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Volumn 27, Issue 3, 1998, Pages 661-667

The requirement for DsbA in pullulanase secretion is independent of disulphide bond formation in the enzyme

Author keywords

[No Author keywords available]

Indexed keywords

PULLULANASE;

EID: 0031963667     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00722.x     Document Type: Article
Times cited : (28)

References (27)
  • 1
    • 0028282814 scopus 로고
    • Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi
    • Bortoli-German, I., Brun, E., Py, B., Chippaux, M., and Barras, F. (1994) Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi. Mol Microbiol 11: 545-553.
    • (1994) Mol Microbiol , vol.11 , pp. 545-553
    • Bortoli-German, I.1    Brun, E.2    Py, B.3    Chippaux, M.4    Barras, F.5
  • 2
    • 0030029288 scopus 로고    scopus 로고
    • Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa
    • Braun, P., Tommassen, J., and Filloux, A. (1996) Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa. Mol Microbiol 19: 297-306.
    • (1996) Mol Microbiol , vol.19 , pp. 297-306
    • Braun, P.1    Tommassen, J.2    Filloux, A.3
  • 3
    • 0030922620 scopus 로고    scopus 로고
    • The disulfide bond in the Aeromonas hydrophila lipase/acyltransferase stabilizes the structure but is not required for secretion or activity
    • Brumlik, M.J., van der Goot, F.G., Wong, K.R., and Buckley, T.J. (1997) The disulfide bond in the Aeromonas hydrophila lipase/acyltransferase stabilizes the structure but is not required for secretion or activity. J Bacteriol 179: 3116-3121.
    • (1997) J Bacteriol , vol.179 , pp. 3116-3121
    • Brumlik, M.J.1    Van Der Goot, F.G.2    Wong, K.R.3    Buckley, T.J.4
  • 4
    • 0028951711 scopus 로고
    • Yersinia spp. HMWP2, a cytosolic protein with a cryptic internal signal sequence which can promote alkaline phosphatase export
    • Guilvout, I., Carniel, E., and Pugsley, A.P. (1995) Yersinia spp. HMWP2, a cytosolic protein with a cryptic internal signal sequence which can promote alkaline phosphatase export. J Bacteriol 177: 1780-1787.
    • (1995) J Bacteriol , vol.177 , pp. 1780-1787
    • Guilvout, I.1    Carniel, E.2    Pugsley, A.P.3
  • 5
    • 0028970780 scopus 로고
    • Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation
    • Hardie, K.R., Schulze, A., Parker, M.W., and Buckley, J.T. (1995) Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation. Mol Microbiol 17: 1035-1044.
    • (1995) Mol Microbiol , vol.17 , pp. 1035-1044
    • Hardie, K.R.1    Schulze, A.2    Parker, M.W.3    Buckley, J.T.4
  • 6
    • 0023449557 scopus 로고
    • Conformation of protein secreted across bacterial outer membanes: A study of enterotoxin translocation from Vibrio choleras
    • Hirst, T.R., and Holmgren, J. (1987) Conformation of protein secreted across bacterial outer membanes: a study of enterotoxin translocation from Vibrio choleras. Proc Natl Acad Sci USA 84: 7418-7422.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7418-7422
    • Hirst, T.R.1    Holmgren, J.2
  • 7
    • 0028104784 scopus 로고
    • PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA
    • Jacob-Dubuisson, F., Pinkner, J., Xu, Z., Striker, R., Padmanhaban, A., and Hultgren, S. (1994) PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA. Proc Natl Acad Sci USA 91: 11552-11556.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11552-11556
    • Jacob-Dubuisson, F.1    Pinkner, J.2    Xu, Z.3    Striker, R.4    Padmanhaban, A.5    Hultgren, S.6
  • 8
    • 0025073184 scopus 로고
    • Molecular characterization of pulA and its product, pullulanase, a secreted enzyme of Klebsiella pneumoniae UNF5023
    • Kornacker, M.G., and Pugsley, A.P. (1989) Molecular characterization of pulA and its product, pullulanase, a secreted enzyme of Klebsiella pneumoniae UNF5023. Mol Microbiol 4: 73-85.
