메뉴 건너뛰기




Volumn 289, Issue 47, 2014, Pages 32571-32582

The CpxR/CpxA Two-component regulatory system up-regulates the multidrug resistance cascade to facilitate Escherichia coli resistance to a model antimicrobial peptide

Author keywords

[No Author keywords available]

Indexed keywords

CASCADE CONTROL SYSTEMS; MICROORGANISMS; PEPTIDES; POLYPEPTIDES;

EID: 84911919911     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.565762     Document Type: Article
Times cited : (91)

References (47)
  • 1
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • Raivio, T. L. (2005) Envelope stress responses and Gram-negative bacterial pathogenesis. Mol. Microbiol. 56, 1119-1128
    • (2005) Mol. Microbiol. , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 2
    • 70349684496 scopus 로고    scopus 로고
    • OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA twocomponent system
    • Ma, Q., and Wood, T. K. (2009) OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA twocomponent system. Environ. Microbiol. 11, 2735-2746
    • (2009) Environ. Microbiol. , vol.11 , pp. 2735-2746
    • Ma, Q.1    Wood, T.K.2
  • 3
    • 0032728835 scopus 로고    scopus 로고
    • The CpxRA signal transduction system of Escherichia coli: Growth-related autoactivation and control of unanticipated target operons
    • De Wulf, P., Kwon, O., and Lin, E. C. (1999) The CpxRA signal transduction system of Escherichia coli: Growth-related autoactivation and control of unanticipated target operons. J. Bacteriol. 181, 6772-6778
    • (1999) J. Bacteriol. , vol.181 , pp. 6772-6778
    • De Wulf, P.1    Kwon, O.2    Lin, E.C.3
  • 4
    • 79953157864 scopus 로고    scopus 로고
    • The CpxR/CpxA two-component system up-regulates two Tat-dependent peptidoglycan amidases to confer bacterial resistance to antimicrobial peptide
    • Weatherspoon-Griffin, N., Zhao, G., Kong, W., Kong, Y., Morigen, Andrews-Polymenis, H., McClelland, M., and Shi, Y. (2011) The CpxR/CpxA two-component system up-regulates two Tat-dependent peptidoglycan amidases to confer bacterial resistance to antimicrobial peptide. J. Biol. Chem. 286, 5529-5539
    • (2011) J. Biol. Chem. , vol.286 , pp. 5529-5539
    • Weatherspoon-Griffin, N.1    Zhao, G.2    Kong, W.3    Kong, Y.4    Morigen Andrews-Polymenis, H.5    McClelland, M.6    Shi, Y.7
  • 5
    • 0037336180 scopus 로고    scopus 로고
    • Comprehensive studies of drug resistance mediated by overexpression of response regulators of two-component signal transduction systems in Escherichia coli
    • Hirakawa, H., Nishino, K., Hirata, T., and Yamaguchi, A. (2003) Comprehensive studies of drug resistance mediated by overexpression of response regulators of two-component signal transduction systems in Escherichia coli. J. Bacteriol. 185, 1851-1856
    • (2003) J. Bacteriol. , vol.185 , pp. 1851-1856
    • Hirakawa, H.1    Nishino, K.2    Hirata, T.3    Yamaguchi, A.4
  • 7
    • 84876187408 scopus 로고    scopus 로고
    • The Cpx stress response confers resistance to some, but not all, bactericidal antibiotics
    • Mahoney, T. F., and Silhavy, T. J. (2013) The Cpx stress response confers resistance to some, but not all, bactericidal antibiotics. J. Bacteriol. 195, 1869-1874
    • (2013) J. Bacteriol. , vol.195 , pp. 1869-1874
    • Mahoney, T.F.1    Silhavy, T.J.2
  • 8
    • 0032844440 scopus 로고    scopus 로고
    • The mar regulon: Multiple resistance to antibiotics and other toxic chemicals
    • Alekshun, M. N., and Levy, S. B. (1999) The mar regulon: Multiple resistance to antibiotics and other toxic chemicals. Trends Microbiol. 7, 410-413
    • (1999) Trends Microbiol. , vol.7 , pp. 410-413
    • Alekshun, M.N.1    Levy, S.B.2
