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Volumn 181, Issue 20, 1999, Pages 6552-6555

Gene disruption studies of penicillin-binding proteins 1a, 1b, and 2a in Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

BAMBERMYCIN; GLYCOSYLTRANSFERASE; PENICILLIN BINDING PROTEIN;

EID: 0032716126     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.20.6552-6555.1999     Document Type: Article
Times cited : (62)

References (38)
  • 2
    • 0030603148 scopus 로고    scopus 로고
    • The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes
    • Berardino, M. D., A. Dijkstra, D. Stuber, W. Keck, and M. Gubler. 1996. The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes. FEBS Lett. 392:184-188.
    • (1996) FEBS Lett. , vol.392 , pp. 184-188
    • Berardino, M.D.1    Dijkstra, A.2    Stuber, D.3    Keck, W.4    Gubler, M.5
  • 3
    • 0029116529 scopus 로고
    • Use of a novel mobilizable vector to inactivate the scrA gene of Streptococcus sobrinus by allelic replacement
    • Buckley, N. D., L. Lee, and D. J. LeBlanc. 1995. Use of a novel mobilizable vector to inactivate the scrA gene of Streptococcus sobrinus by allelic replacement. J. Bacteriol. 177:5028-5034.
    • (1995) J. Bacteriol. , vol.177 , pp. 5028-5034
    • Buckley, N.D.1    Lee, L.2    LeBlanc, D.J.3
  • 4
    • 0027999183 scopus 로고
    • A neuraminidase from Streptococcus pneumoniae has the features of a surface protein
    • Camara, M., G. J. Boulnois, P. W. Andrew, and T. J. Mitchell. 1994. A neuraminidase from Streptococcus pneumoniae has the features of a surface protein. Infect. Immun. 62:3688-3695.
    • (1994) Infect. Immun. , vol.62 , pp. 3688-3695
    • Camara, M.1    Boulnois, G.J.2    Andrew, P.W.3    Mitchell, T.J.4
  • 5
    • 0031771077 scopus 로고    scopus 로고
    • Identification, purification, and characterization of transpeptidase and glycosyltransferase domains of Streptococcus pneumoniae penicillin-binding protein 1a
    • di Guilmi, A. M., N. Mouz, J. P. Andrieu, J. Hoskins, S. R. Jaskunas, J. Gagnon, O. Dideberg, and T. Vernet. 1998. Identification, purification, and characterization of transpeptidase and glycosyltransferase domains of Streptococcus pneumoniae penicillin-binding protein 1a. J. Bacteriol. 180:5652-5659.
    • (1998) J. Bacteriol. , vol.180 , pp. 5652-5659
    • Di Guilmi, A.M.1    Mouz, N.2    Andrieu, J.P.3    Hoskins, J.4    Jaskunas, S.R.5    Gagnon, J.6    Dideberg, O.7    Vernet, T.8
  • 7
    • 0024422438 scopus 로고
    • Nucleotide sequence of the penicillin-binding protein 2B gene of Streptococcus pneumoniae strain R6
    • Dowson, C. G., A. Hutchison, and B. G. Spratt. 1989. Nucleotide sequence of the penicillin-binding protein 2B gene of Streptococcus pneumoniae strain R6. Nucleic Acids Res. 17:7518.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 7518
    • Dowson, C.G.1    Hutchison, A.2    Spratt, B.G.3
  • 9
    • 0028173341 scopus 로고
    • Molecular structures of penicillin-binding proteins and beta-lactamases
    • Ghuysen, J.-M. 1994. Molecular structures of penicillin-binding proteins and beta-lactamases. Trends Microbiol. 2:372-380.
    • (1994) Trends Microbiol. , vol.2 , pp. 372-380
    • Ghuysen, J.-M.1
  • 10
    • 0026049801 scopus 로고
    • Serine beta-lactamases and penicillin-binding proteins
    • Ghuysen, J. M. 1991. Serine beta-lactamases and penicillin-binding proteins. Annu. Rev. Microbiol. 45:37-67.
