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Volumn 23, Issue 5, 1997, Pages 935-944

The penicillin sensory transducer, BlaR, involved in the inducibility of β-lactamase synthesis in Bacillus licheniformis is embedded in the plasma membrane via a four-α-helix bundle

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; PENICILLIN G;

EID: 0031033660     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.2761642.x     Document Type: Article
Times cited : (47)

References (32)
  • 1
    • 0027473683 scopus 로고
    • Sec dependent and sec independent assembly of E. coli inner membrane proteins: The topological rules depend on chain length
    • Andersson, H., and von Heijne, G. (1993) Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length. EMBO J 12: 683-691.
    • (1993) EMBO J , vol.12 , pp. 683-691
    • Andersson, H.1    Von Heijne, G.2
  • 2
    • 0025057970 scopus 로고
    • In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT
    • Baneyx, F., and Georgiou, G. (1990) In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT. J Bacteriol 172: 491-494.
    • (1990) J Bacteriol , vol.172 , pp. 491-494
    • Baneyx, F.1    Georgiou, G.2
  • 3
    • 0025855940 scopus 로고
    • Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: Protease III degrades high-molecularweight substrates in vivo
    • Baneyx, F., and Georgiou, G. (1991) Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecularweight substrates in vivo. J Bacteriol 173: 2696-2703.
    • (1991) J Bacteriol , vol.173 , pp. 2696-2703
    • Baneyx, F.1    Georgiou, G.2
  • 4
    • 0025936242 scopus 로고
    • Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations
    • Brasseur, R. (1991) Differentiation of lipid-associating helices by use of three-dimensional molecular hydrophobicity potential calculations. J Biol Chem 266: 16120-16127.
    • (1991) J Biol Chem , vol.266 , pp. 16120-16127
    • Brasseur, R.1
  • 5
    • 0025053613 scopus 로고
    • Beta-lactamase as a probe of membrane protein assembly and protein export
    • Broome-Smith, J.K., Tadayyon, M., and Zhang, Y. (1990) Beta-lactamase as a probe of membrane protein assembly and protein export. Mol Microbiol 4: 1637-1644.
    • (1990) Mol Microbiol , vol.4 , pp. 1637-1644
    • Broome-Smith, J.K.1    Tadayyon, M.2    Zhang, Y.3
  • 6
    • 0028568176 scopus 로고
    • TOPPRED II: An improved software for membrane protein structure predictions
    • Claros, G., and von Heijne, G. (1994) TOPPRED II: an improved software for membrane protein structure predictions. CABIOS 10: 685-686.
    • (1994) CABIOS , vol.10 , pp. 685-686
    • Claros, G.1    Von Heijne, G.2
  • 7
    • 0019498995 scopus 로고
    • Cell wall turnover in batch and chemostat cultures of Bacillus subtilis
    • De Boer, W.R., Kruyssen, F.J., and Wouters, J.T.M. (1981) Cell wall turnover in batch and chemostat cultures of Bacillus subtilis. J Bacteriol 145: 50-60.
    • (1981) J Bacteriol , vol.145 , pp. 50-60
    • De Boer, W.R.1    Kruyssen, F.J.2    Wouters, J.T.M.3
  • 8
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg, D. (1984) Three-dimensional structure of membrane and surface proteins. Annu Rev Biochem 53: 595-623.
    • (1984) Annu Rev Biochem , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 9
    • 0028173341 scopus 로고
    • Molecular structures of penicillin-binding proteins and ß-lactamases
    • Ghuysen, J.M. (1994) Molecular structures of penicillin-binding proteins and ß-lactamases. Trends Microbiol 2: 372-380.
    • (1994) Trends Microbiol , vol.2 , pp. 372-380
    • Ghuysen, J.M.1
  • 11
    • 0024963567 scopus 로고
    • Signal sequences
    • Gierash, L.M. (1989) Signal sequences. Biochemistry 28: 923-930.
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierash, L.M.1
  • 12
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. (1992) Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J Mol Biol 225: 487-494.
