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Volumn 11, Issue 9, 1997, Pages 1169-1182

Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system

Author keywords

Cpx; DegP; DsbA; protein folding; transcription

Indexed keywords

ENVELOPE PROTEIN;

EID: 0030992719     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.11.9.1169     Document Type: Article
Times cited : (250)

References (66)
  • 2
    • 0018873524 scopus 로고
    • Active oxygen species and the functions of phagocytic leukocytes
    • Badwey, J.A. and M.L. Karnovsky. 1980. Active oxygen species and the functions of phagocytic leukocytes. Annu. Rev. Biochem. 49: 695-726.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 695-726
    • Badwey, J.A.1    Karnovsky, M.L.2
  • 3
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C.A., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell 67: 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 5
    • 0028215784 scopus 로고
    • Salmonella typhimurium loci involved in survival within macrophages
    • Baumler, A.J., J.G. Kusters, I. Stojiljkovic, and F. Heffron. 1994. Salmonella typhimurium loci involved in survival within macrophages. Infect. Immun. 62: 1623-1630.
    • (1994) Infect. Immun. , vol.62 , pp. 1623-1630
    • Baumler, A.J.1    Kusters, J.G.2    Stojiljkovic, I.3    Heffron, F.4
  • 6
    • 0029693738 scopus 로고    scopus 로고
    • The preparation of riboprobes. Basic DNA and RNA protocols
    • Belin, D. 1996a. The preparation of riboprobes. Basic DNA and RNA protocols Methods Mol. Biol. 58: 83-91.
    • (1996) Methods Mol. Biol. , vol.58 , pp. 83-91
    • Belin, D.1
  • 7
    • 0029705357 scopus 로고    scopus 로고
    • The RNase protection assay. Basic DNA and RNA protocols
    • _. 1996b. The RNase protection assay. Basic DNA and RNA protocols. Methods Mol. Biol. 58: 131-136.
    • (1996) Methods Mol. Biol. , vol.58 , pp. 131-136
  • 8
    • 0018411579 scopus 로고
    • Temperature-sensitive mutation in the initiation codon of the rIIB gene of bacteriophage T4
    • Belin, D., J. Hedgpeth, G.B Selzer, and R.H. Epstein. 1979. Temperature-sensitive mutation in the initiation codon of the rIIB gene of bacteriophage T4. Proc. Natl. Acad. Sci. 76: 700-704.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 700-704
    • Belin, D.1    Hedgpeth, J.2    Selzer, G.B.3    Epstein, R.H.4
  • 9
    • 0028593831 scopus 로고
    • The Escherichia coli dsbA gene is partly transcribed from the promoter of a weakly expressed upstream gene
    • Belin, P. and P.L. Boquet. 1994. The Escherichia coli dsbA gene is partly transcribed from the promoter of a weakly expressed upstream gene. Microbiology 140: 3337-3348.
    • (1994) Microbiology , vol.140 , pp. 3337-3348
    • Belin, P.1    Boquet, P.L.2
  • 10
    • 0029111417 scopus 로고
    • A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery
    • Bost, S. and D. Belin. 1995. A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery. EMBO J. 14: 4412-4421.
    • (1995) EMBO J. , vol.14 , pp. 4412-4421
    • Bost, S.1    Belin, D.2
  • 11
    • 0030034915 scopus 로고    scopus 로고
    • Two distinct loci affecting conversion to mucoidy in Pseudomonas aeruginosa in cystic fibrosis encode homologs of the serine protease HtrA
    • Boucher, J.C., J. Martinez-Salazar, M.J. Schurr, M.H. Mudd, and V. Deretic. 1996. Two distinct loci affecting conversion to mucoidy in Pseudomonas aeruginosa in cystic fibrosis encode homologs of the serine protease HtrA. J. Bacteriol. 178: 511-523.
    • (1996) J. Bacteriol. , vol.178 , pp. 511-523
    • Boucher, J.C.1    Martinez-Salazar, J.2    Schurr, M.J.3    Mudd, M.H.4    Deretic, V.5
  • 12
    • 0028061282 scopus 로고
    • Promoter structure, promoter recognition, and transcription activation in prokaryotes
    • Busby, S. and R.H. Ebright. 1994. Promoter structure, promoter recognition, and transcription activation in prokaryotes. Cell 79: 743-746.
    • (1994) Cell , vol.79 , pp. 743-746
    • Busby, S.1    Ebright, R.H.2
  • 13
    • 0028326431 scopus 로고
    • Three-dimensional solution structure of Escherichia coli periplasmic cyclophiln
    • Clubb, R.T., S.B. Ferguson, C.T. Walsh, and G. Wagner. 1994. Three-dimensional solution structure of Escherichia coli periplasmic cyclophiln. Biochemistry 33: 2761-2772.
    • (1994) Biochemistry , vol.33 , pp. 2761-2772
    • Clubb, R.T.1    Ferguson, S.B.2    Walsh, C.T.3    Wagner, G.4
  • 14
    • 0029589618 scopus 로고
