메뉴 건너뛰기




Volumn 52, Issue 4, 2004, Pages 1107-1121

Characterization of an inducible vancomycin resistance system in Streptomyces coelicolor reveals a novel gene (vanK) required for drug resistance

Author keywords

[No Author keywords available]

Indexed keywords

A47934; ALANINE; AMINO ACID; ANTIBIOTIC AGENT; CHLOROEREMOMYCIN; GLYCOPEPTIDE; KANAMYCIN; PEPTIDOGLYCAN; RISTOCETIN; TEICOPLANIN; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 3142743426     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04032.x     Document Type: Article
Times cited : (114)

References (57)
  • 1
    • 0021154432 scopus 로고
    • The structure and mode of action of glycopeptide antibiotics of the vancomycin group
    • Barna, J.C.J., and Williams, D.H. (1984) The structure and mode of action of glycopeptide antibiotics of the vancomycin group. Annu Rev Microbiol 38: 339-357.
    • (1984) Annu Rev Microbiol , vol.38 , pp. 339-357
    • Barna, J.C.J.1    Williams, D.H.2
  • 2
    • 0028942365 scopus 로고
    • Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics
    • Beauregard, D.A., Williams, D.H., Gwynn, M.N., and Knowles, D.J. (1995) Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics. Antimicrob Agents Chemother 39: 781-785.
    • (1995) Antimicrob Agents Chemother , vol.39 , pp. 781-785
    • Beauregard, D.A.1    Williams, D.H.2    Gwynn, M.N.3    Knowles, D.J.4
  • 5
    • 0021710537 scopus 로고
    • The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences
    • Bibb, M.J., Findlay, P.R., and Johnson, M.W. (1984) The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences. Gene 30: 157-166.
    • (1984) Gene , vol.30 , pp. 157-166
    • Bibb, M.J.1    Findlay, P.R.2    Johnson, M.W.3
  • 6
    • 0028079724 scopus 로고
    • The mRNA for the 23S rRNA methylase encoded by the ermE gene of Saccharopolyspora erythraea is translated in the absence of a conventional ribosome-binding site
    • Bibb, M.J., White, J., Ward, J.M., and Janssen, G.R. (1994) The mRNA for the 23S rRNA methylase encoded by the ermE gene of Saccharopolyspora erythraea is translated in the absence of a conventional ribosome-binding site. Mol Microbiol 14: 533-545.
    • (1994) Mol Microbiol , vol.14 , pp. 533-545
    • Bibb, M.J.1    White, J.2    Ward, J.M.3    Janssen, G.R.4
  • 7
    • 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., Blanot, D., Gutmann, L., and van Heijenoort, J. (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    Blanot, D.2    Gutmann, L.3    Van Heijenoort, J.4
  • 8
    • 0029750226 scopus 로고    scopus 로고
    • Peptidoglycan synthesis and structure in Staphylococcus haemolyticus expressing increasing levels of resistance to glycopeptide antibiotics
    • Billot-Klein, D., Gutmann, L., Bryant, D., Bell, D., van Heijenoort, J., Grewal, J., and Shlaes, D.M. (1996) Peptidoglycan synthesis and structure in Staphylococcus haemolyticus expressing increasing levels of resistance to glycopeptide antibiotics. J Bacteriol 178: 4696-4703.
    • (1996) J Bacteriol , vol.178 , pp. 4696-4703
    • Billot-Klein, D.1    Gutmann, L.2    Bryant, D.3    Bell, D.4    Van Heijenoort, J.5    Grewal, J.6    Shlaes, D.M.7
  • 9
    • 0000960760 scopus 로고    scopus 로고
    • Bacterial peptidoglycan biosynthesis and its inhibition
    • Pinto, M. (ed.). Oxford: Elsevier Science
    • Bugg, T.D.H. (1999) Bacterial peptidoglycan biosynthesis and its inhibition. In Comprehensive Natural Products Chemistry, Vol. 3. Pinto, M. (ed.). Oxford: Elsevier Science, pp. 241-294.
