol. 73:5354-5362.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5354-5362
    • Lulko, A.T.1    Veening, J.W.2    Buist, G.3    Smits, W.K.4    Blom, E.J.5    Beekman, A.C.6    Bron, S.7    Kuipers, O.P.8
  • 32
    • 0027319885 scopus 로고
    • An outer membrane protein (OmpA) of Escherichia coli can be translocated across the cytoplasmic membrane of Bacillus subtilis
    • Meens, J., E. Frings, M. Klose, and R. Freudl. 1993. An outer membrane protein (OmpA) of Escherichia coli can be translocated across the cytoplasmic membrane of Bacillus subtilis. Mol. Microbiol. 9:847-855.
    • (1993) Mol. Microbiol. , vol.9 , pp. 847-855
    • Meens, J.1    Frings, E.2    Klose, M.3    Freudl, R.4
  • 33
    • 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 cell-associated protease(s) in two different gram-positive bacteria
    • Meens, J., M. Herbort, 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 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    Herbort, M.2    Klein, M.3    Freudl, R.4
  • 34
    • 33745434063 scopus 로고    scopus 로고
    • Involvement of Bacillus subtilis ClpE in CtsR degradation and protein quality control
    • DOI 10.1128/JB.00287-06
    • 34. Miethke, M., M. Hecker, and U. Gerth. 2006. Involvement of Bacillus subtilis ClpE in CtsR degradation and protein quality control. J. Bacteriol. 188: 4610-4619. (Pubitemid 43956058)
    • (2006) Journal of Bacteriology , vol.188 , Issue.13 , pp. 4610-4619
    • Miethke, M.1    Hecker, M.2    Gerth, U.3
  • 35
    • 0001864545 scopus 로고
    • Sporulation, germination and outgrowth
    • C. R. Harwood and S. M. Cutting (ed.), Wiley, Chichester, United Kingdom
    • Nicholson, W. L., and P. Setlow. 1990. Sporulation, germination and outgrowth, p. 391-450. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for Bacillus. Wiley, Chichester, United Kingdom.
    • (1990) Molecular Biological Methods for Bacillus , pp. 391-450
    • Nicholson, W.L.1    Setlow, P.2
  • 36
    • 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
    • DOI 10.1128/JB.183.2.654-663.2001
    • 36. Noone, D., A. Howell, R. Collery, and K. M. Devine. 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. 1.83:654-663. (Pubitemid 32048125)
    • (2001) Journal of Bacteriology , vol.183 , Issue.2 , pp. 654-663
    • Noone, D.1    Howell, A.2    Collery, R.3    Devine, K.M.4
  • 37
    • 0014432929 scopus 로고
    • Conversion of Bacillus subtilis DNA to phage DNA following mitomycin C induction
    • Okamoto, K., J. A. Mudd, and J. Marmur. 1968. Conversion of Bacillus subtilis DNA to phage DNA following mitomycin C induction. J. Mol. Biol. 34:429-437.
    • (1968) J. Mol. Biol. , vol.34 , pp. 429-437
    • Okamoto, K.1    Mudd, J.A.2    Marmur, J.3
  • 38
    • 0020438726 scopus 로고
    • Molecular cloning of α-amylase gene from Bacillus amyloliquefaciens and its expression in B. subtilis
    • DOI 10.1016/0378-1119(82)90191-3
    • 38. Palva, I. 1982. Molecular cloning of alpha-amylase gene from Bacillus amyloliquefaciens and its expression in B. subtilis. Gene 19:81-87. (Pubitemid 13235744)
    • (1982) Gene , vol.19 , Issue.1 , pp. 81-87
    • Palva, I.1
  • 39
    • 0026591643 scopus 로고
    • Secretion of the Escherichia coli outer membrane proteins OmpA and OmpF in Bacillus subtilis is blocked at an early intracellular step
    • Puohiniemi, R., M. Simonen, S. Muttilainen, J. P. Himanen, and M. Sarvas. 1992. Secretion of the Escherichia coli outer membrane proteins OmpA and OmpF in Bacillus subtilis is blocked at an early intracellular step. Mol. Microbiol. 6:981-990.
    • (1992) Mol. Microbiol. , vol.6 , pp. 981-990
    • Puohiniemi, R.1    Simonen, M.2    Muttilainen, S.3    Himanen, J.P.4    Sarvas, M.5
  • 41
    • 0036678794 scopus 로고    scopus 로고
    • Assigning numbers to the arrows: Parameterizing a gene regulation network by using accurate expression kinetics
    • Ronen, M., R. Rosenberg, B. I. Shraiman, and U. Alon. 2002. Assigning numbers to the arrows: parameterizing a gene regulation network by using accurate expression kinetics. Proc. Natl. Acad. Sci. U. S. A. 99:10555-10560.