    • (1991) Annu. Rev. Microbiol. , vol.45 , pp. 37-67
    • Ghuysen, J.M.1
  • 11
    • 0001098472 scopus 로고
    • Biochemistry of the penicilloyl serine transferases
    • J.-M. Ghuysen and R. Hakenbeck (ed.), Elsevier Science, Amsterdam, The Netherlands
    • Ghuysen, J.-M., and G. Dive. 1994. Biochemistry of the penicilloyl serine transferases, p. 103-129. In J.-M. Ghuysen and R. Hakenbeck (ed.), Bacterial cell wall. Elsevier Science, Amsterdam, The Netherlands.
    • (1994) Bacterial Cell Wall , pp. 103-129
    • Ghuysen, J.-M.1    Dive, G.2
  • 12
    • 0023049764 scopus 로고
    • Antibodies against the benzylpenicillin moiety as a probe for penicillin-binding proteins
    • Hakenbeck, R., H. Ellerbrok, and T. Briese. 1986. Antibodies against the benzylpenicillin moiety as a probe for penicillin-binding proteins. Eur. J. Biochem. 157:101-106.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 101-106
    • Hakenbeck, R.1    Ellerbrok, H.2    Briese, T.3
  • 14
    • 0028845364 scopus 로고
    • An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae
    • Havarstein, L. S., G. Coomaraswamy, and D. A. Morrison. 1995. An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae. Proc. Natl. Acad. Sci. USA 92:11140-11144.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11140-11144
    • Havarstein, L.S.1    Coomaraswamy, G.2    Morrison, D.A.3
  • 15
    • 0014410414 scopus 로고
    • Moenomycin: An inhibitor of cell wall synthesis
    • Huber, F., and F. Nesemann. 1968. Moenomycin: an inhibitor of cell wall synthesis. Biochem. Biophys. Res. Commun. 30:7-13.
    • (1968) Biochem. Biophys. Res. Commun. , vol.30 , pp. 7-13
    • Huber, F.1    Nesemann, F.2
  • 16
    • 0019289889 scopus 로고
    • Dual enzyme activities of cell wall peptidoglycan synthesis: Peptidoglycan transglycosylase and penicillin-sensitive transpeptidase in purified preparations of Escherichia coli penicillin-binding protein 1A
    • Ishino, F., K. Mitsui, S. Tamaki, and M. Matsuhashi. 1980. Dual enzyme activities of cell wall peptidoglycan synthesis: peptidoglycan transglycosylase and penicillin-sensitive transpeptidase in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochem. Biophys. Res. Commun. 97:287-293.
    • (1980) Biochem. Biophys. Res. Commun. , vol.97 , pp. 287-293
    • Ishino, F.1    Mitsui, K.2    Tamaki, S.3    Matsuhashi, M.4
  • 17
    • 0021862671 scopus 로고
    • Dispensability of either penicillin-binding protein-1a or -1b involved in the essential process for cell elongation in Escherichia coli
    • Kato, J., H. Suzuki, and Y. Hirota. 1985. Dispensability of either penicillin-binding protein-1a or -1b involved in the essential process for cell elongation in Escherichia coli. Mol. Gen. Genet. 200:272-277.
    • (1985) Mol. Gen. Genet. , vol.200 , pp. 272-277
    • Kato, J.1    Suzuki, H.2    Hirota, Y.3
  • 18
    • 0027446117 scopus 로고
    • Deletion analysis of the essentiality of penicillin-binding proteins 1A, 2B and 2X of Streptococcus pneumoniae
    • Kell, C. M., U. K. Sharma, D. G. Dowson, C. Town, T. S. Balganesh, and B. G. Spratt. 1993. Deletion analysis of the essentiality of penicillin-binding proteins 1A, 2B and 2X of Streptococcus pneumoniae. FEMS Microbiol. Lett. 106:171-176.
