메뉴 건너뛰기




Volumn 224, Issue 1-2, 1998, Pages 67-75

Identification and molecular characterization of a gene homologous to epr (endopeptidase resistance gene) in Staphylococcus aureus

Author keywords

ALE 1; FemA B; Lysostaphin; Peptidoglycan

Indexed keywords

GLYCINE; GLYCYLGLYCINE; HYDROLASE; LYSOSTAPHIN; PEPTIDE; PEPTIDOGLYCAN; PROTEINASE; SERINE;

EID: 0032509190     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00508-3     Document Type: Article
Times cited : (30)

References (31)
  • 1
    • 0014006256 scopus 로고
    • Staphylococcus aureus strains in the '52, 52A, 80, 81 complex'
    • Asheshov E.H. Staphylococcus aureus strains in the '52, 52A, 80, 81 complex'. Nature. 209:1966;638-639.
    • (1966) Nature , vol.209 , pp. 638-639
    • Asheshov, E.H.1
  • 2
    • 0024460146 scopus 로고
    • FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: Molecular cloning and characterization
    • Berger-Bächi B., Barberis-Maino L., Strässle A., Kayser F.H. FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: Molecular cloning and characterization. Mol. Gen. Genet. 219:1989;263-269.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 263-269
    • Berger-Bächi, B.1    Barberis-Maino, L.2    Strässle, A.3    Kayser, F.H.4
  • 3
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock W.O., Fernandez J.M., Short J.M. XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. BioTech. 5:1987;376-379.
    • (1987) BioTech. , vol.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 4
    • 0028116666 scopus 로고
    • A method to isolate RNA from gram-positive bacteria and mycobacteria
    • Cheung L., Eberhardt K.J., Fischetti V.A. A method to isolate RNA from gram-positive bacteria and mycobacteria. Analyt. Biochem. 222:1994;511-514.
    • (1994) Analyt. Biochem. , vol.222 , pp. 511-514
    • Cheung, L.1    Eberhardt, K.J.2    Fischetti, V.A.3
  • 5
    • 0028961002 scopus 로고
    • The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus
    • Dehart H.P., Heath H.E., Heath L.S., Leblanc P.A., Sloan G.L. The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus. Appl. Environ. Microbiol. 61:1995;1475-1479.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1475-1479
    • Dehart, H.P.1    Heath, H.E.2    Heath, L.S.3    Leblanc, P.A.4    Sloan, G.L.5
  • 6
    • 0026639828 scopus 로고
    • Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain
    • de Jonge B.L.M., Chang Y.-S., Gage D., Tomasz A. Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain. J. Biol. Chem. 267:1992;11248-11254.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11248-11254
    • De Jonge, B.L.M.1    Chang, Y.-S.2    Gage, D.3    Tomasz, A.4
  • 8
    • 0027498007 scopus 로고
    • Influence of femB on methicillin resistance and peptidoglycan metabolism in Staphylococcus aureus
    • Henze U., Sidow T., Wecke J., Labischinski H., Berger-Bächi B. Influence of femB on methicillin resistance and peptidoglycan metabolism in Staphylococcus aureus. J. Bacteriol. 175:1993;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
  • 9
    • 0015501773 scopus 로고
    • The biosynthesis of the cross-linking peptides in the cell wall peptidoglycan of Staphylococcus aureus
    • Kamiryo T., Matsuhashi M. The biosynthesis of the cross-linking peptides in the cell wall peptidoglycan of Staphylococcus aureus. J. Biol. Chem. 247:1972;6306-6311.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6306-6311
    • Kamiryo, T.1    Matsuhashi, M.2
  • 10
    • 0029759502 scopus 로고    scopus 로고
    • Staphylococcal peptidoglycan interpeptide bridge biosynthesis: A novel antistaphylococcal target?
    • Kopp U., Roos M., Wecke J., Labischinski H. Staphylococcal peptidoglycan interpeptide bridge biosynthesis: a novel antistaphylococcal target? Microb. Drug Res. 2:1996;29-41.
    • (1996) Microb. Drug Res. , vol.2 , pp. 29-41
    • Kopp, U.1    Roos, M.2    Wecke, J.3    Labischinski, H.4
  • 11
    • 0024470531 scopus 로고
    • Detection of bacterial cell wall hydrolases after denaturing polyacrylamide gel electrophoresis