    • (2002) Proc. Natl. Acad. Sci.U. S. A , vol.99 , pp. 10555-10560
    • Ronen, M.1    Rosenberg, R.2    Shraiman, B.I.3    Alon, U.4
  • 43
    • 0032818328 scopus 로고    scopus 로고
    • Engineering of a Staphylococcus camosus surface display system, by substitution or deletion of a Staphylococcus hyicus lipase propeptide
    • Samuelson, P., F. Cano, A. Robert, and S. Stahl. 1999. Engineering of a Staphylococcus camosus surface display system, by substitution or deletion of a Staphylococcus hyicus lipase propeptide. FEMS Microbiol. Lett. 179:131-139.
    • (1999) FEMS Microbiol. Lett. , vol.179 , pp. 131-139
    • Samuelson, P.1    Cano, F.2    Robert, A.3    Stahl, S.4
  • 45
    • 0038348600 scopus 로고    scopus 로고
    • Production of a human calcitonin precursor with Staphylococcus carnosus: Secretory expression and single-step recovery by expanded bed adsorption
    • DOI 10.1016/S0032-9592(02)00332-1
    • 45. Sandgathe, A., D. Tippe, S. Dilsen, J. Meens, M. Halfar, D. Weuster-Botz, R. Freudl, J. Thommes, and M. R. Kula. 2003. Production of a human calcitonin precursor with Staphylococcus carnosus: secretory expression and singlestep recovery by expanded bed adsorption. Process Biochem. 38:1351-1363. (Pubitemid 36708619)
    • (2003) Process Biochemistry , vol.38 , Issue.9 , pp. 1351-1363
    • Sandgathe, A.1    Tippe, D.2    Dilsen, S.3    Meens, J.4    Halfar, M.5    Weuster-Botz, D.6    Freudl, R.7    Thommes, J.8    Kula, M.-R.9
  • 46
    • 8844264456 scopus 로고    scopus 로고
    • Post-translocational folding of secretory proteins in Gram-positive bacteria. Biochim
    • Sarvas, M., C. R. Harwood, S. Bron, and J. M. van Dijl. 2004. Post-translocational folding of secretory proteins in Gram-positive bacteria. Biochim. Biophys. Acta 1694:311-327.
    • (2004) Biophys. Acta , vol.1694 , pp. 311-327
    • Sarvas, M.1    Harwood, C.R.2    Bron, S.3    Van Dijl, J.M.4
  • 47
    • 0023274371 scopus 로고
    • Secretion of human serum albumin from. Bacillus subtilis
    • Saunders, C. W., B. J. Schmidt, R. L. Mallonee, and M. S. Guyer. 1987. Secretion of human serum albumin from. Bacillus subtilis. J. Bacteriol. 169: 2917-2925.
    • (1987) J. Bacteriol. , vol.169 , pp. 2917-2925
    • Saunders, C.W.1    Schmidt, B.J.2    Mallonee, R.L.3    Guyer, M.S.4
  • 48
    • 0031940127 scopus 로고    scopus 로고
    • Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis
    • 48. Scharf, C., S. Riethdorf, H. Ernst, S. Engelmann, U. Volker, and M. Hecker. 1998. Thioredoxin. is an essential protein induced by multiple stresses in Bacillus subtilis. J. Bacteriol. 180:1869-1877. (Pubitemid 28173069)
    • (1998) Journal of Bacteriology , vol.180 , Issue.7 , pp. 1869-1877
    • Scharf, C.1    Riethdorf, S.2    Ernst, H.3    Engelmann, S.4    Volker, U.5    Hecker, M.6
  • 49
    • 0034490227 scopus 로고    scopus 로고
    • Intramolecular chaperones: Polypeptide extensions that modulate protein folding
    • Shinde, U., and M. Inouye. 2000. Intramolecular chaperones: polypeptide extensions that modulate protein folding. Semin. Cell Dev. Biol. 11:35-44.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 35-44
    • Shinde, U.1    Inouye, M.2
  • 50
    • 0035038835 scopus 로고    scopus 로고
    • Secretion of human growth hormone by the food-grade bacterium Staphylococcus carnosus requires a propeptide irrespective of the signal peptide used
    • Sturmfels, A., F. Gotz, and A. Peschel. 2001. Secretion of human growth hormone by the food-grade bacterium Staphylococcus carnosus requires a propeptide irrespective of the signal peptide used. Arch. Microbiol. 175:295-300.
