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Volumn 181, Issue 16, 1999, Pages 4842-4847

The periplasmic murein peptide-binding protein MppA is a negative regulator of multiple antibiotic resistance in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BINDING PROTEIN; CEFOXITIN; CYCLOHEXANE; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN; PEPTIDOGLYCAN; PROTEIN MPPA; TETRACYCLINE; TRIPEPTIDE; UNCLASSIFIED DRUG;

EID: 0032839003     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.16.4842-4847.1999     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 0000148162 scopus 로고    scopus 로고
    • Regulation of chromosomally mediated multiple antibiotic resistance: The mar regulon
    • Alekshun, M. N., and S. B. Levy. 1997. Regulation of chromosomally mediated multiple antibiotic resistance: the mar regulon. Antimicrob. Agents and Chemother. 41:2067-2075.
    • (1997) Antimicrob. Agents and Chemother , vol.41 , pp. 2067-2075
    • Alekshun, M.N.1    Levy, S.B.2
  • 2
    • 0027419613 scopus 로고
    • Genetic and functional analysis of the multiple antibiotic resistance (mar) locus in Escherichia coli
    • Cohen, S. P., H. Hachler, and S. B. Levy. 1993. Genetic and functional analysis of the multiple antibiotic resistance (mar) locus in Escherichia coli. J. Bacteriol. 175:1484-1492.
    • (1993) J. Bacteriol. , vol.175 , pp. 1484-1492
    • Cohen, S.P.1    Hachler, H.2    Levy, S.B.3
  • 3
    • 0027131605 scopus 로고
    • Salicylate induction of antibiotic resistance in Escherichia coli: Activation of the mar operon and a mar-independent pathway
    • Cohen, S. P., S. B. Levy, J. Foulds, and J. L. Rosner. 1993. Salicylate induction of antibiotic resistance in Escherichia coli: activation of the mar operon and a mar-independent pathway. J. Bacteriol. 175:7856-7862.
    • (1993) J. Bacteriol. , vol.175 , pp. 7856-7862
    • Cohen, S.P.1    Levy, S.B.2    Foulds, J.3    Rosner, J.L.4
  • 4
    • 0024235788 scopus 로고
    • Mara locus causes decreased expression of OmpF porin in multiple-antibiotic-resistant (Mar) mutants of Escherichia coli
    • Cohen, S. P., L. M. McMurry, and S. B. Levy. 1988. marA locus causes decreased expression of OmpF porin in multiple-antibiotic-resistant (Mar) mutants of Escherichia coli. J. Bacteriol. 170:5416-5422.
    • (1988) J. Bacteriol. , vol.170 , pp. 5416-5422
    • Cohen, S.P.1    McMurry, L.M.2    Levy, S.B.3
  • 5
    • 0030470440 scopus 로고    scopus 로고
    • Isolation, over-expression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli
    • De Biase, D., A. Tramonti, R. A. John, and F. Rossa. 1996. Isolation, over-expression, and biochemical characterization of the two isoforms of glutamic acid decarboxylase from Escherichia coli. Protein Expr. Purif. 8:430-438.
    • (1996) Protein Expr. Purif. , vol.8 , pp. 430-438
    • De Biase, D.1    Tramonti, A.2    John, R.A.3    Rossa, F.4
  • 6
    • 0015854977 scopus 로고
    • Solubilization of the cytoplasmic membrane of Escherichia coli by ionic detergent sodium-lauryl sarcosinate
    • Filip, C., G. Fletcher, J. L. Wulff, and C. F. Earhart. 1973. Solubilization of the cytoplasmic membrane of Escherichia coli by ionic detergent sodium-lauryl sarcosinate. J. Bacteriol. 115:717-722.
    • (1973) J. Bacteriol. , vol.115 , pp. 717-722
    • Filip, C.1    Fletcher, G.2    Wulff, J.L.3    Earhart, C.F.4
  • 7
    • 0017891745 scopus 로고
    • New major outer membrane protein found in an Escherichia coli tolF mutant resistant to bacteriophage Tulb
    • Foulds, J., and T.-J. Chai. 1978. New major outer membrane protein found in an Escherichia coli tolF mutant resistant to bacteriophage Tulb. J. Bacteriol. 133:1478-1483.
