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Volumn 178, Issue 17, 1996, Pages 5272-5278

Evidence that the PBP 5 synthesis repressor (psr) of Enterococcus hirae is also involved in the regulation of cell wall composition and other cell wall-related properties

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME; PENICILLIN BINDING PROTEIN; PENICILLIN BINDING PROTEIN 5; PENICILLIN G; RHAMNOSE; UNCLASSIFIED DRUG;

EID: 0029829905     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.17.5272-5278.1996     Document Type: Article
Times cited : (27)

References (30)
  • 1
    • 0022516658 scopus 로고
    • In Streptococcus faecium penicillin-binding protein 5 alone is sufficient for growth at sub-maximal but not at maximal rate
    • Canepari, P., M. D. M. Lleó, G. Cornaglia, R. Fontana, and G. Satta. 1986. In Streptococcus faecium penicillin-binding protein 5 alone is sufficient for growth at sub-maximal but not at maximal rate. J. Gen. Microbiol. 132:625-631.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 625-631
    • Canepari, P.1    Lleó, M.D.M.2    Cornaglia, G.3    Fontana, R.4    Satta, G.5
  • 2
    • 0026831875 scopus 로고
    • Cloning and sequence analysis of the muramidase-2 gene from Enterococcus hirae
    • Chu, C.-P., R. Kariyama, L. Daneo-Moore, and G. D. Shockman. 1992. Cloning and sequence analysis of the muramidase-2 gene from Enterococcus hirae. J. Bacteriol. 174:1619-1625.
    • (1992) J. Bacteriol. , vol.174 , pp. 1619-1625
    • Chu, C.-P.1    Kariyama, R.2    Daneo-Moore, L.3    Shockman, G.D.4
  • 3
    • 0017870993 scopus 로고
    • Autolytic defective mutant of Streptococcus faecalis
    • Cornett, J. B., B. E. Redman, and G. D. Shockman. 1978. Autolytic defective mutant of Streptococcus faecalis. J. Bacteriol. 133:631-640.
    • (1978) J. Bacteriol. , vol.133 , pp. 631-640
    • Cornett, J.B.1    Redman, B.E.2    Shockman, G.D.3
  • 4
    • 0019209161 scopus 로고
    • The penicillin-binding proteins in Streptococcus faecalis ATCC 9790
    • Coyette, J., J.-M. Ghuysen, and R. Fontana. 1980. The penicillin-binding proteins in Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 110:445-456.
    • (1980) Eur. J. Biochem. , vol.110 , pp. 445-456
    • Coyette, J.1    Ghuysen, J.-M.2    Fontana, R.3
  • 6
    • 85035171873 scopus 로고
    • The Rockefeller University. Personal communication
    • de Junge, B. (The Rockefeller University). 1995. Personal communication.
    • (1995)
    • De Junge, B.1
  • 7
    • 0026077749 scopus 로고
    • The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2′ are similar
    • El Kharroubi, A., P. Jacques, G. Piras, J. Van Beeumen, J. Coyette, and J.-M. Ghuysen. 1991. The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2′ are similar. Biochem. J. 280:463-469.
    • (1991) Biochem. J. , vol.280 , pp. 463-469
    • El Kharroubi, A.1    Jacques, P.2    Piras, G.3    Van Beeumen, J.4    Coyette, J.5    Ghuysen, J.-M.6
  • 8
    • 0014443051 scopus 로고
    • Control of teichoic acid and teichuronic acid biosynthesis in chemostat cultures of B. subtilis var. niger
    • Ellwood, D. C., and D. W. Tempest. 1969. Control of teichoic acid and teichuronic acid biosynthesis in chemostat cultures of B. subtilis var. niger. Biochem. J. 111:1-5.
    • (1969) Biochem. J. , vol.111 , pp. 1-5
    • Ellwood, D.C.1    Tempest, D.W.2
  • 9
    • 0028041404 scopus 로고
    • Overproduction of a low-affinity penicillin-binding protein high-level ampicillin resistance in Enterococcus faecium
    • Fontana, R., M. Aldegheri, M. Ligozzi, H. Lopez, A. Sucari, and G. Satta. 1994. Overproduction of a low-affinity penicillin-binding protein and high-level ampicillin resistance in Enterococcus faecium. Antimicrob. Agents Chemother. 38:1980-1983.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1980-1983
    • Fontana, R.1    Aldegheri, M.2    Ligozzi, M.3    Lopez, H.4    Sucari, A.5    Satta, G.6
  • 10
    • 0021079734 scopus 로고
    • Identification of a streptococcal penicillin-binding protein that reacts very slowly with penicillin