    • (1992) J Mol Biol , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 13
    • 0025681503 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne, G., and Manoil, C. (1990) Membrane proteins: from sequence to structure. Protein Eng 4: 109-112.
    • (1990) Protein Eng , vol.4 , pp. 109-112
    • Von Heijne, G.1    Manoil, C.2
  • 14
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction
    • Jacobs, C., Huang, L., Bartowsky, E., Normark, S., and Park, J.T. (1994) Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction. EMBO J 13: 4684-4694.
    • (1994) EMBO J , vol.13 , pp. 4684-4694
    • Jacobs, C.1    Huang, L.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 15
    • 0028986826 scopus 로고
    • AmpD, essential for both β-lactamase regulation and cell wall recycling, is a novel cytosolic N-acetylmuramyl-L-alanine amidase
    • Jacobs, C., Joris, B., Jamin, M., van Beeumen, J., van Heijenoort, J., Park, J.T., Normark, S., and Frère, J.M. (1995) AmpD, essential for both β-lactamase regulation and cell wall recycling, is a novel cytosolic N-acetylmuramyl-L-alanine amidase. Mol Microbiol 15: 553-559.
    • (1995) Mol Microbiol , vol.15 , pp. 553-559
    • Jacobs, C.1    Joris, B.2    Jamin, M.3    Van Beeumen, J.4    Van Heijenoort, J.5    Park, J.T.6    Normark, S.7    Frère, J.M.8
  • 17
    • 77957222923 scopus 로고
    • Induction of ßlactamase and low-affinity penicillin-binding protein 2′ synthesis in Gram-positive bacteria
    • Joris, B., Hardt, K., and Ghuysen, J.M. (1994) Induction of ßlactamase and low-affinity penicillin-binding protein 2′ synthesis in Gram-positive bacteria. New Comprehensive Biochem 27: 505-515.
    • (1994) New Comprehensive Biochem , vol.27 , pp. 505-515
    • Joris, B.1    Hardt, K.2    Ghuysen, J.M.3
  • 18
    • 0023232314 scopus 로고
    • A second regulatory gene, blaR1, encoding a potential penicillin-binding protein required for induction of β-lactamase in Bacillus licheniformis
    • Kobayashi, T., Zhu, Y.F., Nicholls, N., and Lampen, J.O. (1987) A second regulatory gene, blaR1, encoding a potential penicillin-binding protein required for induction of β-lactamase in Bacillus licheniformis. J Bacteriol 169: 3873-3878.
    • (1987) J Bacteriol , vol.169 , pp. 3873-3878
    • Kobayashi, T.1    Zhu, Y.F.2    Nicholls, N.3    Lampen, J.O.4
  • 19
    • 0014702482 scopus 로고
    • Resistance of Escherichia coli to penicillins
    • Lindström, E.B., Boman, H.G., and Steele, B.B. (1970) Resistance of Escherichia coli to penicillins. J Bacteriol 101:218-231.
    • (1970) J Bacteriol , vol.101 , pp. 218-231
    • Lindström, E.B.1    Boman, H.G.2    Steele, B.B.3
  • 20
    • 0025872118 scopus 로고
    • Disulfide crosslinking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli
    • Lynch, B.A., and Koshland, D.E. (1991) Disulfide crosslinking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli. Proc Natl Acad Sci USA 88: 10741-10410.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10741-110410
    • Lynch, B.A.1    Koshland, D.E.2
  • 21
    • 0029787789 scopus 로고    scopus 로고
    • Identification of the mp/gene encoding UDP-N-acetylmuramate: L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan
    • Mengin-Lecreulx, D., van Heijenoort, J., and Park, J.T. (1996) Identification of the mp/gene encoding UDP-N-acetylmuramate: L-alanyl-γ-D-glutamyl-meso-diaminopimelate ligase in Escherichia coli and its role in recycling of cell wall peptidoglycan. J Bacteriol 178: 5347-5352.
    • (1996) J Bacteriol , vol.178 , pp. 5347-5352
    • Mengin-Lecreulx, D.1    Van Heijenoort, J.2    Park, J.T.3
  • 22
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn, M.V., Privé, G.G., Milligan, D.L., Scott, W.G., Yeh, J., Jancarik, J., Koshland, D.E., Jr, and Kim, S.-H. (1991) Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254: 1342-1347.