    • (1978) J. Bacteriol. , vol.133 , pp. 1478-1483
    • Foulds, J.1    Chai, T.-J.2
  • 8
    • 0002116418 scopus 로고
    • The bacterial amino acid decarboxylases
    • Gale, E. F. 1946. The bacterial amino acid decarboxylases. Adv. Enzymol. 6:1-32.
    • (1946) Adv. Enzymol. , vol.6 , pp. 1-32
    • Gale, E.F.1
  • 9
    • 0027287346 scopus 로고
    • Overexpression of the MarA positive regulator is sufficient to confer multiple antibiotic resistance in Escherichia coli
    • Gambino, L., S. J. Gracheck, and P. F. Miller. 1993. Overexpression of the MarA positive regulator is sufficient to confer multiple antibiotic resistance in Escherichia coli. J. Bacteriol. 175:2888-2894.
    • (1993) J. Bacteriol. , vol.175 , pp. 2888-2894
    • Gambino, L.1    Gracheck, S.J.2    Miller, P.F.3
  • 10
    • 0020513997 scopus 로고
    • Amplifiable resistance to tetracycline, chloramphenicol, and other antibiotics in Escherichia coli: Involvement of a non-plasmid-determined efflux of tetracycline
    • George, A. M., and S. B. Levy. 1983. Amplifiable resistance to tetracycline, chloramphenicol, and other antibiotics in Escherichia coli: involvement of a non-plasmid-determined efflux of tetracycline. J. Bacteriol. 155:531-540.
    • (1983) J. Bacteriol. , vol.155 , pp. 531-540
    • George, A.M.1    Levy, S.B.2
  • 12
    • 0030977050 scopus 로고    scopus 로고
    • Exchange of glutamate and γ-aminobutyrate in a Lactobacillus strain
    • Higuchi, T., H. Hayashi, and K. Abe. 1997. Exchange of glutamate and γ-aminobutyrate in a Lactobacillus strain. J. Bacteriol. 179:3362-3364.
    • (1997) J. Bacteriol. , vol.179 , pp. 3362-3364
    • Higuchi, T.1    Hayashi, H.2    Abe, K.3
  • 13
    • 0022762079 scopus 로고
    • Peptide uptake by Salmonella typhimurium: The periplasmic binding protein
    • Hiles, I. D., and C. F. Higgins. 1986. Peptide uptake by Salmonella typhimurium: the periplasmic binding protein. Eur. J. Biochem. 158:561-567.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 561-567
    • Hiles, I.D.1    Higgins, C.F.2
  • 14
    • 0028168986 scopus 로고
    • The negative regulator of β-lactamase induction ampd is a N-acetyl-anhydromuramyl-L-alanine amidase
    • Höltje, J.-V., U. Kopp, A. Ursinus, and B. Wiedemann. 1994. The negative regulator of β-lactamase induction AmpD is a N-acetyl-anhydromuramyl-L-alanine amidase. FEMS Microbiol. Lett. 122:159-164.
    • (1994) FEMS Microbiol. Lett. , vol.122 , pp. 159-164
    • Höltje, J.-V.1    Kopp, U.2    Ursinus, A.3    Wiedemann, B.4
  • 15
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for β-lactamase induction
    • Jacobs, C., L.-J. Huang, E. Bartowsky, S. Normark, and J. T. Park. 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.-J.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 17
    • 0028040011 scopus 로고
    • New outer membrane-associated protease of Escherichia coli K-12
    • Kaufmann, A., Y.-D. Stierhof, and U. Henning. 1994. New outer membrane-associated protease of Escherichia coli K-12. J. Bacteriol. 176:359-367.
    • (1994) J. Bacteriol. , vol.176 , pp. 359-367
    • Kaufmann, A.1    Stierhof, Y.-D.2    Henning, U.3
  • 18
    • 0024469170 scopus 로고
    • AmpG is essential for high-level expression of AmpC β-lactamase in Enterobacter cloacae
    • Korfmann, G., and C. C. Sanders. 1989. AmpG is essential for high-level expression of AmpC β-lactamase in Enterobacter cloacae. Antimicrob. Agents Chemother. 33:1946-1951.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1946-1951
    • Korfmann, G.1    Sanders, C.C.2
  • 19
    • 0024844958 scopus 로고
    • Isolation, cloning, and primary structure of a cationic 16kDa outer membrane protein of Salmonella typhimurium
    • Koski, P., M. Rhen, J. Kantele, and M. Vaara. 1989. Isolation, cloning, and primary structure of a cationic 16kDa outer membrane protein of Salmonella typhimurium. J. Biol. Chem. 264:18973-18980.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18973-18980
    • Koski, P.1    Rhen, M.2    Kantele, J.3    Vaara, M.4
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0028926676 scopus 로고
    • Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli
    • Ma, D., D. N. Cook, M. Alberti, N. G. Pon, H. Nikaido, and J. E. Hearst. 1995. Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli. Mol. Microbiol. 16:45-55.