    • Fontana, R., R. Cerini, P. Longoni, A. Grossato, and P. Canepari. 1983. Identification of a streptococcal penicillin-binding protein that reacts very slowly with penicillin. J. Bacteriol. 155:1343-1350.
    • (1983) J. Bacteriol. , vol.155 , pp. 1343-1350
    • Fontana, R.1    Cerini, R.2    Longoni, P.3    Grossato, A.4    Canepari, P.5
  • 11
    • 0022402975 scopus 로고
    • Transition from resistance to hypersusceptibility to β-lactam antibiotics associated with loss of a low-affinity penicillin-binding protein in a Streptococcus faecium mutant highly resistant to penicillin
    • Fontana, R., A. Grossato, L. Rossi, Y. R. Cheng, and G. Satta. 1985. Transition from resistance to hypersusceptibility to β-lactam antibiotics associated with loss of a low-affinity penicillin-binding protein in a Streptococcus faecium mutant highly resistant to penicillin. Antimicrob. Agents Chemother. 28:678-683.
    • (1985) Antimicrob. Agents Chemother. , vol.28 , pp. 678-683
    • Fontana, R.1    Grossato, A.2    Rossi, L.3    Cheng, Y.R.4    Satta, G.5
  • 13
    • 0025315524 scopus 로고
    • Properties of cell wall-associated DD-carboxypeptidase of Enterococcus hirae (Streptococcus faecium) ATCC 9790 extracted with alkali
    • Kariyama, R., O. Massidda, L. Daneo-Moore, and G. D. Shockman. 1990. Properties of cell wall-associated DD-carboxypeptidase of Enterococcus hirae (Streptococcus faecium) ATCC 9790 extracted with alkali. J. Bacteriol. 172:3718-3724.
    • (1990) J. Bacteriol. , vol.172 , pp. 3718-3724
    • Kariyama, R.1    Massidda, O.2    Daneo-Moore, L.3    Shockman, G.D.4
  • 14
    • 0026691017 scopus 로고
    • Extracellular and cellular distribution of muramidase-2 and muramidase-1 of Enterococcus hirae ATCC 9790
    • Kariyama, R., and G. D. Shockman. 1992. Extracellular and cellular distribution of muramidase-2 and muramidase-1 of Enterococcus hirae ATCC 9790. J. Bacteriol. 174:3235-3241.
    • (1992) J. Bacteriol. , vol.174 , pp. 3235-3241
    • Kariyama, R.1    Shockman, G.D.2
  • 15
    • 0021099776 scopus 로고
    • Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecalis, a bacterial glycoenzyme
    • Kawamura, T., and G. D. Shockman. 1983. Purification and some properties of the endogenous, autolytic N-acetylmuramoylhydrolase of Streptococcus faecalis, a bacterial glycoenzyme. J. Biol. Chem. 258:9514-9521.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9514-9521
    • Kawamura, T.1    Shockman, G.D.2
  • 16
    • 0026519577 scopus 로고
    • Overproduction of a penicillin-binding protein is not the only mechanism of penicillin resistance in Enterococcus faecium
    • Klare, I., A. C. Rodloff, J. Wagner, W. Witte, and R. Hakenbeck. 1992. Overproduction of a penicillin-binding protein is not the only mechanism of penicillin resistance in Enterococcus faecium. Antimicrob. Agents Chemother. 36:783-787.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 783-787
    • Klare, I.1    Rodloff, A.C.2    Wagner, J.3    Witte, W.4    Hakenbeck, R.5
  • 17
    • 0026673165 scopus 로고
    • Sequencing and analysis of the Bacillus subtilis lytRABC divergon: A regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier
    • Lazarevic, V., P. Margot, B. Soldo, and D. Karamata. 1992. Sequencing and analysis of the Bacillus subtilis lytRABC divergon: a regulatory unit encompassing the structural genes of the N-acetylmuramoyl-L-alanine amidase and its modifier. J. Gen. Microbiol. 138:1949-1961.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1949-1961
    • Lazarevic, V.1    Margot, P.2    Soldo, B.3    Karamata, D.4
  • 18
    • 0027537345 scopus 로고
    • Identification of a genetic element (psr) which negatively controls expression of Enterococcus hirae penicillin-binding protein 5
    • Ligozzi, M., F. Pittaluga, and R. Fonlana. 1993. Identification of a genetic element (psr) which negatively controls expression of Enterococcus hirae penicillin-binding protein 5. J. Bacteriol. 175:2046-2051.