  • 9
    • 0029025536 scopus 로고
    • Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli
    • Seoane, A. S., and Levy, S. B. (1995) Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli. J. Bacteriol. 177, 3414-3419
    • (1995) J. Bacteriol. , vol.177 , pp. 3414-3419
    • Seoane, A.S.1    Levy, S.B.2
  • 11
    • 0029295437 scopus 로고
    • The MarR repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli: Prototypic member of a family of bacterial regulatory proteins involved in sensing phenolic compounds
    • Sulavik, M. C., Gambino, L. F., and Miller, P. F. (1995) The MarR repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli: Prototypic member of a family of bacterial regulatory proteins involved in sensing phenolic compounds. Mol Med 1, 436-446
    • (1995) Mol Med , vol.1 , pp. 436-446
    • Sulavik, M.C.1    Gambino, L.F.2    Miller, P.F.3
  • 12
    • 0036084082 scopus 로고    scopus 로고
    • The multiple antibiotic resistance (mar) locus and its significance
    • Randall, L. P., and Woodward, M. J. (2002) The multiple antibiotic resistance (mar) locus and its significance. Res. Vet. Sci. 72, 87-93
    • (2002) Res. Vet. Sci. , vol.72 , pp. 87-93
    • Randall, L.P.1    Woodward, M.J.2
  • 13
    • 0026095607 scopus 로고
    • MarA, a regulated locus which controls expression of chromosomal multiple antibiotic resistance in Escherichia coli
    • Hächler, H., Cohen, S. P., and Levy, S. B. (1991) marA, a regulated locus which controls expression of chromosomal multiple antibiotic resistance in Escherichia coli. J. Bacteriol. 173, 5532-5538
    • (1991) J. Bacteriol. , vol.173 , pp. 5532-5538
    • Hächler, H.1    Cohen, S.P.2    Levy, S.B.3
  • 14
    • 0032746803 scopus 로고    scopus 로고
    • Structural requirements for marbox function in transcriptional activation of mar/sox/rob regulon promoters in Escherichia coli: Sequence, orientation and spatial relationship to the core promoter
    • Martin, R. G., Gillette, W. K., Rhee, S., and Rosner, J. L. (1999) Structural requirements for marbox function in transcriptional activation of mar/sox/rob regulon promoters in Escherichia coli: Sequence, orientation and spatial relationship to the core promoter. Mol. Microbiol. 34, 431-441
    • (1999) Mol. Microbiol. , vol.34 , pp. 431-441
    • Martin, R.G.1    Gillette, W.K.2    Rhee, S.3    Rosner, J.L.4
  • 15
    • 0037898916 scopus 로고    scopus 로고
    • Bile salts and fatty acids induce the expression of Escherichia coli AcrAB multidrug efflux pump through their interaction with Rob regulatory protein
    • Rosenberg, E. Y., Bertenthal, D., Nilles, M. L., Bertrand, K. P., and Nikaido, H. (2003) Bile salts and fatty acids induce the expression of Escherichia coli AcrAB multidrug efflux pump through their interaction with Rob regulatory protein. Mol. Microbiol. 48, 1609-1619
    • (2003) Mol. Microbiol. , vol.48 , pp. 1609-1619
    • Rosenberg, E.Y.1    Bertenthal, D.2    Nilles, M.L.3    Bertrand, K.P.4    Nikaido, H.5
  • 16
    • 0030004590 scopus 로고    scopus 로고
    • Autoactivation of the marRAB multiple antibiotic resistance operon by the MarA transcriptional activator in Escherichia coli
    • Martin, R. G., Jair, K. W., Wolf, R. E., Jr., and Rosner, J. L. (1996) Autoactivation of the marRAB multiple antibiotic resistance operon by the MarA transcriptional activator in Escherichia coli. J. Bacteriol. 178, 2216-2223
    • (1996) J. Bacteriol. , vol.178 , pp. 2216-2223
    • Martin, R.G.1    Jair, K.W.2    Wolf, R.E.3    Rosner, J.L.4
  • 17
    • 0027937658 scopus 로고
    • Genetic relationship between soxRS and mar loci in promoting multiple antibiotic resistance in Escherichia coli