    • (1995) Mol. Microbiol. , vol.16 , pp. 45-55
    • Ma, D.1    Cook, D.N.2    Alberti, M.3    Pon, N.G.4    Nikaido, H.5    Hearst, J.E.6
  • 22
    • 0030023489 scopus 로고    scopus 로고
    • The local repressor AcrR plays a modulating role in the regulation of acrAB genes of Escherichia coli by global stress signals
    • Ma, D., M. Alberti, C. Lynch, H. Nikaido, and J. E. Hearst. 1996. The local repressor AcrR plays a modulating role in the regulation of acrAB genes of Escherichia coli by global stress signals. Mol. Microbiol. 19:101-112.
    • (1996) Mol. Microbiol. , vol.19 , pp. 101-112
    • Ma, D.1    Alberti, M.2    Lynch, C.3    Nikaido, H.4    Hearst, J.E.5
  • 23
    • 0030004341 scopus 로고    scopus 로고
    • Identification of mar mutants among quinolone-resistant clinical isolates of Escherichia coli
    • Maneewannakul, K., and S. B. Levy. 1996. Identification of mar mutants among quinolone-resistant clinical isolates of Escherichia coli. Antimicrob. Agents Chemother. 40:1695-1698.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 1695-1698
    • Maneewannakul, K.1    Levy, S.B.2
  • 24
    • 0029079304 scopus 로고
    • Binding of purified multiple antibiotic-resistance repressor protein (MarR) to mar operator sequences
    • Martin, R. G., and J. L. Rosner. 1995. Binding of purified multiple antibiotic-resistance repressor protein (MarR) to mar operator sequences. Proc. Natl. Acad. Sci. USA 92:5456-5460.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5456-5460
    • Martin, R.G.1    Rosner, J.L.2
  • 25
    • 0023432172 scopus 로고
    • Role of micF in tolC-mediated regulation of OmpF, a major outer membrane protein of Escherichia coli K-12
    • Mirsa, R., and P. R. Reeves. 1987. Role of micF in tolC-mediated regulation of OmpF, a major outer membrane protein of Escherichia coli K-12. J. Bacteriol. 169:4722-4730.
    • (1987) J. Bacteriol. , vol.169 , pp. 4722-4730
    • Mirsa, R.1    Reeves, P.R.2
  • 26
    • 0344363037 scopus 로고
    • A unique mechanism regulating gene expression: Translational inhibition by a complementary RNA transcript (micRNA)
    • Mizuno, T., M. Chou, and M. Inouye. 1984. A unique mechanism regulating gene expression: translational inhibition by a complementary RNA transcript (micRNA). Proc. Natl. Acad. Sci. USA 81:1966-1970.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1966-1970
    • Mizuno, T.1    Chou, M.2    Inouye, M.3
  • 27
    • 0030029513 scopus 로고    scopus 로고
    • AcrAB efflux pump plays a major role in the antibiotic resistance phenotype of Escherichia coli multiple-antibiotic-resistance (Mar) mutants
    • Okusu, H., D. Ma, and H. Nikaido. 1996. AcrAB efflux pump plays a major role in the antibiotic resistance phenotype of Escherichia coli multiple-antibiotic-resistance (Mar) mutants. J. Bacteriol. 178:306-308.
    • (1996) J. Bacteriol. , vol.178 , pp. 306-308
    • Okusu, H.1    Ma, D.2    Nikaido, H.3
  • 28
    • 0027514558 scopus 로고
    • Turnover and recycling of the murein sacculus in oligopeptide permease-negative strains of Escherichia coli: Indirect evidence for an alternative permease system and for a monolayered sacculus
    • Park, J. T. 1993. Turnover and recycling of the murein sacculus in oligopeptide permease-negative strains of Escherichia coli: indirect evidence for an alternative permease system and for a monolayered sacculus. J. Bacteriol. 175:7-11.