    • (1999) Comprehensive Natural Products Chemistry , vol.3 , pp. 241-294
    • Bugg, T.D.H.1
  • 10
    • 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., Wright, G.D., Dutka-Malen, S., Arthur, M., Courvalin, P., and Walsh, C.T. (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
  • 11
    • 0037417230 scopus 로고    scopus 로고
    • Infection with vancomycin-resistant Staphylococcus aureus containing the vanA resistance gene
    • Chang, S., Sievert, D.M., Hageman, J.C., Boulton, M.L., Tenover, F.C., Downes, F.P., et al. (2003) Infection with vancomycin-resistant Staphylococcus aureus containing the vanA resistance gene. N Engl J Med 348: 1342-1347.
    • (2003) N Engl J Med , vol.348 , pp. 1342-1347
    • Chang, S.1    Sievert, D.M.2    Hageman, J.C.3    Boulton, M.L.4    Tenover, F.C.5    Downes, F.P.6
  • 12
    • 0038274041 scopus 로고    scopus 로고
    • Vancomycin analogues active against vanA-resistant strains inhibit bacterial transglycosylase without binding substrate
    • Chen, L., Walker, D., Sun, B., Hu, Y., Walker, S., and Kahne, D. (2003) Vancomycin analogues active against vanA-resistant strains inhibit bacterial transglycosylase without binding substrate. Proc Natl Acad Sci USA 100: 5658-5663.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5658-5663
    • Chen, L.1    Walker, D.2    Sun, B.3    Hu, Y.4    Walker, S.5    Kahne, D.6
  • 13
    • 0029796373 scopus 로고    scopus 로고
    • New directions in antibacterial research
    • Chu, D.T., Plattner, J.J., and Katz, L. (1996) New directions in antibacterial research. J Med Chem 39: 3853-3874.
    • (1996) J Med Chem , vol.39 , pp. 3853-3874
    • Chu, D.T.1    Plattner, J.J.2    Katz, L.3
  • 14
    • 0033485286 scopus 로고    scopus 로고
    • Binding of glycopeptide antibiotics to a model of a vancomycin-resistant bacterium
    • Cooper, M.A., and Williams, D.H. (1999) Binding of glycopeptide antibiotics to a model of a vancomycin-resistant bacterium. Chem Biol 6: 891-899.
    • (1999) Chem Biol , vol.6 , pp. 891-899
    • Cooper, M.A.1    Williams, D.H.2
  • 15
    • 0034612342 scopus 로고    scopus 로고
    • One step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Si USA 97: 6640-6645.
    • (2000) Proc Natl Acad Si USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 16
    • 0031089715 scopus 로고    scopus 로고
    • Signal transduction via the histidyl-aspartyl phospho-relay
    • Egger, L.A., Park, H., and Inouye, M. (1997) Signal transduction via the histidyl-aspartyl phospho-relay. Genes Cells 2: 167-184.
    • (1997) Genes Cells , vol.2 , pp. 167-184
    • Egger, L.A.1    Park, H.2    Inouye, M.3
  • 17
    • 0030716395 scopus 로고    scopus 로고
    • Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation
    • Ehlert, K., Schröder, W., and Labischinski, H. (1997) Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. J Bacteriol 179: 7573-7576.
    • (1997) J Bacteriol , vol.179 , pp. 7573-7576
    • Ehlert, K.1    Schröder, W.2    Labischinski, H.3
  • 18
    • 0033574743 scopus 로고    scopus 로고
    • Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala
    • Ge, M., Chem, Z., Onishi, H.R., Kohler, J., Silver, L.L., Kerns, R., et al. (1999) Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala. Science 284: 507-511.
    • (1999) Science , vol.284 , pp. 507-511
    • Ge, M.1    Chem, Z.2    Onishi, H.R.3    Kohler, J.4    Silver, L.L.5    Kerns, R.6
  • 19
    • 0037452723 scopus 로고    scopus 로고
    • Gene replacement by PCR targeting in Streptomyces and its use to identify a protein domain involved in the biosynthesis of the sesquiterpene odour geosmin
    • Gust, B., Challis, G.L., Fowler, K., Kieser, T., and Chater, K.F. (2003) Gene replacement by PCR targeting in Streptomyces and its use to identify a protein domain involved in the biosynthesis of the sesquiterpene odour geosmin. Proc Natl Acad Sci USA 100: 1541-1546.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 20
    • 0029796977 scopus 로고    scopus 로고
    • Analysis of two-component signal transduction systems involved in transcriptional regulation
    • Hackenbeck, R., and Stock, J.B. (1996) Analysis of two-component signal transduction systems involved in transcriptional regulation. Methods Enzymol 273: 281-300.