    • (1993) FEMS Microbiol. Lett. , vol.106 , pp. 171-176
    • Kell, C.M.1    Sharma, U.K.2    Dowson, D.G.3    Town, C.4    Balganesh, T.S.5    Spratt, B.G.6
  • 20
    • 0024374096 scopus 로고
    • Nucleotide sequences of the pbpX genes encoding the penicillin-binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506
    • Laible, G., R. Hakenbeck, M. A. Sicard, B. Joris, and J.-M. Ghuysen. 1989. Nucleotide sequences of the pbpX genes encoding the penicillin-binding proteins 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506. Mol. Microbiol. 3:1337-1348.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1337-1348
    • Laible, G.1    Hakenbeck, R.2    Sicard, M.A.3    Joris, B.4    Ghuysen, J.-M.5
  • 21
    • 0025816587 scopus 로고
    • Inter-species recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae
    • Laible, G., B. G. Spratt, and R. Hakenbeck. 1991. Inter-species recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 5:1993-2002.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1993-2002
    • Laible, G.1    Spratt, B.G.2    Hakenbeck, R.3
  • 22
    • 0026782639 scopus 로고
    • Molecular, genetic, and functional analysis of the basic replicon of pVA380-1a plasmid of oral streptococcal origin
    • LeBlanc, D. J., L. N. Lee, and A. Abu-Al-Jaibat. 1992. Molecular, genetic, and functional analysis of the basic replicon of pVA380-1a plasmid of oral streptococcal origin. Plasmid 28:130-145.
    • (1992) Plasmid , vol.28 , pp. 130-145
    • LeBlanc, D.J.1    Lee, L.N.2    Abu-Al-Jaibat, A.3
  • 23
    • 0026711139 scopus 로고
    • Nucleotide sequences of genes encoding penicillin-binding proteins from Streptococcus pneumoniae and Streptococcus oralis with high homology to Escherichia coli penicillin-binding proteins 1A and 1B
    • Martin, C., T. Briese, and R. Hakenbeck. 1992. Nucleotide sequences of genes encoding penicillin-binding proteins from Streptococcus pneumoniae and Streptococcus oralis with high homology to Escherichia coli penicillin-binding proteins 1A and 1B. J. Bacteriol. 174:4517-4523.
    • (1992) J. Bacteriol. , vol.174 , pp. 4517-4523
    • Martin, C.1    Briese, T.2    Hakenbeck, R.3
  • 24
    • 0026782144 scopus 로고
    • Relatedness of penicillin-binding protein 1a genes from different clones of penicillin-resistant Streptococcus pneumoniae isolated in South Africa and Spain
    • Martin, C., C. Sibold, and R. Hakenbeck. 1992. Relatedness of penicillin-binding protein 1a genes from different clones of penicillin-resistant Streptococcus pneumoniae isolated in South Africa and Spain. EMBO J. 11:3831-3836.
    • (1992) EMBO J. , vol.11 , pp. 3831-3836
    • Martin, C.1    Sibold, C.2    Hakenbeck, R.3
  • 25
    • 10044253923 scopus 로고
    • Utilization of lipid-linked precursors and the formation of peptidoglycan in the process of cell growth and division. Membrane enzymes involved in the final steps of peptidoglycan synthesis and the mechanism of their regulation
    • J.-M. Ghuysen and R. Hakenbeck (ed.), Elsevier Sciences Amsterdam, The Netherlands
    • Matsuhashi, M. 1994. Utilization of lipid-linked precursors and the formation of peptidoglycan in the process of cell growth and division. Membrane enzymes involved in the final steps of peptidoglycan synthesis and the mechanism of their regulation, p. 55-72. In J.-M. Ghuysen and R. Hakenbeck (ed.), Bacterial cell wall. Elsevier Sciences Amsterdam, The Netherlands.