    • (1993) J. Bacteriol. , vol.175 , pp. 7-11
    • Park, J.T.1
  • 29
    • 0031886481 scopus 로고    scopus 로고
    • MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-γ-D-glutamyl-meso-diaminopimelate
    • Park, J. T., D. RayChaudhuri, H. Li, S. Normark, and D. Mengin-LeCreulx. 1998. MppA, a periplasmic binding protein essential for import of the bacterial cell wall peptide L-alanyl-γ-D-glutamyl-meso-diaminopimelate. J. Bacteriol. 180:1215-1223.
    • (1998) J. Bacteriol. , vol.180 , pp. 1215-1223
    • Park, J.T.1    Raychaudhuri, D.2    Li, H.3    Normark, S.4    Mengin-LeCreulx, D.5
  • 30
    • 0032169864 scopus 로고    scopus 로고
    • A novel DNA-binding motif in MarA: The first structure for an AraC family transcriptional activator
    • Rhee, S., R. G. Martin, J. L. Rosner, and D. R. Davies. 1998. A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator. Proc. Natl. Acad. Sci. USA 95:10413-10418.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10413-10418
    • Rhee, S.1    Martin, R.G.2    Rosner, J.L.3    Davies, D.R.4
  • 33
    • 0029025536 scopus 로고
    • Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon of Escherichia coli
    • Seoane, A. S., and S. B. Levy. 1995. Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon of Escherichia coli. J. Bacteriol. 177:3414-3419.
    • (1995) J. Bacteriol. , vol.177 , pp. 3414-3419
    • Seoane, A.S.1    Levy, S.B.2
  • 34
    • 0026641173 scopus 로고
    • Escherichia coli has two homologous glutamate decarboxylase genes that map to distinct loci
    • Smith, D. K., T. Kassam, B. Singh, and J. F. Elliott. 1992. Escherichia coli has two homologous glutamate decarboxylase genes that map to distinct loci. J. Bacteriol. 174:5820-5826.
    • (1992) J. Bacteriol. , vol.174 , pp. 5820-5826
    • Smith, D.K.1    Kassam, T.2    Singh, B.3    Elliott, J.F.4
  • 35
    • 0025271478 scopus 로고
    • Signal transduction in bacteria
    • Stock, J. B., A. M. Stock, and J. M. Mottonen. 1990. Signal transduction in bacteria. Nature 344:395-400.
    • (1990) Nature , vol.344 , pp. 395-400
    • Stock, J.B.1    Stock, A.M.2    Mottonen, J.M.3
  • 36
    • 0030942395 scopus 로고    scopus 로고
    • The Salmonella typhimurium mar locus: Molecular and genetic analyses and assessment of its requirement for virulence
    • Sulavik, M. C., M. Dazer, and P. F. Miller. 1997. The Salmonella typhimurium mar locus: molecular and genetic analyses and assessment of its requirement for virulence. J. Bacteriol. 179:1857-1866.
    • (1997) J. Bacteriol. , vol.179 , pp. 1857-1866
    • Sulavik, M.C.1    Dazer, M.2    Miller, P.F.3
  • 37
    • 0020559318 scopus 로고
    • Mutation of the N-acetylmuramyl-L-alanine amidase gene of Escherichia coli K-12
    • Tomioka, S., T. Nikaido, T. Miyakawa, and M. Matsuhashi. 1983. Mutation of the N-acetylmuramyl-L-alanine amidase gene of Escherichia coli K-12. J. Bacteriol. 156:463-465.
    • (1983) J. Bacteriol. , vol.156 , pp. 463-465
    • Tomioka, S.1    Nikaido, T.2    Miyakawa, T.3    Matsuhashi, M.4
  • 38
    • 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
  • 39
    • 0030983818 scopus 로고    scopus 로고
    • Role of the acrAB locus in organic solvent tolerance mediated by expression of marA, soxS, or robA in Escherichia coli
    • White, D. G., J. D. Goldman, B. Demple, and S. B. Levy. 1997. Role of the acrAB locus in organic solvent tolerance mediated by expression of marA, soxS, or robA in Escherichia coli. J. Bacteriol. 179:6122-6126.
    • (1997) J. Bacteriol. , vol.179 , pp. 6122-6126
    • White, D.G.1    Goldman, J.D.2    Demple, B.3    Levy, S.B.4


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