메뉴 건너뛰기




Volumn 44, Issue 6, 2000, Pages 1660-1666

vanC cluster of vancomycin-resistant Enterococcus gallinarum BM4174

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDASE; LIGASE; RACEMASE; VANCOMYCIN;

EID: 0034081093     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.44.6.1660-1666.2000     Document Type: Article
Times cited : (67)

References (44)
  • 2
    • 0033032394 scopus 로고    scopus 로고
    • Characterization and modelling of VanT, a novel, membrane-bound, serine racemase from vancomycin-resistant Enterococcus gallinarum BM4174
    • Arias, C. A., M. Martin-Martinez, T. L. Blundell, M. Arthur, P. Courvalin, and P. E. Reynolds. 1999. Characterization and modelling of VanT, a novel, membrane-bound, serine racemase from vancomycin-resistant Enterococcus gallinarum BM4174. Mol. Microbiol. 31:1653-1664.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1653-1664
    • Arias, C.A.1    Martin-Martinez, M.2    Blundell, T.L.3    Arthur, M.4    Courvalin, P.5    Reynolds, P.E.6
  • 3
    • 0026658877 scopus 로고
    • The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147
    • Arthur, M., C. Molinas, and P. Courvalin. 1992. The VanS-VanR two-component regulatory system controls synthesis of depsipeptide peptidoglycan precursors in Enterococcus faecium BM4147. J. Bacteriol. 174:2582-2591.
    • (1992) J. Bacteriol. , vol.174 , pp. 2582-2591
    • Arthur, M.1    Molinas, C.2    Courvalin, P.3
  • 5
    • 0027941244 scopus 로고
    • Contribution of Van Y D,D-carboxypeptidase to glycopeptide resistance in Enterococcus faecalis by hydrolysis of peptidoglycan precursors
    • Arthur, M., F. Depardieu, H. A. Snaith, P. E. Reynolds, and P. Courvalin. 1994. Contribution of Van Y D,D-carboxypeptidase to glycopeptide resistance in Enterococcus faecalis by hydrolysis of peptidoglycan precursors. Antimicrob. Agents Chemother. 38:1899-1903.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1899-1903
    • Arthur, M.1    Depardieu, F.2    Snaith, H.A.3    Reynolds, P.E.4    Courvalin, P.5
  • 6
    • 0025741584 scopus 로고
    • Structural relationship between the vancomycin resistance protein VanH and 2-hydroxycarboxylic acid dehydrogenases
    • Arthur, M., C. Molinas, S. Dutka-Malen, and P. Courvalin. 1991. Structural relationship between the vancomycin resistance protein VanH and 2-hydroxycarboxylic acid dehydrogenases. Gene 103:133-134.
    • (1991) Gene , vol.103 , pp. 133-134
    • Arthur, M.1    Molinas, C.2    Dutka-Malen, S.3    Courvalin, P.4
  • 7
    • 0030796911 scopus 로고    scopus 로고
    • Mutations leading to increased levels of resistance to glycopeptide antibiotics in VanB-type enterococci
    • Baptista, M., F. Depardieu, P. E. Reynolds, P. Courvalin, and M. Arthur. 1997. Mutations leading to increased levels of resistance to glycopeptide antibiotics in VanB-type enterococci. Mol. Microbiol. 25:93-105.
    • (1997) Mol. Microbiol. , vol.25 , pp. 93-105
    • Baptista, M.1    Depardieu, F.2    Reynolds, P.E.3    Courvalin, P.4    Arthur, M.5
  • 8
    • 0032910346 scopus 로고    scopus 로고
    • Single-cell analysis of glycopeptide resistance gene expression in teicoplanin-resistant mutants of a VanB-type Enterococcus faecalis
    • Baptista, M., P. Rodrigues, F. Depardieu, P. Courvalin, and M. Arthur. 1999. Single-cell analysis of glycopeptide resistance gene expression in teicoplanin-resistant mutants of a VanB-type Enterococcus faecalis. Mol. Microbiol. 32:17-28.