    • (1994) Bacterial Cell Wall , pp. 55-72
    • Matsuhashi, M.1
  • 26
  • 27
    • 0028145059 scopus 로고
    • Conjugal transfer of cosmid DNA from Escherichia coli to Saccharopolyspora spinosa: Effects of chromosomal insertions on macrolide A83543 production
    • Matsushima, P., M. C. Broughton, J. R. Turner, and R. H. Baltz. 1994. Conjugal transfer of cosmid DNA from Escherichia coli to Saccharopolyspora spinosa: effects of chromosomal insertions on macrolide A83543 production. Gene 146:39-45.
    • (1994) Gene , vol.146 , pp. 39-45
    • Matsushima, P.1    Broughton, M.C.2    Turner, J.R.3    Baltz, R.H.4
  • 28
    • 0021690285 scopus 로고
    • Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides
    • Nakagawa, J., S. Tamaki, S. Tomioka, and M. Matsuhashi. 1984. Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. J. Biol. Chem. 259:13937-13946.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13937-13946
    • Nakagawa, J.1    Tamaki, S.2    Tomioka, S.3    Matsuhashi, M.4
  • 30
    • 0344008953 scopus 로고    scopus 로고
    • Unpublished data
    • Nicas, T. I. Unpublished data.
    • Nicas, T.I.1
  • 31
    • 0033014014 scopus 로고    scopus 로고
    • Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins
    • Paik, J., I. Kern, R. Lurz, and R. Hakenbeck. 1999. Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins. J. Bacteriol. 181:3852-3856.
    • (1999) J. Bacteriol. , vol.181 , pp. 3852-3856
    • Paik, J.1    Kern, I.2    Lurz, R.3    Hakenbeck, R.4
  • 32
    • 0030058939 scopus 로고    scopus 로고
    • Monofunctional biosynthetic peptidoglycan transglycosylases
    • Spratt, B. G., J. Zhou, M. Taylor, and M. J. Merrick. 1996. Monofunctional biosynthetic peptidoglycan transglycosylases. Mol. Microbiol. 19:639-647.
    • (1996) Mol. Microbiol. , vol.19 , pp. 639-647
    • Spratt, B.G.1    Zhou, J.2    Taylor, M.3    Merrick, M.J.4
  • 34
    • 0017679507 scopus 로고
    • Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro
    • Tamaki, S., S. Nakajima, and M. Matsuhashi. 1977. Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro. Proc. Natl. Acad. Sci. USA 74:5472-5476.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 5472-5476
    • Tamaki, S.1    Nakajima, S.2    Matsuhashi, M.3
  • 36
    • 0022389693 scopus 로고
    • Lysis of Escherichia coli by beta-lactam antibiotics: Deletion analysis of the role of penicillin-binding proteins 1A and 1B
    • Yousif, S. Y., J. K. Broome-Smith, and B. G. Spratt. 1985. Lysis of Escherichia coli by beta-lactam antibiotics: deletion analysis of the role of penicillin-binding proteins 1A and 1B. J. Gen. Microbiol. 131:2839-2845.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 2839-2845
    • Yousif, S.Y.1    Broome-Smith, J.K.2    Spratt, B.G.3
  • 37
    • 0345303189 scopus 로고    scopus 로고
    • Unpublished data
    • Zhao, G. Unpublished data.
    • Zhao, G.1
  • 38
    • 0028882487 scopus 로고
    • Hybrid proteins of the transglycosylase and the transpeptidase domains of PBP1b and PBP3 of Escherichia coli
    • Zijderveld, C. A. L., Q. Waisfisz, M. E. G. Aarsman, and N. Nanninga. 1995. Hybrid proteins of the transglycosylase and the transpeptidase domains of PBP1b and PBP3 of Escherichia coli. J. Bacteriol. 177:6290-6293.
    • (1995) J. Bacteriol. , vol.177 , pp. 6290-6293
    • Zijderveld, C.A.L.1    Waisfisz, Q.2    Aarsman, M.E.G.3    Nanninga, N.4


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