    • Mutational activation of the Cpx signal transduction pathway of Escherichia coli suppresses the toxicity conferred by certain envelope-associated stresses
    • Cosma, C.L., P.N. Danese, J.H. Carlson, T.J. Silhavy, and W.B. Snyder. 1995. Mutational activation of the Cpx signal transduction pathway of Escherichia coli suppresses the toxicity conferred by certain envelope-associated stresses. Mol. Microbiol. 18: 491-505.
    • (1995) Mol. Microbiol. , vol.18 , pp. 491-505
    • Cosma, C.L.1    Danese, P.N.2    Carlson, J.H.3    Silhavy, T.J.4    Snyder, W.B.5
  • 15
    • 0030998321 scopus 로고    scopus 로고
    • E and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • E and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli. Genes & Dev. (this issue).
    • (1997) Genes & Dev. , Issue.THIS ISSUE
    • Danese, P.N.1    Silhavy, T.J.2
  • 16
    • 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., W.B. Snyder, C.L. Cosma, L.J.B. Davis, and T.J. Silhavy. 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.B.4    Silhavy, T.J.5
  • 18
    • 0027725286 scopus 로고
    • The deduced amino acid sequence of the cloned cpxR gene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli
    • Dong, J.M., S. Iuchi, H.S. Kwan, Z. Lu, and E.C.C. Lin. 1993. The deduced amino acid sequence of the cloned cpxR gene suggests the protein is the cognate regulator for the membrane sensor, CpxA, in a two-component signal transduction system of Escherichia coli. Gene 136: 227-230.
    • (1993) Gene , vol.136 , pp. 227-230
    • Dong, J.M.1    Iuchi, S.2    Kwan, H.S.3    Lu, Z.4    Lin, E.C.C.5
  • 19
    • 0027963327 scopus 로고
    • Characterization and genetic complementation of a Brucella abortus high-temperature-requirement A (htrA) deletion mutant
    • Elzer, P.H., R.W. Phillips, M.E. Kovach, K.M. Peterson, and R.M. Roop II. 1994. Characterization and genetic complementation of a Brucella abortus high-temperature-requirement A (htrA) deletion mutant. Infect. Immun. 62: 4135-4139.
    • (1994) Infect. Immun. , vol.62 , pp. 4135-4139
    • Elzer, P.H.1    Phillips, R.W.2    Kovach, M.E.3    Peterson, K.M.4    Roop II, R.M.5
  • 20
    • 0024727149 scopus 로고
    • E subunit of Escherichia coli RNA polymerase: A second alternate σ factor involved in high-temperature gene expression
    • E subunit of Escherichia coli RNA polymerase: A second alternate σ factor involved in high-temperature gene expression. Genes & Dev. 3: 1462-1471.
    • (1989) Genes & Dev. , vol.3 , pp. 1462-1471
    • Erickson, J.W.1    Gross, C.A.2
  • 21
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: Mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan, J.R. and V. Deretic. 1996. Microbial pathogenesis in cystic fibrosis: Mucoid Pseudomonas aeruginosa and Burkholderia cepacia. Microbiol. Rev. 60: 539-574.
    • (1996) Microbiol. Rev. , vol.60 , pp. 539-574
    • Govan, J.R.1    Deretic, V.2
  • 22
    • 0028971218 scopus 로고
    • Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
    • Guilhot, C., G. Jander, N.L. Martin, and J. Beckwith. 1995. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. 92: 9895-9899.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 9895-9899
    • Guilhot, C.1    Jander, G.2    Martin, N.L.3    Beckwith, J.4
  • 23
    • 0029127550 scopus 로고
    • Identification of cutC and cutF (nlpE) genes involved in copper tolerance in Escherichia coli
    • Gupta, S.D., B.T.O. Lee, J. Camakaris, and H.C. Wu. 1995. Identification of cutC and cutF (nlpE) genes involved in copper tolerance in Escherichia coli. J. Bacteriol. 177: 4207-4215.
    • (1995) J. Bacteriol. , vol.177 , pp. 4207-4215
    • Gupta, S.D.1    Lee, B.T.O.2    Camakaris, J.3    Wu, H.C.4
  • 24
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose Pbad promoter
    • Guzman, L.M., D. Belin, M.J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose Pbad promoter. J. Bacteriol. 177: 4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 25
    • 0027488103 scopus 로고
    • Immunophilins: Structure-function relationship and possible role in microbial pathogenicity
    • Hacker, J. and G. Fischer. 1993. Immunophilins: Structure-function relationship and possible role in microbial pathogenicity. Mol. Microbiol. 10: 445-456.
    • (1993) Mol. Microbiol. , vol.10 , pp. 445-456
    • Hacker, J.1    Fischer, G.2
  • 26
    • 0025756590 scopus 로고
    • Two distinct forms of peptidyl-prolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells
    • Hayano, T., N. Takahashi, S. Kato, N. Kaki, and M. Suzuki. 1991. Two distinct forms of peptidyl-prolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells. Biochemistry 30: 3041-3048.
