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Volumn 192, Issue 19, 2010, Pages 5212-5219

Toxicity of the colicin M catalytic domain exported to the periplasm is FkpA independent

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; COLICIN; COLICIN M; FERRIC HYDROXAMATE UPTAKE PROTEIN COMPONENT A; OUTER MEMBRANE PROTEIN A; PERIPLASMIC PROTEIN; PROTEIN FKPA; PROTEIN TONB; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; FKPA PROTEIN, E COLI; MEMBRANE PROTEIN; OMPA OUTER MEMBRANE PROTEINS; OUTER MEMBRANE PROTEIN; PEPTIDYLPROLYL ISOMERASE; SIGNAL PEPTIDE;

EID: 77957346780     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00431-10     Document Type: Article
Times cited : (15)

References (29)
  • 1
    • 0042026692 scopus 로고    scopus 로고
    • Native state proline isomerization: An intrinsic molecular switch
    • Andreotti, A. H. 2003. Native state proline isomerization: an intrinsic molecular switch. Biochemistry 42:9516-9524.
    • (2003) Biochemistry , vol.42 , pp. 9516-9524
    • Andreotti, A.H.1
  • 2
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arié, J.-P., N. Sassoon, and J.-M. Betton. 2001. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 39:199-210.
    • (2001) Mol. Microbiol. , vol.39 , pp. 199-210
    • Arié, J.-P.1    Sassoon, N.2    Betton, J.-M.3
  • 3
    • 66149088098 scopus 로고    scopus 로고
    • Human- and plant-pathogenic Pseudomonas species produce bacteriocins exhibiting colicin M-like hydrolase activity towards peptidoglycan precursors
    • Barreteau, H., A. Bouhss, M. Fourgeaud, J. L. Mainardi, T. Touzé, F. Gérard, D. Blanot, M. Arthur, and D. Mengin-Lecreulx. 2009. Human- and plant-pathogenic Pseudomonas species produce bacteriocins exhibiting colicin M-like hydrolase activity towards peptidoglycan precursors. J. Bacteriol. 191:3657-3664.
    • (2009) J. Bacteriol. , vol.191 , pp. 3657-3664
    • Barreteau, H.1    Bouhss, A.2    Fourgeaud, M.3    Mainardi, J.L.4    Touzé, T.5    Gérard, F.6    Blanot, D.7    Arthur, M.8    Mengin-Lecreulx, D.9
  • 6
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: Modular design and evolution
    • Braun, V., S. I. Patzer, and K. Hantke. 2002. Ton-dependent colicins and microcins: modular design and evolution. Biochimie 84:365-380.
    • (2002) Biochimie , vol.84 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 8
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 9
    • 0033524959 scopus 로고    scopus 로고
    • Integration of the colicin A pore-forming domain into the cytoplasmic membrane of Escherichia coli
    • Duché, D., Y. Corda, V. Géli, and D. Baty. 1999. Integration of the colicin A pore-forming domain into the cytoplasmic membrane of Escherichia coli. J. Mol. Biol. 285:1965-1975.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1965-1975
    • Duché, D.1    Corda, Y.2    Géli, V.3    Baty, D.4
  • 10
    • 0036589204 scopus 로고    scopus 로고
    • The pore-forming domain of colicin A fused to a signal peptide: A tool for studying pore-formation and inhibition
    • Duché, D. 2002. The pore-forming domain of colicin A fused to a signal peptide: a tool for studying pore-formation and inhibition. Biochimie 84: 455-464.
    • (2002) Biochimie , vol.84 , pp. 455-464
    • Duché, D.1
  • 11
    • 33747354636 scopus 로고    scopus 로고
    • Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors
    • El Ghachi, M., A. Bouhss, H. Barreteau, T. Touze, G. Auger, D. Blanot, and D. Mengin-Lecreulx. 2006. Colicin M exerts its bacteriolytic effect via enzymatic degradation of undecaprenyl phosphate-linked peptidoglycan precursors. J. Biol. Chem. 281:22761-22772.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22761-22772
    • El Ghachi, M.1    Bouhss, A.2    Barreteau, H.3    Touze, T.4    Auger, G.5    Blanot, D.6    Mengin-Lecreulx, D.7
  • 12
    • 0030007664 scopus 로고    scopus 로고
    • Colicin M is inactivated during import by its immunity protein
    • Gross, P., and V. Braun. 1996. Colicin M is inactivated during import by its immunity protein. Mol. Gen. Genet. 251:388-396.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 388-396
    • Gross, P.1    Braun, V.2
  • 13
    • 0025280089 scopus 로고
    • Colicin M is only bactericidal when provided from outside the cell
    • Harkness, R. E., and V. Braun. 1990. Colicin M is only bactericidal when provided from outside the cell. Mol. Gen. Genet. 222:37-40.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 37-40
    • Harkness, R.E.1    Braun, V.2
  • 14
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • Hullmann, J., S. I. Patzer, C. Römer, K. Hantke, and V. Braun. 2008. Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol. Microbiol. 69:926-937.
    • (2008) Mol. Microbiol. , vol.69 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Römer, C.3    Hantke, K.4    Braun, V.5