    • (1989) Mol Microbiol , vol.4 , pp. 73-85
    • Kornacker, M.G.1    Pugsley, A.P.2
  • 9
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol 154: 367-382.
    • (1987) Methods Enzymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 10
    • 0030741915 scopus 로고    scopus 로고
    • Interactions of the components of the general secretion pathway: Role of Pseudomonas aeruginosa type IV pilin subunits in complex formation and extracellular protein secretion
    • Lu, H.-M., Motley, S.T., and Lory, S. (1997) Interactions of the components of the general secretion pathway: role of Pseudomonas aeruginosa type IV pilin subunits in complex formation and extracellular protein secretion. Mol Microbiol 25: 247-259.
    • (1997) Mol Microbiol , vol.25 , pp. 247-259
    • Lu, H.-M.1    Motley, S.T.2    Lory, S.3
  • 11
    • 0029612321 scopus 로고
    • The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa
    • McIver, K.S., Kessler, E., Olson, J.C., and Ohman, D.E. (1995) The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. Mol Microbiol 18: 877-889.
    • (1995) Mol Microbiol , vol.18 , pp. 877-889
    • McIver, K.S.1    Kessler, E.2    Olson, J.C.3    Ohman, D.E.4
  • 12
    • 0022365856 scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • Michaelis, S., Chapon, C., d'Enfert, C., Pugsley, A.P., and Schwartz, M. (1985) Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae. J Bacteriol 164: 633-638.
    • (1985) J Bacteriol , vol.164 , pp. 633-638
    • Michaelis, S.1    Chapon, C.2    D'Enfert, C.3    Pugsley, A.P.4    Schwartz, M.5
  • 13
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 14
    • 0027404411 scopus 로고
    • Long-lived periplasmic intermediate in the general secretory pathway in Escherichia coli
    • Poquet, I., Faucher, D., and Pugsley, A.P. (1993) Long-lived periplasmic intermediate in the general secretory pathway in Escherichia coli. EMBO J 12: 271-278.
    • (1993) EMBO J , vol.12 , pp. 271-278
    • Poquet, I.1    Faucher, D.2    Pugsley, A.P.3
  • 15
    • 0030920684 scopus 로고    scopus 로고
    • The conserved tetracysteine motif in the general secretory pathway component PuIE is required for efficient pullulanase secretion
    • Possot, O., and Pugsley, A. (1997) The conserved tetracysteine motif in the general secretory pathway component PuIE is required for efficient pullulanase secretion. Gene 192: 45-50.
    • (1997) Gene , vol.192 , pp. 45-50
    • Possot, O.1    Pugsley, A.2
  • 16
    • 0031005016 scopus 로고    scopus 로고
    • Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway
    • Possot, O., Letellier, L., and Pugsley, A.P. (1997) Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway. Mol Microbiol 24: 457-464.
    • (1997) Mol Microbiol , vol.24 , pp. 457-464
    • Possot, O.1    Letellier, L.2    Pugsley, A.P.3
  • 17
    • 0027085709 scopus 로고
    • Translocation of a folded protein across the outer membrane via the general secretory pathway in Escherichia coli
    • Pugsley, A.P. (1992) Translocation of a folded protein across the outer membrane via the general secretory pathway in Escherichia coli. Proc Natl Acad Sci USA 89: 12058-12062.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 12058-12062
    • Pugsley, A.P.1
  • 18
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley, A.P. (1993a) 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
  • 19
    • 0027337742 scopus 로고
    • Processing and methylation of PulG, a pilin-like component of the general secretory pathway of Klebsiella oxytoca
    • Pugsley, A.P. (1993b) Processing and methylation of PulG, a pilin-like component of the general secretory pathway of Klebsiella oxytoca. Mol Microbol 9: 295-308.