    • Miller, P. F., Gambino, L. F., Sulavik, M. C., and Gracheck, S. J. (1994) Genetic relationship between soxRS and mar loci in promoting multiple antibiotic resistance in Escherichia coli. Antimicrob. Agents Chemother. 38, 1773-1779
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1773-1779
    • Miller, P.F.1    Gambino, L.F.2    Sulavik, M.C.3    Gracheck, S.J.4
  • 18
    • 0029079304 scopus 로고
    • Binding of purified multiple antibiotic-resistance repressor protein (MarR) to mar operator sequences
    • Martin, R. G., and Rosner, J. L. (1995) Binding of purified multiple antibiotic-resistance repressor protein (MarR) to mar operator sequences. Proc. Natl. Acad. Sci. U.S.A. 92, 5456-5460
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5456-5460
    • Martin, R.G.1    Rosner, J.L.2
  • 19
    • 76449106786 scopus 로고    scopus 로고
    • Different effects of transcriptional regulators MarA, SoxS and Rob on susceptibility of Escherichia coli to cationic antimicrobial peptides (CAMPs): Rob-dependent CAMP induction of the marRAB operon
    • Warner, D. M., and Levy, S. B. (2010) Different effects of transcriptional regulators MarA, SoxS and Rob on susceptibility of Escherichia coli to cationic antimicrobial peptides (CAMPs): Rob-dependent CAMP induction of the marRAB operon. Microbiology 156, 570-578
    • (2010) Microbiology , vol.156 , pp. 570-578
    • Warner, D.M.1    Levy, S.B.2
  • 22
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and Wanner, B. L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U.S.A. 97, 6640-6645
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 23
    • 0037094370 scopus 로고    scopus 로고
    • Construction of targeted single copy lac fusions using lambda Red and FLP-mediated site-specific recombination in bacteria
    • Ellermeier, C. D., Janakiraman, A., and Slauch, J. M. (2002) Construction of targeted single copy lac fusions using lambda Red and FLP-mediated site-specific recombination in bacteria. Gene 290, 153-161
    • (2002) Gene , vol.290 , pp. 153-161
    • Ellermeier, C.D.1    Janakiraman, A.2    Slauch, J.M.3
  • 24
    • 0029116605 scopus 로고
    • Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon
    • Soncini, F. C., Véscovi, E. G., and Groisman, E. A. (1995) Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon. J. Bacteriol. 177, 4364-4371
    • (1995) J. Bacteriol. , vol.177 , pp. 4364-4371
    • Soncini, F.C.1    Véscovi, E.G.2    Groisman, E.A.3
  • 25
    • 33646007627 scopus 로고    scopus 로고
    • AnRNAsensor for intracellular Mg2+
    • Cromie, M. J., Shi, Y., Latifi, T., and Groisman, E. A. (2006) AnRNAsensor for intracellular Mg2+. Cell 125, 71-84
    • (2006) Cell , vol.125 , pp. 71-84
    • Cromie, M.J.1    Shi, Y.2    Latifi, T.3    Groisman, E.A.4
  • 26
    • 0015869217 scopus 로고
    • Protamines. Isolation, characterization, structure and function
    • Ando, T., Yamasaki, M., and Suzuki, K. (1973) Protamines. Isolation, characterization, structure and function. Mol. Biol. Biochem. Biophys. 12, 1-114
    • (1973) Mol. Biol. Biochem. Biophys. , vol.12 , pp. 1-114
    • Ando, T.1    Yamasaki, M.2    Suzuki, K.3
  • 27
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Miller, J. H. (1972) Experiments in Molecular Genetics, pp. 352-355, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 28
    • 0037447083 scopus 로고    scopus 로고
    • Closing the loop: The PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD
    • Kato, A., Latifi, T., and Groisman, E. A. (2003) Closing the loop: The PmrA/PmrB two-component system negatively controls expression of its posttranscriptional activator PmrD. Proc. Natl. Acad. Sci. U.S.A. 100, 4706-4711