    • LeClerc D., Asselin A. Detection of bacterial cell wall hydrolases after denaturing polyacrylamide gel electrophoresis. Can. J. Microbiol. 35:1989;749-753.
    • (1989) Can. J. Microbiol. , vol.35 , pp. 749-753
    • Leclerc, D.1    Asselin, A.2
  • 12
    • 0027987494 scopus 로고
    • Sequence analysis and molecular characterization of genes required for the biosynthesis of type 1 capsular polysaccharide in Staphylococcus aureus
    • Lin W.S., Cunneen T., Lee C.Y. Sequence analysis and molecular characterization of genes required for the biosynthesis of type 1 capsular polysaccharide in Staphylococcus aureus. J. Bacteriol. 176:1994;7005-7016.
    • (1994) J. Bacteriol. , vol.176 , pp. 7005-7016
    • Lin, W.S.1    Cunneen, T.2    Lee, C.Y.3
  • 13
    • 0025822537 scopus 로고
    • FemA, which encodes a factor essential for expression of methicillin resistance, affects glycine content of peptidoglycan in methicillin-resistant and methicillin-susceptible Staphylococcus aureus strains
    • Maidhof H., Reinicke B., Blümel P., Berger-Bächi B., Labischinski H. femA, which encodes a factor essential for expression of methicillin resistance, affects glycine content of peptidoglycan in methicillin-resistant and methicillin-susceptible Staphylococcus aureus strains. J. Bacteriol. 173:1991;3507-3513.
    • (1991) J. Bacteriol. , vol.173 , pp. 3507-3513
    • Maidhof, H.1    Reinicke, B.2    Blümel, P.3    Berger-Bächi, B.4    Labischinski, H.5
  • 14
    • 0001259110 scopus 로고
    • Biosynthesis of the peptidoglycan of bacterial cell wall
    • Matsuhashi M., Dietrich C.P., Strominger J.L. Biosynthesis of the peptidoglycan of bacterial cell wall. J. Biol. Chem. 242:1967;3191-3206.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3191-3206
    • Matsuhashi, M.1    Dietrich, C.P.2    Strominger, J.L.3
  • 15
    • 0018367443 scopus 로고
    • Relationship between lysostaphin endopeptidase production and cell wall composition in Staphylococcus staphylolyticus
    • Robinson J.M., Hardman J.K., Sloan G.L. Relationship between lysostaphin endopeptidase production and cell wall composition in Staphylococcus staphylolyticus. J. Bacteriol. 137:1979;1158-1164.
    • (1979) J. Bacteriol. , vol.137 , pp. 1158-1164
    • Robinson, J.M.1    Hardman, J.K.2    Sloan, G.L.3
  • 16
    • 0003122522 scopus 로고
    • Structure of peptidoglycan
    • In: Rogers, H.-J. (Ed.), Chapman & Hall, London, pp.
    • Rogers, H.-J., Perkins, H.R., Ward, J.B., 1980. Structure of peptidoglycan. In: Rogers, H.-J. (Ed.), Microbial Cell Walls and Membranes. Chapman & Hall, London, pp. 190-214.
    • (1980) Microbial Cell Walls and Membranes , pp. 190-214
    • Rogers, H.-J.1    Perkins, H.R.2    Ward, J.B.3
  • 19
    • 0001371631 scopus 로고
    • Purification and properties of lysostaphin - A lytic agent for Staphylococcus aureus
    • Schindler C.A., Schuhardt V.T. Purification and properties of lysostaphin - a lytic agent for Staphylococcus aureus. Biochim. Biophys. Acta. 97:1965;242-250.
    • (1965) Biochim. Biophys. Acta , vol.97 , pp. 242-250
    • Schindler, C.A.1    Schuhardt, V.T.2
  • 20
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer K.H., Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36:1972;407-477.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 21
    • 0000576186 scopus 로고
    • Gram-positive cocci
    • In: Sneath, P.H.A., Mair, N.S., Holt, J.G. (Eds.), Williams & Wilkins, Baltimore, MD, pp.
    • Schleifer, K.H., 1986. Gram-positive cocci. In: Sneath, P.H.A., Mair, N.S., Holt, J.G. (Eds.), Bergey's Manual of Systematic Bacteriology. Williams & Wilkins, Baltimore, MD, pp. 99-1103.
    • (1986) Bergey's Manual of Systematic Bacteriology , pp. 99-1103
    • Schleifer, K.H.1
  • 22
    • 0023968572 scopus 로고
    • Mercury and tetracycline resistance genes and flanking repeats associated with methicillin resistance on the chromosome of Staphylococcus aureus