    • (1993) Mol Microbol , vol.9 , pp. 295-308
    • Pugsley, A.P.1
  • 20
    • 0022633064 scopus 로고
    • Extracellular pullulanase of Klebsiella pneumoniae is a lipoprotein
    • Pugsley, A.P., Chapon, C., and Schwartz, M. (1986) Extracellular pullulanase of Klebsiella pneumoniae is a lipoprotein. J Bacteriol 166: 1083-1088.
    • (1986) J Bacteriol , vol.166 , pp. 1083-1088
    • Pugsley, A.P.1    Chapon, C.2    Schwartz, M.3
  • 21
    • 0025805809 scopus 로고
    • Two distinct steps in pullulanase secretion by Escherichia coli K12
    • Pugsley, A.P., Poquet, I., and Kornacker, M.G. (1991a) Two distinct steps in pullulanase secretion by Escherichia coli K12. Mol Microbiol 5: 865-873.
    • (1991) Mol Microbiol , vol.5 , pp. 865-873
    • Pugsley, A.P.1    Poquet, I.2    Kornacker, M.G.3
  • 22
    • 0025977330 scopus 로고
    • The general secretion pathway is directly required for extracellular pullulanase secretion in Escherichia coli
    • Pugsley, A.P., Kornacker, M.G., and Poquet, I. (1991b) The general secretion pathway is directly required for extracellular pullulanase secretion in Escherichia coli. Mol Microbiol 5: 343-352.
    • (1991) Mol Microbiol , vol.5 , pp. 343-352
    • Pugsley, A.P.1    Kornacker, M.G.2    Poquet, I.3
  • 23
    • 0029816618 scopus 로고    scopus 로고
    • Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting β-lactamase secretion by the general secretory pathway
    • Sauvonnet, N., and Pugsley, A.P. (1996) Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting β-lactamase secretion by the general secretory pathway. Mol Microbiol 22: 1-7.
    • (1996) Mol Microbiol , vol.22 , pp. 1-7
    • Sauvonnet, N.1    Pugsley, A.P.2
  • 24
    • 0029128930 scopus 로고
    • Extracellular secretion of pullulanase is unaffected by minor sequence changes but is usually prevented by adding reporter proteins to its N- or C-terminal end
    • Sauvonnet, N., Poquet, I., and Pugsley, A.P. (1995) Extracellular secretion of pullulanase is unaffected by minor sequence changes but is usually prevented by adding reporter proteins to its N- or C-terminal end. J Bacteriol 177: 5238-5246.
    • (1995) J Bacteriol , vol.177 , pp. 5238-5246
    • Sauvonnet, N.1    Poquet, I.2    Pugsley, A.P.3
  • 25
    • 0029048819 scopus 로고
    • Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi
    • Shevchik, V.E., Bortoli-German, I., Robert-Baudouy, J., Robinet, S., Barras, F., and Condemine, G. (1995) Differential effect of dsbA and dsbC mutations on extracellular enzyme secretion in Erwinia chrysanthemi. Mol Microbiol 16: 745-753.
    • (1995) Mol Microbiol , vol.16 , pp. 745-753
    • Shevchik, V.E.1    Bortoli-German, I.2    Robert-Baudouy, J.3    Robinet, S.4    Barras, F.5    Condemine, G.6
  • 26
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • Shevchik, V.E., Robert-Badouy, J., and Condemine, G. (1997) Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins. EMBO J 16: 3007-3016.
    • (1997) EMBO J , vol.16 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Badouy, J.2    Condemine, G.3
  • 27
    • 0000697987 scopus 로고    scopus 로고
    • Secretion across the bacterial outer membrane
    • Escherichia coli and Salmonella. Neidhardt, F.C., Curtiss, III, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington DC: American Society for Microbiology Press
    • Wandersman, C. (1996) Secretion across the bacterial outer membrane. In Escherichia coli and Salmonella. Cellular and Molecular Biology. Neidhardt, F.C., Curtiss, III, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., et al. (eds). Washington DC: American Society for Microbiology Press, pp. 955-966.
    • (1996) Cellular and Molecular Biology , pp. 955-966
    • Wandersman, C.1


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