    • (1996) Methods Enzymol , vol.273 , pp. 281-300
    • Hackenbeck, R.1    Stock, J.B.2
  • 21
    • 0034087501 scopus 로고    scopus 로고
    • Vancomycin resistance in enterococci: Reprogramming of the D-Ala-D-Ala ligases in bacterial peptidoglycan biosynthesis
    • Healy, V.L., Lessard, I.A., Roper, D.I., Knox, J.R., and Walsh, C.T. (2000) Vancomycin resistance in enterococci: reprogramming of the D-Ala-D-Ala ligases in bacterial peptidoglycan biosynthesis. Chem Biol 7: R109-R119.
    • (2000) Chem Biol , vol.7
    • Healy, V.L.1    Lessard, I.A.2    Roper, D.I.3    Knox, J.R.4    Walsh, C.T.5
  • 23
    • 0035831448 scopus 로고    scopus 로고
    • FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets
    • Hegde, S.S., and Shrader, T.E. (2001) FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets. J Biol Chem 276: 6998-7003.
    • (2001) J Biol Chem , vol.276 , pp. 6998-7003
    • Hegde, S.S.1    Shrader, T.E.2
  • 24
    • 0027498007 scopus 로고
    • Influence of femB on methicillin resistance and peptidoglycan metabolism in Staphylococcus aureus
    • Henze, U., Sidow, T., Wecke, J., Labischinski, H., and Berger-Bächi, B. (1993) Influence of femB on methicillin resistance and peptidoglycan metabolism in Staphylococcus aureus. J Bacteriol 175: 1612-1620.
    • (1993) J Bacteriol , vol.175 , pp. 1612-1620
    • Henze, U.1    Sidow, T.2    Wecke, J.3    Labischinski, H.4    Berger-Bächi, B.5
  • 25
    • 0036015637 scopus 로고    scopus 로고
    • A signal transduction system in Streptomyces coelicolor that activates the expression of a putative cell wall glycan operon in response to vancomycin and other cell wall-specific antibiotics
    • Hong, H.-J., Paget, M.S.B., and Buttner, M.J. (2002) A signal transduction system in Streptomyces coelicolor that activates the expression of a putative cell wall glycan operon in response to vancomycin and other cell wall-specific antibiotics. Mol Microbiol 44: 1199-1211.
    • (2002) Mol Microbiol , vol.44 , pp. 1199-1211
    • Hong, H.-J.1    Paget, M.S.B.2    Buttner, M.J.3
  • 26
    • 0038561132 scopus 로고    scopus 로고
    • Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis
    • Ikeda, H., Ishikawa, J., Hanamoto, A., Shinose, M., Kikuchi, H., Shiba, T., et al. (2003) Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis. Nature Biotechnol 21: 526-531.
    • (2003) Nature Biotechnol , vol.21 , pp. 526-531
    • Ikeda, H.1    Ishikawa, J.2    Hanamoto, A.3    Shinose, M.4    Kikuchi, H.5    Shiba, T.6
  • 27
    • 0024633469 scopus 로고
    • Unusual transcriptional and translational features of the aminoglycoside phosphotransferase gene (aph) from Streptomyces fradiae
    • Janssen, G.R., Ward, J.M., and Bibb, M.J. (1989) Unusual transcriptional and translational features of the aminoglycoside phosphotransferase gene (aph) from Streptomyces fradiae. Genes Dev 3: 415-429.
    • (1989) Genes Dev , vol.3 , pp. 415-429
    • Janssen, G.R.1    Ward, J.M.2    Bibb, M.J.3
  • 29
    • 0029759502 scopus 로고    scopus 로고
    • Staphylococcal peptidoglycan interpeptide bridge biosynthesis: A novel antistaphylococcal target?
    • Kopp, U., Roos, M., Wecke, J., and Labischinski, H. (1996) Staphylococcal peptidoglycan interpeptide bridge biosynthesis: a novel antistaphylococcal target? Microb Drug Resist 2: 29-41.