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Privé, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5    Jancarik, J.6    Koshland Jr., D.E.7    Kim, S.-H.8
  • 23
    • 0015327122 scopus 로고
    • Novel method for detection of β-lactamase by using a chromogenic cephalosporin substrate
    • O'Callaghan, C.H., Morris, A., Kirby, S.M., and Shingler, A.M. (1972) Novel method for detection of β-lactamase by using a chromogenic cephalosporin substrate. Antimicrob Ag Chemother 1:283-288.
    • (1972) Antimicrob Ag Chemother , vol.1 , pp. 283-288
    • O'Callaghan, C.H.1    Morris, A.2    Kirby, S.M.3    Shingler, A.M.4
  • 24
    • 0029738191 scopus 로고    scopus 로고
    • The convergence of murein recycling research with β-lactamase research
    • Park, J.T. (1996) The convergence of murein recycling research with β-lactamase research. Microb Drug Resistance 2: 105-112.
    • (1996) Microb Drug Resistance , vol.2 , pp. 105-112
    • Park, J.T.1
  • 25
    • 0003869089 scopus 로고
    • B. licheniformis protoplast transformation
    • Harwood, C.R., and Cutting, S. (eds). New York: John Wiley
    • Quax, W. (1990) B. licheniformis protoplast transformation. In Molecular Biological Methods for Bacillus. Harwood, C.R., and Cutting, S. (eds). New York: John Wiley, pp. 152-153.
    • (1990) Molecular Biological Methods for Bacillus , pp. 152-153
    • Quax, W.1
  • 27
    • 8044256924 scopus 로고
    • Transmembrane signal transducing proteins
    • Surette, M.G., and Stock, J.B. (1994) Transmembrane signal transducing proteins. New Comprehensive Biochem 27: 465-483.
    • (1994) New Comprehensive Biochem , vol.27 , pp. 465-483
    • Surette, M.G.1    Stock, J.B.2
  • 28
    • 0027299392 scopus 로고
    • Characterization of the membrane sensor PenJ for β-lactam antibiotics from Bacillus licheniformis by amino acid substitution
    • Takagi, M., Ohta, T., Johki, S., and Imanaka, T. (1993) Characterization of the membrane sensor PenJ for β-lactam antibiotics from Bacillus licheniformis by amino acid substitution. FEMS Microbiol Lett 110: 127-132.
    • (1993) FEMS Microbiol Lett , vol.110 , pp. 127-132
    • Takagi, M.1    Ohta, T.2    Johki, S.3    Imanaka, T.4
  • 30
    • 0027015628 scopus 로고
    • Functional zinc-binding motifs in enzymes and DNA-binding proteins
    • Vallee, B.L., and Auld, D.S. (1992) Functional zinc-binding motifs in enzymes and DNA-binding proteins. Faraday Discuss 93: 47-65.
    • (1992) Faraday Discuss , vol.93 , pp. 47-65
    • Vallee, B.L.1    Auld, D.S.2
  • 31
    • 0025020692 scopus 로고
    • Identification of BIaR, the signal transducer for β-lactamase production in Bacillus licheniformis, as a penicillin-binding protein with strong homology to the OXA-2 β-lactamase (class D) of Salmonella typhimurium
    • Zhu, Y.F., Curran, I.H.A., Joris, B., Ghuysen, J.M., and Lampen, J.O. (1990) Identification of BIaR, the signal transducer for β-lactamase production in Bacillus licheniformis, as a penicillin-binding protein with strong homology to the OXA-2 β-lactamase (class D) of Salmonella typhimurium. J Bacteriol 172: 1137-1141.
    • (1990) J Bacteriol , vol.172 , pp. 1137-1141
    • Zhu, Y.F.1    Curran, I.H.A.2    Joris, B.3    Ghuysen, J.M.4    Lampen, J.O.5
  • 32
    • 0026669936 scopus 로고
    • Structure, function, and fate of the BIaR signal transducer involved in induction of β-lactamase in Bacillus licheniformis
    • Zhu, Y.F., Englebert, S., Joris, B., Ghuysen, J.M., Kobayashi, T., and Lampen, J.O. (1992) Structure, function, and fate of the BIaR signal transducer involved in induction of β-lactamase in Bacillus licheniformis. J Bacteriol 174: 6171-6178.
    • (1992) J Bacteriol , vol.174 , pp. 6171-6178
    • Zhu, Y.F.1    Englebert, S.2    Joris, B.3    Ghuysen, J.M.4    Kobayashi, T.5    Lampen, J.O.6


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