    • (1993) J. Bacteriol. , vol.175 , pp. 2046-2051
    • Ligozzi, M.1    Pittaluga, F.2    Fonlana, R.3
  • 19
    • 0023626896 scopus 로고
    • Bacteriostatic and bactericidal activities of β-lactams against Streptococcus (Enterococcus) faecium are associated with saturation of different penicillin-binding proteins
    • Lleo, M. D. M. P. Canepari, G. Cornaglia, R. Fontana, and G. Satta. 1987. Bacteriostatic and bactericidal activities of β-lactams against Streptococcus (Enterococcus) faecium are associated with saturation of different penicillin-binding proteins. Antimicrob. Agents Chemother. 31:1618-1626.
    • (1987) Antimicrob. Agents Chemother. , vol.31 , pp. 1618-1626
    • Lleo, M.D.M.1    Canepari, P.2    Cornaglia, G.3    Fontana, R.4    Satta, G.5
  • 21
    • 0000787896 scopus 로고
    • Teichoic acid and peptidoglycan assembly in gram positive organisms
    • V. Ginsberg and P. Robbins (ed.), Wiley, New York
    • Munson, R. S., and L. Glaser. 1981. Teichoic acid and peptidoglycan assembly in gram positive organisms, p. 91-123. In V. Ginsberg and P. Robbins (ed.), Biology of carbohydrates, vol. 1. Wiley, New York.
    • (1981) Biology of Carbohydrates , vol.1 , pp. 91-123
    • Munson, R.S.1    Glaser, L.2
  • 22
    • 0015417926 scopus 로고
    • Influence of macromolecular biosynthesis on cellular autolysis in Streptococcus faecalis
    • Sayare, M., L. Daneo-Moore, and G. D. Shockman. 1972. Influence of macromolecular biosynthesis on cellular autolysis in Streptococcus faecalis. J. Bacteriol. 112:337-344.
    • (1972) J. Bacteriol. , vol.112 , pp. 337-344
    • Sayare, M.1    Daneo-Moore, L.2    Shockman, G.D.3
  • 23
    • 9544234058 scopus 로고
    • Bacterial cell wall synthesis: The effect of threonine depletion
    • Shockman, G. D. 1959. Bacterial cell wall synthesis: the effect of threonine depletion. J. Biol. Chem. 234:2340-2342.
    • (1959) J. Biol. Chem. , vol.234 , pp. 2340-2342
    • Shockman, G.D.1
  • 24
    • 0009853507 scopus 로고
    • Amino acids
    • F. Kavanagh (ed.), Academic Press, New York
    • Shockman, G. D. 1963. Amino acids, p. 567-673. In F. Kavanagh (ed.), Analytical microbiology. Academic Press, New York.
    • (1963) Analytical Microbiology , pp. 567-673
    • Shockman, G.D.1
  • 26
    • 77956866741 scopus 로고
    • Microbial peptidoglycan (murein) hydrolases
    • J.-M. Ghuysen and R. Hakenbeck (ed.), Elsevier Science B. V., Amsterdam
    • Shockman, G. D., and J.-V. Höltje. 1994. Microbial peptidoglycan (murein) hydrolases, p. 131-166. In J.-M. Ghuysen and R. Hakenbeck (ed.), Bacterial cell wall. Elsevier Science B. V., Amsterdam.
    • (1994) Bacterial Cell Wall , pp. 131-166
    • Shockman, G.D.1    Höltje, J.-V.2
  • 27
    • 0011171195 scopus 로고
    • Relations between bacterial cell wall synthesis, growth phase, and autolysis
    • Shockman, G. D., J. J. Kolb, and G. Toennies. 1958. Relations between bacterial cell wall synthesis, growth phase, and autolysis. J. Biol. Chem. 230:961-977.
    • (1958) J. Biol. Chem. , vol.230 , pp. 961-977
    • Shockman, G.D.1    Kolb, J.J.2    Toennies, G.3
  • 28
    • 9544245332 scopus 로고
    • The relationship of autolysin to lysozyme sensitivity of Streptococcus faecalis 9790
    • L. B. Guze (ed.), The Williams and Wilkins Co., Baltimore
    • Shockman, G. D., J. S. Thompson, and M. J. Conover. 1968. The relationship of autolysin to lysozyme sensitivity of Streptococcus faecalis 9790, p. 248-260. In L. B. Guze (ed.), Microbial protoplasts, spheroplasts and L-forms. The Williams and Wilkins Co., Baltimore.
    • (1968) Microbial Protoplasts, Spheroplasts and L-forms , pp. 248-260
    • Shockman, G.D.1    Thompson, J.S.2    Conover, M.J.3
  • 29
    • 77956994971 scopus 로고
    • Analysis of sugars found in glycopeptide
    • Spiro, R. G. 1966. Analysis of sugars found in glycopeptide. Methods Enzymol. 8:3-26.
    • (1966) Methods Enzymol. , vol.8 , pp. 3-26
    • Spiro, R.G.1
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


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