    • (1996) Microb Drug Resist , vol.2 , pp. 29-41
    • Kopp, U.1    Roos, M.2    Wecke, J.3    Labischinski, H.4
  • 30
    • 0014957798 scopus 로고
    • LL-diaminopimelic acid containing peptidoglycans in walls of Streptomyces sp. and of Clostridium perfringens (type A)
    • Leyh-Bouille, M., Bonaly, R., Ghuysen, J.-M., Tinelli, R., and Tipper, D. (1970) LL-diaminopimelic acid containing peptidoglycans in walls of Streptomyces sp. and of Clostridium perfringens (type A). Biochemistry 9: 2944-2952.
    • (1970) Biochemistry , vol.9 , pp. 2944-2952
    • Leyh-Bouille, M.1    Bonaly, R.2    Ghuysen, J.-M.3    Tinelli, R.4    Tipper, D.5
  • 31
    • 0030967599 scopus 로고    scopus 로고
    • Structure of the DNA-binding domain of the OmpR family of response regulators
    • Mizuno, T., and Tanaka, I. (1997) Structure of the DNA-binding domain of the OmpR family of response regulators. Mol Microbiol 24: 665-670.
    • (1997) Mol Microbiol , vol.24 , pp. 665-670
    • Mizuno, T.1    Tanaka, I.2
  • 32
    • 0036889040 scopus 로고    scopus 로고
    • Leaderless mRNAs bind 70S ribosomes more strongly than 30S ribosomal subunits in Escherichia coli
    • O'Donnell, S.M., and Janssen, G.R. (2002) Leaderless mRNAs bind 70S ribosomes more strongly than 30S ribosomal subunits in Escherichia coli. J Bacteriol 184: 6930-6933.
    • (2002) J Bacteriol , vol.184 , pp. 6930-6933
    • O'Donnell, S.M.1    Janssen, G.R.2
  • 34
    • 0036682463 scopus 로고    scopus 로고
    • 'Superbug' hurdles key drug barrier
    • Pearson, H. (2002) 'Superbug' hurdles key drug barrier. Nature 418: 469-470.
    • (2002) Nature , vol.418 , pp. 469-470
    • Pearson, H.1
  • 36
    • 0037173032 scopus 로고    scopus 로고
    • Assembling the glycopeptide antibiotic scaffold: The biosynthesis of A47934 from Streptomyces toyocaensis NRRL15009
    • Pootoolal, J., Thomas, M.G., Marshall, C.G., Neu, J.M., Hubbard, B.K., Walsh, C.T., and Wright, G.D. (2002b) Assembling the glycopeptide antibiotic scaffold: the biosynthesis of A47934 from Streptomyces toyocaensis NRRL15009. Proc Natl Acad Sci USA 99: 8962-8967.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8962-8967
    • Pootoolal, J.1    Thomas, M.G.2    Marshall, C.G.3    Neu, J.M.4    Hubbard, B.K.5    Walsh, C.T.6    Wright, G.D.7
  • 37
    • 0028235256 scopus 로고
    • Analysis of peptidoglycan precursors in vancomycin-resistant Enterococcus gallinarum BM4174
    • Reynolds, P.E., Snaith, H.A., Maguire, A.J., Dutka-Malen, S., and Courvalin, P. (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
  • 38
    • 0037416970 scopus 로고    scopus 로고
    • FemABX peptidyl transferases: A link between branched-chain cell wall peptide formation and β-lactam resistance in Gram-positive cocci
    • Rohrer, S., and Berger-Bächi, B. (2003) FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and β-lactam resistance in Gram-positive cocci. Antimicrob Agents Chemother 47: 837-846.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 837-846
    • Rohrer, S.1    Berger-Bächi, B.2
  • 39
    • 0033529856 scopus 로고    scopus 로고
    • The essential Staphylococcus aureus gene fmhB is involved in the first step of peptidoglycan pentaglycine interpeptide formation
    • Rohrer, S., Ehlert, K., Tschierske, M., Labischinski, H., and Berger-Bachi, B. (1999) The essential Staphylococcus aureus gene fmhB is involved in the first step of peptidoglycan pentaglycine interpeptide formation. Proc Natl Acad Sci USA 96: 9351-9356.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9351-9356
    • Rohrer, S.1    Ehlert, K.2    Tschierske, M.3    Labischinski, H.4    Berger-Bachi, B.5
  • 40
    • 0036210885 scopus 로고    scopus 로고
    • Further evidence that a cell wall precursor [C(55)-MurNAc-(peptide)- GlcNAc] serves as an acceptor in a sorting reaction
    • Ruzin, A., Severin, A., Ritacco, F., Tabei, K., Singh, G., Bradford, P.A., et al. (2002) Further evidence that a cell wall precursor [C(55)-MurNAc-(peptide)-GlcNAc] serves as an acceptor in a sorting reaction. J Bacteriol 184: 2141-2147.