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4706-4711
    • Kato, A.1    Latifi, T.2    Groisman, E.A.3
  • 29
    • 0037135593 scopus 로고    scopus 로고
    • Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli
    • De Wulf, P., McGuire, A. M., Liu, X., and Lin, E. C. (2002) Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli. J. Biol. Chem. 277, 26652-26661
    • (2002) J. Biol. Chem. , vol.277 , pp. 26652-26661
    • De Wulf, P.1    McGuire, A.M.2    Liu, X.3    Lin, E.C.4
  • 31
    • 63049096052 scopus 로고    scopus 로고
    • Characterization of the Cpx regulon in Escherichia coli strain MC4100
    • Price, N. L., and Raivio, T. L. (2009) Characterization of the Cpx regulon in Escherichia coli strain MC4100. J. Bacteriol. 191, 1798-1815
    • (2009) J. Bacteriol. , vol.191 , pp. 1798-1815
    • Price, N.L.1    Raivio, T.L.2
  • 32
    • 84872012492 scopus 로고    scopus 로고
    • Multiple envelope stress response pathways are activated in an Escherichia coli strain with mutations in two members of the DedA membrane protein family
    • Sikdar, R., Simmons, A. R., and Doerrler, W. T. (2013) Multiple envelope stress response pathways are activated in an Escherichia coli strain with mutations in two members of the DedA membrane protein family. J. Bacteriol. 195, 12-24
    • (2013) J. Bacteriol. , vol.195 , pp. 12-24
    • Sikdar, R.1    Simmons, A.R.2    Doerrler, W.T.3
  • 33
    • 3142592449 scopus 로고    scopus 로고
    • PhoP-regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B
    • Shi, Y., Cromie, M. J., Hsu, F. F., Turk, J., and Groisman, E. A. (2004) PhoP-regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B. Mol. Microbiol. 53, 229-241
    • (2004) Mol. Microbiol. , vol.53 , pp. 229-241
    • Shi, Y.1    Cromie, M.J.2    Hsu, F.F.3    Turk, J.4    Groisman, E.A.5
  • 34
    • 7644244749 scopus 로고    scopus 로고
    • Genetic evidence for functional interactions between TolC and AcrA proteins of a major antibiotic efflux pump of Escherichia coli
    • Gerken, H., and Misra, R. (2004) Genetic evidence for functional interactions between TolC and AcrA proteins of a major antibiotic efflux pump of Escherichia coli. Mol. Microbiol. 54, 620-631
    • (2004) Mol. Microbiol. , vol.54 , pp. 620-631
    • Gerken, H.1    Misra, R.2
  • 35
    • 3943108216 scopus 로고    scopus 로고
    • Structure and function of TolC: The bacterial exit duct for proteins and drugs
    • Koronakis, V., Eswaran, J., and Hughes, C. (2004) Structure and function of TolC: The bacterial exit duct for proteins and drugs. Annu. Rev. Biochem. 73, 467-489
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 467-489
    • Koronakis, V.1    Eswaran, J.2    Hughes, C.3
  • 36
    • 57349141498 scopus 로고    scopus 로고
    • MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II
    • Yamanaka, H., Kobayashi, H., Takahashi, E., and Okamoto, K. (2008) MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II. J. Bacteriol. 190, 7693-7698
    • (2008) J. Bacteriol. , vol.190 , pp. 7693-7698
    • Yamanaka, H.1    Kobayashi, H.2    Takahashi, E.3    Okamoto, K.4
  • 37
    • 76449101997 scopus 로고    scopus 로고
    • Involvement and necessity of the Cpx regulon in the event of aberrant -barrel outer membrane protein assembly
    • Gerken, H., Leiser, O. P., Bennion, D., and Misra, R. (2010) Involvement and necessity of the Cpx regulon in the event of aberrant -barrel outer membrane protein assembly. Mol. Microbiol. 75, 1033-1046
    • (2010) Mol. Microbiol. , vol.75 , pp. 1033-1046
    • Gerken, H.1    Leiser, O.P.2    Bennion, D.3    Misra, R.4
  • 38
    • 1842477219 scopus 로고    scopus 로고