    • (1999) Mol. Microbiol. , vol.32 , pp. 17-28
    • Baptista, M.1    Rodrigues, P.2    Depardieu, F.3    Courvalin, P.4    Arthur, M.5
  • 9
    • 0028605482 scopus 로고
    • Association constants for the binding of vancomycin and teicoplanin to N-acetyl-D-alanyl-D-alanine and N-acetyl-D-alanyl-D-serine
    • Billot-Klein, D., L. Gutmann, S. Sable, E. Guitet, and J. van Heijenoort. 1994. Association constants for the binding of vancomycin and teicoplanin to N-acetyl-D-alanyl-D-alanine and N-acetyl-D-alanyl-D-serine. Biochem. J. 304: 1021-1022.
    • (1994) Biochem. J. , vol.304 , pp. 1021-1022
    • Billot-Klein, D.1    Gutmann, L.2    Sable, S.3    Guitet, E.4    Van Heijenoort, J.5
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0026355435 scopus 로고
    • Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: Biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA
    • Bugg, T. D. H., G. D. Wright, S. Dutka-Malen, M. Arthur, P. Courvalin, and C. T. Walsh. 1991. Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. Biochemistry 30:10408-10415.
    • (1991) Biochemistry , vol.30 , pp. 10408-10415
    • Bugg, T.D.H.1    Wright, G.D.2    Dutka-Malen, S.3    Arthur, M.4    Courvalin, P.5    Walsh, C.T.6
  • 12
    • 0000182975 scopus 로고
    • XL1-Blue - A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock, W. O., J. M. Fernandez, and J. M. Short. 1987. XL1-Blue - a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. BioTechniques 5:376.
    • (1987) Biotechniques , vol.5 , pp. 376
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 13
    • 0033011933 scopus 로고    scopus 로고
    • Characterization of the vanD glycopeptide resistance gene cluster from Enterococcus faecium BM4339
    • Casadewall, B., and P. Courvalin. 1999. Characterization of the vanD glycopeptide resistance gene cluster from Enterococcus faecium BM4339. J. Bacteriol. 181:3644-3648.
    • (1999) J. Bacteriol. , vol.181 , pp. 3644-3648
    • Casadewall, B.1    Courvalin, P.2
  • 14
    • 0025149087 scopus 로고
    • High efficiency introduction of plasmid DNA into glycine-treated Enterococcus faecalis by electroporation
    • Cruz-Rodz, A. L., and M. S. Gilmore. 1990. High efficiency introduction of plasmid DNA into glycine-treated Enterococcus faecalis by electroporation. Mol. Gen. Genet. 224:152-154.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 152-154
    • Cruz-Rodz, A.L.1    Gilmore, M.S.2
  • 15
    • 0026522234 scopus 로고
    • Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine: D-alanine ligase-related protein necessary for vancomycin resistance
    • Dutka-Malen, S., C. Molinas, M. Arthur, and P. Courvalin. 1992. Sequence of the vanC gene of Enterococcus gallinarum BM4174 encoding a D-alanine: D-alanine ligase-related protein necessary for vancomycin resistance. Gene 112:53-58.
    • (1992) Gene , vol.112 , pp. 53-58
    • Dutka-Malen, S.1    Molinas, C.2    Arthur, M.3    Courvalin, P.4
  • 16
    • 0029863413 scopus 로고    scopus 로고
    • B two-component regulatory system in Enterococcus faecalis V583
    • B two-component regulatory system in Enterococcus faecalis V583. J. Bacteriol. 178:1302-1309.
    • (1996) J. Bacteriol. , vol.178 , pp. 1302-1309
    • Evers, S.1    Courvalin, P.2
  • 18
    • 0029976603 scopus 로고    scopus 로고
    • Using CLUSTAL for multiple sequence alignments
    • Higgins, D. G., J. D. Thompson, and T. J. Gibson. 1996. Using CLUSTAL for multiple sequence alignments. Methods Enzymol. 266:383-402.
    • (1996) Methods Enzymol. , vol.266 , pp. 383-402
    • Higgins, D.G.1    Thompson, J.D.2    Gibson, T.J.3
  • 20
    • 0028204226 scopus 로고
    • Identification of the DNA-binding site for the phosphorylated VanR protein required for vancomycin resistance in Enterococcus faecium
    • Holman, T. R., Z. Wu, B. L. Wanner, and C. T. Walsh. 1994. Identification of the DNA-binding site for the phosphorylated VanR protein required for vancomycin resistance in Enterococcus faecium. Biochemistry 33:4625-4631.