    • (2002) J Bacteriol , vol.184 , pp. 2141-2147
    • Ruzin, A.1    Severin, A.2    Ritacco, F.3    Tabei, K.4    Singh, G.5    Bradford, P.A.6
  • 41
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K.H., and Kandler, O. (1972) Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev 36: 407-477.
    • (1972) Bacteriol Rev , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 42
    • 0031576683 scopus 로고    scopus 로고
    • The roles of dimerization and membrane anchoring in activity of glycopeptide antibiotics against vancomycin-resistant bacteria
    • Sharman, G.J., Try, A.C., Dancer, R.J., Cho, Y.R., Staroske, T., Bardsley, B., et al. (1997) The roles of dimerization and membrane anchoring in activity of glycopeptide antibiotics against vancomycin-resistant bacteria. J Am Chem Soc 119: 12041-12047.
    • (1997) J Am Chem Soc , vol.119 , pp. 12041-12047
    • Sharman, G.J.1    Try, A.C.2    Dancer, R.J.3    Cho, Y.R.4    Staroske, T.5    Bardsley, B.6
  • 43
    • 0035198239 scopus 로고    scopus 로고
    • Direct interaction of a vancomycin derivative with bacterial enzymes involved in cell wall biosynthesis
    • Sinha Roy, R., Yang, P., Kodali, S., Xiong, Y., Kim, R.M., Griffin, P.R., et al. (2001) Direct interaction of a vancomycin derivative with bacterial enzymes involved in cell wall biosynthesis. Chem Biol 8: 1095-1106.
    • (2001) Chem Biol , vol.8 , pp. 1095-1106
    • Sinha Roy, R.1    Yang, P.2    Kodali, S.3    Xiong, Y.4    Kim, R.M.5    Griffin, P.R.6
  • 44
    • 0023184524 scopus 로고
    • Evolution of an inducible penicillin-target protein in methicillin-resistant Staphylococcus aureus by gene fusion
    • Song, M.D., Wachi, M., Doi, M., Ishino, F., and Matsuhashi, M. (1987) Evolution of an inducible penicillin-target protein in methicillin-resistant Staphylococcus aureus by gene fusion. FEBS Lett 221: 167-171.
    • (1987) FEBS Lett , vol.221 , pp. 167-171
    • Song, M.D.1    Wachi, M.2    Doi, M.3    Ishino, F.4    Matsuhashi, M.5
  • 45
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • Spratt, B.G. (1994) Resistance to antibiotics mediated by target alterations. Science 264: 388-393.
    • (1994) Science , vol.264 , pp. 388-393
    • Spratt, B.G.1
  • 46
    • 0024040909 scopus 로고
    • Penicillin-binding proteins of gram-negative bacteria
    • Spratt, B.G., and Cromie, K.D. (1988) Penicillin-binding proteins of gram-negative bacteria. Rev Infect Dis 10: 699-711.
    • (1988) Rev Infect Dis , vol.10 , pp. 699-711
    • Spratt, B.G.1    Cromie, K.D.2
  • 47
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock, A.M., Mottonen, J.M., Stock, J.B., and Schutt, C.E. (1989) Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature 337: 745-749.
    • (1989) Nature , vol.337 , pp. 745-749
    • Stock, A.M.1    Mottonen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 48
    • 0031019864 scopus 로고    scopus 로고
    • Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus
    • Strandén, A.M., Ehlert, K., Labischinski, H., and Berger-Bächi, B. (1997) Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus. J Bacteriol 179: 9-16.
    • (1997) J Bacteriol , vol.179 , pp. 9-16
    • Strandén, A.M.1    Ehlert, K.2    Labischinski, H.3    Berger-Bächi, B.4
  • 50
    • 1542275552 scopus 로고    scopus 로고
    • Evidence for the translation initiation of leaderless mRNAs by the intact 70S ribosome without its dissociation into subunits in Eubacteria
    • Udagawa, T., Shimizu, Y., and Ueda, T. (2004) Evidence for the translation initiation of leaderless mRNAs by the intact 70S ribosome without its dissociation into subunits in Eubacteria. J Biol Chem 278: 8539-8646.