    • In vivo substrate specificity of periplasmic disulfide oxidoreductases
    • Hiniker, A., and Bardwell, J. (2004) In vivo substrate specificity of periplasmic disulfide oxidoreductases. J. Biol. Chem. 279, 12967-12973
    • (2004) J. Biol. Chem. , vol.279 , pp. 12967-12973
    • Hiniker, A.1    Bardwell, J.2
  • 39
    • 84873552933 scopus 로고    scopus 로고
    • Reduction of cellular stress by TolC-dependent efflux pumps in Escherichia coli indicated by BaeSR and CpxARP activation of spy in efflux mutants
    • Rosner, J. L., and Martin, R. G. (2013) Reduction of cellular stress by TolC-dependent efflux pumps in Escherichia coli indicated by BaeSR and CpxARP activation of spy in efflux mutants. J. Bacteriol. 195, 1042-1050
    • (2013) J. Bacteriol. , vol.195 , pp. 1042-1050
    • Rosner, J.L.1    Martin, R.G.2
  • 40
    • 77956528494 scopus 로고    scopus 로고
    • Aromatic acid metabolites of Escherichia coli K-12 can induce the marRAB operon
    • Chubiz, L. M., and Rao, C. V. (2010) Aromatic acid metabolites of Escherichia coli K-12 can induce the marRAB operon. J. Bacteriol. 192, 4786-4789
    • (2010) J. Bacteriol. , vol.192 , pp. 4786-4789
    • Chubiz, L.M.1    Rao, C.V.2
  • 41
    • 14544286364 scopus 로고    scopus 로고
    • Indole induces the expression of multidrug exporter genes in Escherichia coli
    • Hirakawa, H., Inazumi, Y., Masaki, T., Hirata, T., and Yamaguchi, A. (2005) Indole induces the expression of multidrug exporter genes in Escherichia coli. Mol. Microbiol. 55, 1113-1126
    • (2005) Mol. Microbiol. , vol.55 , pp. 1113-1126
    • Hirakawa, H.1    Inazumi, Y.2    Masaki, T.3    Hirata, T.4    Yamaguchi, A.5
  • 42
    • 0028951033 scopus 로고
    • The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP
    • Danese, P. N., Snyder, W. B., Cosma, C. L., Davis, L. J., and Silhavy, T. J. (1995) The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP. Genes Dev. 9, 387-398
    • (1995) Genes Dev. , vol.9 , pp. 387-398
    • Danese, P.N.1    Snyder, W.B.2    Cosma, C.L.3    Davis, L.J.4    Silhavy, T.J.5
  • 43
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • Danese, P. N., and Silhavy, T. J. (1998) CpxP, a stress-combative member of the Cpx regulon. J. Bacteriol. 180, 831-839
    • (1998) J. Bacteriol. , vol.180 , pp. 831-839
    • Danese, P.N.1    Silhavy, T.J.2
  • 44
    • 0032869034 scopus 로고    scopus 로고
    • Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12: Identification of extracellular Mg2+-responsive promoters
    • Kato, A., Tanabe, H., and Utsumi, R. (1999) Molecular characterization of the PhoP-PhoQ two-component system in Escherichia coli K-12: Identification of extracellular Mg2+-responsive promoters. J. Bacteriol. 181, 5516-5520
    • (1999) J. Bacteriol. , vol.181 , pp. 5516-5520
    • Kato, A.1    Tanabe, H.2    Utsumi, R.3
  • 45
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman, M. R., and Yount, N. Y. (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55, 27-55
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 46
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden, K. A. (2005) Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3, 238-250
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 47
    • 0028983261 scopus 로고
    • Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway
    • Snyder, W. B., Davis, L. J., Danese, P. N., Cosma, C. L., and Silhavy, T. J. (1995) Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway. J. Bacteriol. 177, 4216-4223
    • (1995) J. Bacteriol. , vol.177 , pp. 4216-4223
    • Snyder, W.B.1    Davis, L.J.2    Danese, P.N.3    Cosma, C.L.4    Silhavy, T.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.