    • Skinner S., Inglis B., Matthews P.R., Stewart P.R. Mercury and tetracycline resistance genes and flanking repeats associated with methicillin resistance on the chromosome of Staphylococcus aureus. Mol. Microbiol. 2:1988;289-297.
    • (1988) Mol. Microbiol. , vol.2 , pp. 289-297
    • Skinner, S.1    Inglis, B.2    Matthews, P.R.3    Stewart, P.R.4
  • 23
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern E.M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:1975;503-517.
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-517
    • Southern, E.M.1
  • 24
    • 0021797402 scopus 로고
    • Molecular relationships among serogroup B bacteriophages of Staphylococcus aureus
    • Stewart P.R., Waldron H.G., Lee J.S., Matthews P.R. Molecular relationships among serogroup B bacteriophages of Staphylococcus aureus. J. Virol. 55:1985;111-116.
    • (1985) J. Virol. , vol.55 , pp. 111-116
    • Stewart, P.R.1    Waldron, H.G.2    Lee, J.S.3    Matthews, P.R.4
  • 25
    • 0031019864 scopus 로고    scopus 로고
    • Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus
    • Stranden A.M., Ehlert K., Labischinski H., Berger-Bächi B. Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus. J. Bacteriol. 179:1997;9-16.
    • (1997) J. Bacteriol. , vol.179 , pp. 9-16
    • Stranden, A.M.1    Ehlert, K.2    Labischinski, H.3    Berger-Bächi, B.4
  • 26
    • 0025015465 scopus 로고
    • Characterization of sodium dodecyl sulfate-stable Staphylococcus aureus bacteriolytic enzymes by polyacrylamide gel electrophoresis
    • Sugai M., Akiyama T., Komatsuzawa H., Miyake Y., Suginaka H. Characterization of sodium dodecyl sulfate-stable Staphylococcus aureus bacteriolytic enzymes by polyacrylamide gel electrophoresis. J. Bacteriol. 172:1990;6494-6498.
    • (1990) J. Bacteriol. , vol.172 , pp. 6494-6498
    • Sugai, M.1    Akiyama, T.2    Komatsuzawa, H.3    Miyake, Y.4    Suginaka, H.5
  • 27
    • 0031046570 scopus 로고    scopus 로고
    • Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis EPK1
    • Sugai M., Fujiwara T., Akiyama T., Ohara M., Komatsuzawa H., Inoue S., Suginaka H. Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis EPK1. J. Bacteriol. 179:1997;1193-1202.
    • (1997) J. Bacteriol. , vol.179 , pp. 1193-1202
    • Sugai, M.1    Fujiwara, T.2    Akiyama, T.3    Ohara, M.4    Komatsuzawa, H.5    Inoue, S.6    Suginaka, H.7
  • 28
    • 0030747364 scopus 로고    scopus 로고
    • Epr, which encodes glycylglycine endopeptidase resistance, is homologous to femAB and affects serine content of peptidoglycan cross bridges in Staphylococcus capitis and Staphylococcus aureus
    • Sugai M., Fujiwara T., Ohta K., Komatsuzawa H., Ohara M., Suginaka H. epr, which encodes glycylglycine endopeptidase resistance, is homologous to femAB and affects serine content of peptidoglycan cross bridges in Staphylococcus capitis and Staphylococcus aureus. J. Bacteriol. 179:1997;4311-4318.
    • (1997) J. Bacteriol. , vol.179 , pp. 4311-4318
    • Sugai, M.1    Fujiwara, T.2    Ohta, K.3    Komatsuzawa, H.4    Ohara, M.5    Suginaka, H.6
  • 29
    • 0014665803 scopus 로고
    • A method for demonstrating the stepwise addition of glycine from transfer RNA into the murein precursor of Staphylococcus aureus
    • Thorndike J., Park J.T. A method for demonstrating the stepwise addition of glycine from transfer RNA into the murein precursor of Staphylococcus aureus. Biochem. Biophys. Res. Commun. 34:1969;642-647.
    • (1969) Biochem. Biophys. Res. Commun. , vol.34 , pp. 642-647
    • Thorndike, J.1    Park, J.T.2
  • 30
    • 0030970757 scopus 로고    scopus 로고
    • Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus
    • Thumm G., Götz F. Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus. Mol. Microbiol. 23:1997;1251-1265.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1251-1265
    • Thumm, G.1    Götz, F.2
  • 31
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vector and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vector and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 33:1985;103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.