    • (2001) Arch. Microbiol. , vol.175 , pp. 295-300
    • Sturmfels, A.1    Gotz, F.2    Peschel, A.3
  • 51
    • 0035900335 scopus 로고    scopus 로고
    • Functional analysis of the propeptides of subtilisin e and aqualysin i as intramolecular chaperones
    • DOI 10.1016/S0014-5793(01)03053-8, PII S0014579301030538
    • 51. Takagi, H., M. Koga, S. Katsurada, Y. Yabuta, U. Shinde, M. Inouye, and S. Nakamori. 2001. Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones. FEBS Lett. 508:210-214. (Pubitemid 33079247)
    • (2001) FEBS Letters , vol.508 , Issue.2 , pp. 210-214
    • Takagi, H.1    Koga, M.2    Katsurada, S.3    Yabuta, Y.4    Shinde, U.5    Inouye, M.6    Nakamori, S.7
  • 53
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genomebased survey of the secretóme. Microbiol
    • Tjalsma, H., A. Bolhuis, J. D. Jongbloed, S. Bron, and J. M. van Dijl. 2000. Signal peptide-dependent protein transport in Bacillus subtilis: a genomebased survey of the secretóme. Microbiol. Mol. Biol. Rev. 64:515-547.
    • (2000) 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
  • 54
    • 0038460233 scopus 로고    scopus 로고
    • Complementary impact of paralogous Oxal-like proteins of Bacillus subtilis on post-translocational stages in protein secretion
    • Tjalsma, H., S. Bron, and J. M. van Dijl. 2003. Complementary impact of paralogous Oxal-like proteins of Bacillus subtilis on post-translocational stages in protein secretion. J. Biol. Chem. 278:15622-15632.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15622-15632
    • Tjalsma, H.1    Bron, S.2    Van Dijl, J.M.3
  • 56
    • 0034891203 scopus 로고    scopus 로고
    • Translocation of proteins across the cell envelope of Gram-positive bacteria
    • van Wely, K. H., J. Swaving, R. Freudl, and A. J. Driessen. 2001. Translocation of proteins across the cell envelope of Gram-positive bacteria. FEMS Microbiol. Rev. 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
  • 57
  • 58
    • 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
  • 60
    • 0025304236 scopus 로고
    • Characterization of PBSX, a defective prophage of Bacillus subtilis
    • 60. Wood, H. E., M. T. Dawson, K. M. Devine, and D. J. McConnell. 1990. Characterization of PBSX, a defective prophage of Bacillus subtilis. J. Bacteriol. 172:2667-2674. (Pubitemid 20141424)
    • (1990) Journal of Bacteriology , vol.172 , Issue.5 , pp. 2667-2674
    • Wood, H.E.1    Dawson, M.T.2    Devine, K.M.3    McConnell, D.J.4
  • 61
    • 0035976917 scopus 로고    scopus 로고
    • Folding pathway mediated by an intramolecular chaperone: Propeptide release modulates activation precision of pro-subtilisin
    • Yabuta, Y., H. Takagi, M. Inouye, and U. Shinde. 2001. Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin. J. Biol. Chem. 276:44427-44434.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44427-44434
    • Yabuta, Y.1    Takagi, H.2    Inouye, M.3    Shinde, U.4
  • 62
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mpl8 and pUC19 vectors
    • Yunisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yunisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 63
    • 0017349566 scopus 로고
    • Bacillus subtilis bacteriophage SPbeta: Localization of the prophage attachment site, and specialized transduction
    • Zahler, S. A., R. Z. Korman, R. Rosenthal, and H. E. Hemphill. 1977. Bacillus subtilis bacteriophage SPbeta: localization of the prophage attachment site, and specialized transduction. J. Bacteriol. 129:556-558.
    • (1977) J. Bacteriol. , vol.129 , pp. 556-558
    • Zahler, S.A.1    Korman, R.Z.2    Rosenthal, R.3    Hemphill, H.E.4
  • 64
    • 85153636936 scopus 로고    scopus 로고
    • The genus Bacillus
    • E. Goldman and L. Green (ed.), CRC Press, Boca Raton, FL.
    • Zeigler, D. R., and J. B. Perkins. 2008. The genus Bacillus, p. 309-338. In E. Goldman and L. Green (ed.), Practical handbook of microbiology. CRC Press, Boca Raton, FL
    • (2008) Practical Handbook of Microbiology , pp. 309-338
    • Zeigler, D.R.1    Perkins, J.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.