  • 15
    • 75149196290 scopus 로고    scopus 로고
    • The colicin Ia receptor, Cir, is also the translocator for colicin Ia
    • Jakes, K. S., and A. Finkelstein. 2010. The colicin Ia receptor, Cir, is also the translocator for colicin Ia. Mol. Microbiol. 75:567-578.
    • (2010) Mol. Microbiol. , vol.75 , pp. 567-578
    • Jakes, K.S.1    Finkelstein, A.2
  • 16
    • 73949113446 scopus 로고    scopus 로고
    • Chaperone domains convert prolyl isomerases into generic catalysts of protein folding
    • Jakob, R. P., G. Zoldàk, T. Aumüller, and F. X. Schmid. 2009. Chaperone domains convert prolyl isomerases into generic catalysts of protein folding. Proc. Natl. Acad. Sci. U. S. A. 106:20282-20287.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 20282-20287
    • Jakob, R.P.1    Zoldàk, G.2    Aumüller, T.3    Schmid, F.X.4
  • 17
    • 0036589253 scopus 로고    scopus 로고
    • Killing of E. coli cells by E group nuclease colicins
    • James, R., C. N. Penfold, G. R. Moore, and C. Kleanthous. 2002. Killing of E. coli cells by E group nuclease colicins. Biochimie 84:381-389.
    • (2002) Biochimie , vol.84 , pp. 381-389
    • James, R.1    Penfold, C.N.2    Moore, G.R.3    Kleanthous, C.4
  • 18
    • 0034767924 scopus 로고    scopus 로고
    • Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm
    • Journet, L., E. Bouveret, A. Rigal, R. Lloubes, C. Lazdunski, and H. Bénédetti. 2001. Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm. Mol. Microbiol. 42:331-344.
    • (2001) Mol. Microbiol. , vol.42 , pp. 331-344
    • Journet, L.1    Bouveret, E.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Bénédetti, H.6
  • 21
    • 0032991467 scopus 로고    scopus 로고
    • Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB
    • Larsen, R. A., M. G. Thomas, and K. Postle. 1999. Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB. Mol. Microbiol. 31:1809-1824.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1809-1824
    • Larsen, R.A.1    Thomas, M.G.2    Postle, K.3
  • 22
    • 0025087137 scopus 로고
    • Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery
    • Oliver, D. B., R. J. Cabelli, K. M. Dolan, and G. P. Jarosik. 1990. Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery. Proc. Natl. Acad. Sci. U. S. A. 87:8227-8231.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 8227-8231
    • Oliver, D.B.1    Cabelli, R.J.2    Dolan, K.M.3    Jarosik, G.P.4
  • 24
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • Saul, F. A., J. P. Arié, B. Vulliez-le Normand, R. Kahn, J.-M. Betton, and G. A. Bentley. 2004. Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335:595-608.
    • (2004) J. Mol. Biol. , vol.335 , pp. 595-608
    • Saul, F.A.1    Arié, J.P.2    Vulliez-le Normand, B.3    Kahn, R.4    Betton, J.-M.5    Bentley, G.A.6
  • 25
    • 0026344184 scopus 로고
    • Evidence for a TonB-dependent energy transduction complex in Escherichia coli
    • Skare, J. T., and K. Postle. 1991. Evidence for a TonB-dependent energy transduction complex in Escherichia coli. Mol. Microbiol. 12:2883-2890.
    • (1991) Mol. Microbiol. , vol.12 , pp. 2883-2890
    • Skare, J.T.1    Postle, K.2
  • 26
    • 77957830356 scopus 로고    scopus 로고
    • E. coli genome manipulation by P1 transduction, unit 1.17
    • John Wiley & Sons, Inc., New York, NY
    • Thomason, L. C., N. Costantino, and D. L. Court. 2007. E. coli genome manipulation by P1 transduction, unit 1.17. In Current protocols in molecular biology. John Wiley & Sons, Inc., New York, NY.
    • (2007) Current Protocols in Molecular Biology
    • Thomason, L.C.1    Costantino, N.2    Court, D.L.3
  • 27
    • 33645021327 scopus 로고    scopus 로고
    • RF cloning: A restriction-free method for inserting target genes into plasmids
    • Van den Ent, F., and J. Löwe. 2006. RF cloning: a restriction-free method for inserting target genes into plasmids. J. Biochem. Biophys. Methods 67:67-74.
    • (2006) J. Biochem. Biophys. Methods , vol.67 , pp. 67-74
    • Van Den Ent, F.1    Löwe, J.2
  • 28
    • 0025809486 scopus 로고
    • New pUC-derived cloning vectors with different selectable markers and DNA replication origins
    • Vieira, J., and J. Messing. 1991. New pUC-derived cloning vectors with different selectable markers and DNA replication origins. Gene 100:189-194.
    • (1991) Gene , vol.100 , pp. 189-194
    • Vieira, J.1    Messing, J.2
  • 29
    • 54449087613 scopus 로고    scopus 로고
    • Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli
    • Zeth, K., C. Römer, S. I. Patzer, and V. Braun. 2008. Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli. J. Biol. Chem. 283:25324-25331.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25324-25331
    • Zeth, K.1    Römer, C.2    Patzer, S.I.3    Braun, V.4


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