    • (2004) J Biol Chem , vol.278 , pp. 8539-8646
    • Udagawa, T.1    Shimizu, Y.2    Ueda, T.3
  • 51
    • 0034680167 scopus 로고    scopus 로고
    • Molecular mechanisms that confer antibacterial drug resistance
    • Walsh, C.T. (2000) Molecular mechanisms that confer antibacterial drug resistance. Nature 406: 775-781.
    • (2000) Nature , vol.406 , pp. 775-781
    • Walsh, C.T.1
  • 52
    • 0029678259 scopus 로고    scopus 로고
    • Bacterial resistance to vancomycin: Five genes and one missing hydrogen bond tell the story
    • Walsh, C.T., Fisher, S.L., Park, I.S., Prahalad, M., and Wu, Z. (1996) Bacterial resistance to vancomycin: five genes and one missing hydrogen bond tell the story. Chem Biol 3: 21-28.
    • (1996) Chem Biol , vol.3 , pp. 21-28
    • Walsh, C.T.1    Fisher, S.L.2    Park, I.S.3    Prahalad, M.4    Wu, Z.5
  • 53
    • 0022636926 scopus 로고
    • Construction and characterisation of a series of multi-copy promoter-probe plasmid vectors for Streptomyces using the aminoglycoside phosphotransferase gene from Tn5 as indicator
    • Ward, J.M., Janssen, G.R., Kieser, T., Bibb, M.J., Buttner, M.J., and Bibb, M.J. (1986) Construction and characterisation of a series of multi-copy promoter-probe plasmid vectors for Streptomyces using the aminoglycoside phosphotransferase gene from Tn5 as indicator. Mol Gen Genet 203: 468-478.
    • (1986) Mol Gen Genet , vol.203 , pp. 468-478
    • Ward, J.M.1    Janssen, G.R.2    Kieser, T.3    Bibb, M.J.4    Buttner, M.J.5    Bibb, M.J.6
  • 54
    • 0344827209 scopus 로고    scopus 로고
    • Genetic analysis of a high-level vancomycin-resistant isolate of Staphylococcus aureus
    • Weigel, L.M., Clewell, D.B., Gill, S.R., Clark, N.C., McDougal, L.K., Flannagan, S.E., et al. (2003) Genetic analysis of a high-level vancomycin-resistant isolate of Staphylococcus aureus. Science 28: 1569-1571.
    • (2003) Science , vol.28 , pp. 1569-1571
    • Weigel, L.M.1    Clewell, D.B.2    Gill, S.R.3    Clark, N.C.4    McDougal, L.K.5    Flannagan, S.E.6
  • 55
    • 0033519259 scopus 로고    scopus 로고
    • Vancomycin group of antibiotics and the fight against resistant bacteria
    • Williams, D.H., and Bardsley, B. (1999) Vancomycin group of antibiotics and the fight against resistant bacteria. Angew Chem Int Ed 38: 1172-1193.
    • (1999) Angew Chem Int Ed , vol.38 , pp. 1172-1193
    • Williams, D.H.1    Bardsley, B.2
  • 56
    • 0020546708 scopus 로고
    • Detailed binding sites of the antibiotics vancomycin and ristocetin A: Determination of intermolecular distances in antibiotic/substrate complexes by use of the time-dependent NOE
    • Williams, D.H., Williamson, M.P., Butcher, D.W., and Hammond, S.J. (1983) Detailed binding sites of the antibiotics vancomycin and ristocetin A: determination of intermolecular distances in antibiotic/substrate complexes by use of the time-dependent NOE. J Am Chem Soc 105: 1332-1339.
    • (1983) J Am Chem Soc , vol.105 , pp. 1332-1339
    • Williams, D.H.1    Williamson, M.P.2    Butcher, D.W.3    Hammond, S.J.4
  • 57
    • 0030722957 scopus 로고    scopus 로고
    • Expression of a streptomycete leaderless mRNA encoding chloramphenicol acetyltransferase in Escherichia coli
    • Wu, C.J., and Janssen, G.R. (1997) Expression of a streptomycete leaderless mRNA encoding chloramphenicol acetyltransferase in Escherichia coli. J Bacteriol 179: 6824-6830.
    • (1997) J Bacteriol , vol.179 , pp. 6824-6830
    • Wu, C.J.1    Janssen, G.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.