    • (1994) Biochemistry , vol.33 , pp. 4625-4631
    • Holman, T.R.1    Wu, Z.2    Wanner, B.L.3    Walsh, C.T.4
  • 21
    • 0000207681 scopus 로고
    • TMBase - A database of membrane spanning protein segments
    • Holmann, K., and W. Stoffel. 1993. TMBase - a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 374:166.
    • (1993) Biol. Chem. Hoppe-seyler , vol.374 , pp. 166
    • Holmann, K.1    Stoffel, A.W.2
  • 22
    • 0012413056 scopus 로고
    • Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalis var. zymogenes
    • Jacob, A. E., and S. J. Hobbs. 1974. Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalis var. zymogenes. J. Bacteriol. 174:5982-5984.
    • (1974) J. Bacteriol. , vol.174 , pp. 5982-5984
    • Jacob, A.E.1    Hobbs, S.J.2
  • 23
    • 0020475449 scopus 로고
    • A simple method for displaying hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 24
    • 0026892270 scopus 로고
    • Modified peptidoglycan precursors produced by glycopeptide-resistant enterococci
    • Messer, J., and P. E. Reynolds. 1992. Modified peptidoglycan precursors produced by glycopeptide-resistant enterococci. FEMS Microbiol. Lett. 94: 195-200.
    • (1992) Fems Microbiol. Lett. , vol.94 , pp. 195-200
    • Messer, J.1    Reynolds, P.E.2
  • 26
    • 0028071883 scopus 로고
    • Analysis of genes encoding D-alanine: D-alanine ligase-related enzymes in Enterococcus casseliflavus and Enterococcus flavescens
    • Navarro, F., and P. Courvalin. 1994. Analysis of genes encoding D-alanine: D-alanine ligase-related enzymes in Enterococcus casseliflavus and Enterococcus flavescens. Antimicrob. Agents Chemother. 38:1788-1793.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1788-1793
    • Navarro, F.1    Courvalin, P.2
  • 27
    • 0021073779 scopus 로고
    • Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis
    • Norrander, J., T. Kempe, and J. Messing. 1983. Construction of improved M13 vectors using oligodeoxynucleotide-directed mutagenesis. Gene 26: 101-106.
    • (1983) Gene , vol.26 , pp. 101-106
    • Norrander, J.1    Kempe, T.2    Messing, J.3
  • 28
    • 0023691425 scopus 로고
    • Genetic applications of an inverse polymerase reaction
    • Ochman, H., A. S. Gerber, and D. L. Hart. 1988. Genetic applications of an inverse polymerase reaction. Genetics 120:621-623.
    • (1988) Genetics , vol.120 , pp. 621-623
    • Ochman, H.1    Gerber, A.S.2    Hart, D.L.3
  • 29
    • 0030922878 scopus 로고    scopus 로고
    • Bacterial resistance to vancomycin: Overproduction, purification, and characterization of VanC-2 from Enterococcus casseliflavus as a D-Ala:D-Ser ligase
    • Park, I. S., L. Chung-Hung, and C. T. Walsh. 1997. Bacterial resistance to vancomycin: overproduction, purification, and characterization of VanC-2 from Enterococcus casseliflavus as a D-Ala:D-Ser ligase. Proc. Natl. Acad. Sci. USA 94:101140-10044.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 101140-110044
    • Park, I.S.1    Chung-Hung, L.2    Walsh, C.T.3
  • 30
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J. S., and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 32
    • 0024553747 scopus 로고
    • Rapid extraction of bacterial genomic DNA with guanidinium thiocyanate
    • Pitcher, D. G., N. A. Saunders, and R. J. Owen. 1989. Rapid extraction of bacterial genomic DNA with guanidinium thiocyanate. Lett. Appl. Microbiol. 8:151-156.
    • (1989) Lett. Appl. Microbiol. , vol.8 , pp. 151-156
    • Pitcher, D.G.1    Saunders, N.A.2    Owen, R.J.3
  • 33
    • 0028076784 scopus 로고
    • Glycopeptide resistance mediated by enterococcal transposon Tn 1546 requires VanX for hydrolysis of D-alanyl-n-alanine
    • Reynolds, P. E., F. Depardieu, S. Dutka-Malen, M. Arthur, and P. Courvalin. 1994. Glycopeptide resistance mediated by enterococcal transposon Tn 1546 requires VanX for hydrolysis of D-alanyl-n-alanine. Mol. Microbiol. 13:1065-1070.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1065-1070
    • Reynolds, P.E.1    Depardieu, F.2    Dutka-Malen, S.3    Arthur, M.4    Courvalin, P.5
  • 34
    • 0028235256 scopus 로고
    • Analysis of peptidoglycan precursors in vancomycin-resistant Enterococcus gallinarum BM4174
    • Reynolds, P. E., H. A. Snaith, A. J. Maguire, S. Dutka-Malen, and P. Courvalin. 1994. Analysis of peptidoglycan precursors in vancomycin-resistant Enterococcus gallinarum BM4174. Biochem. J. 301:5-8.
    • (1994) Biochem. J. , vol.301 , pp. 5-8
    • Reynolds, P.E.1    Snaith, H.A.2    Maguire, A.J.3    Dutka-Malen, S.4    Courvalin, P.5
  • 35
    • 0031899463 scopus 로고    scopus 로고
    • Control of peptidoglycan synthesis in vancomycin-resistant enterococci: D,D-peptidases and D,D-carboxypeptidases
    • Reynolds, P. E. 1998. Control of peptidoglycan synthesis in vancomycin-resistant enterococci: D,D-peptidases and D,D-carboxypeptidases. Cell. Mol. Life Sci. 54:325-331.
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 325-331
    • Reynolds, P.E.1
  • 36
    • 0032585993 scopus 로고    scopus 로고
    • C encodes both D,D-dipeplidase (VanX) and D,D-carboxypeptidase (VanY) activities in vancomycin-resistant Enterococcus gallinarum BM4174
    • C encodes both D,D-dipeplidase (VanX) and D,D-carboxypeptidase (VanY) activities in vancomycin-resistant Enterococcus gallinarum BM4174. Mol. Microbiol. 34: 341-349.
    • (1999) Mol. Microbiol. , vol.34 , pp. 341-349
    • Reynolds, P.E.1    Arias, C.A.2    Courvalin, P.3
  • 37
    • 0029034396 scopus 로고
    • Inducible and constitutive expression of vznC-1-encoded resistance to vancomycin in Enterococcus gallinarum
    • Sahm, D. F., L. Free, and S. Handwerker. 1995. Inducible and constitutive expression of vznC-1-encoded resistance to vancomycin in Enterococcus gallinarum. Antimicrob. Agents Chemother. 39:1480-1484.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1480-1484
    • Sahm, D.F.1    Free, L.2    Handwerker, S.3
  • 40
    • 0032578489 scopus 로고    scopus 로고
    • In vivo characterization of type A and B vancomycin-resistant enterococci (VRE) VanRS two-component systems in Escherichia coli: A nonpathogenic model for studying the VRE signal transduction pathways
    • Silva, J. C., A. Haldimann, M. K. Prahalad, C. T. Walsh, and B. L. Wanner. 1998. In vivo characterization of type A and B vancomycin-resistant enterococci (VRE) VanRS two-component systems in Escherichia coli: a nonpathogenic model for studying the VRE signal transduction pathways. Proc. Natl. Acad. Sci. USA 95:11951-11956.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11951-11956
    • Silva, J.C.1    Haldimann, A.2    Prahalad, M.K.3    Walsh, C.T.4    Wanner, B.L.5
  • 41
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 42
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock, J. B., A. J. Ninfa, and A. M. Stock. 1989. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. 53:450-490.
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 43
    • 0028887438 scopus 로고
    • The gtcRS operon coding for two-component system regulatory proteins is located adjacent to the grs operon of Bacillus brevis
    • Turgay, K., and M. A. Marahiel. 1995. The gtcRS operon coding for two-component system regulatory proteins is located adjacent to the grs operon of Bacillus brevis. DNA Seq. 5:283-290.
    • (1995) DNA Seq. , vol.5 , pp. 283-290
    • Turgay, K.1    Marahiel, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.