    • (1991) Biochemistry , vol.30 , pp. 3041-3048
    • Hayano, T.1    Takahashi, N.2    Kato, S.3    Kaki, N.4    Suzuki, M.5
  • 27
    • 0029064061 scopus 로고
    • Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins
    • Horne, S.M. and K.D. Young. 1995. Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins. Arch. Microbiol. 163: 357-365.
    • (1995) Arch. Microbiol. , vol.163 , pp. 357-365
    • Horne, S.M.1    Young, K.D.2
  • 28
    • 0024121496 scopus 로고
    • arcA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways
    • Iuchi, S. and E.C.C. Lin. 1988. arcA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways. Proc. Natl. Acad. Sci. 85: 1888-1892.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 1888-1892
    • Iuchi, S.1    Lin, E.C.C.2
  • 29
    • 0028154918 scopus 로고
    • Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation
    • Jander, G., N.L. Martin, and J. Beckwith. 1994. Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. EMBO J. 13: 5121-5127.
    • (1994) EMBO J. , vol.13 , pp. 5121-5127
    • Jander, G.1    Martin, N.L.2    Beckwith, J.3
  • 31
    • 0028051844 scopus 로고
    • Synergistic activation of transcription by bacteriophage lambda cI protein and E. coli cAMP receptor protein
    • Joung, J., D. Koepp, and A. Hochschild. 1994. Synergistic activation of transcription by bacteriophage lambda cI protein and E. coli cAMP receptor protein. Science 265: 1863-1866.
    • (1994) Science , vol.265 , pp. 1863-1866
    • Joung, J.1    Koepp, D.2    Hochschild, A.3
  • 32
    • 0026567097 scopus 로고
    • Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme
    • Kamitani, S., Y. Akiyama, and K. Ito. 1992. Identification and characterization of an Escherichia coli gene required for the formation of correctly folded alkaline phosphatase, a periplasmic enzyme. EMBO J. 11: 57-62.
    • (1992) EMBO J. , vol.11 , pp. 57-62
    • Kamitani, S.1    Akiyama, Y.2    Ito, K.3
  • 33
    • 0024720319 scopus 로고
    • Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cAMP in Escherichia coli
    • Kawamukai, M., H. Matsuda, W. Fujii, R. Utsumi, and T. Komano. 1989. Nucleotide sequences of fic and fic-1 genes involved in cell filamentation induced by cAMP in Escherichia coli. J. Bacteriol. 171: 4525-4529.
    • (1989) J. Bacteriol. , vol.171 , pp. 4525-4529
    • Kawamukai, M.1    Matsuda, H.2    Fujii, W.3    Utsumi, R.4    Komano, T.5
  • 34
    • 0028809455 scopus 로고
    • Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase
    • Kleerebezem, M., M. Heutink, and J. Tommassen. 1995. Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase. Mol. Microbiol. 18: 313-320.
    • (1995) Mol. Microbiol. , vol.18 , pp. 313-320
    • Kleerebezem, M.1    Heutink, M.2    Tommassen, J.3
  • 35
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S.W. and R. Kolter. 1996. SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 178: 1770-1773.
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 36
    • 0028197624 scopus 로고
    • Target of the transcriptional activation function of phage lambda cI protein
    • Li, M., H. Moyle, and M. Susskind. 1994. Target of the transcriptional activation function of phage lambda cI protein. Science 263: 75-77.
    • (1994) Science , vol.263 , pp. 75-77
    • Li, M.1    Moyle, H.2    Susskind, M.3
  • 38
    • 0025325366 scopus 로고
    • Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: A periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A
    • Liu, J. and C.T. Walsh. 1990. Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: A periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A. Proc. Natl. Acad. Sci. 87: 4028-4032.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 4028-4032
    • Liu, J.1    Walsh, C.T.2
  • 39
    • 0029858049 scopus 로고    scopus 로고
    • Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: Characterization of DNA binding at target promoters
    • Lynch, A.S. and E.C.C. Lin. 1996. Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: Characterization of DNA binding at target promoters. J. Bacteriol. 178: 6238-6249.
    • (1996) J. Bacteriol. , vol.178 , pp. 6238-6249
    • Lynch, A.S.1    Lin, E.C.C.2
  • 40
    • 0027440762 scopus 로고
    • Nitric oxide synthase: Function and mechanism
    • Marletta, M.A. 1993. Nitric oxide synthase: Function and mechanism. Adv. Exp. Med. Biol. 338: 281-284.
    • (1993) Adv. Exp. Med. Biol. , vol.338 , pp. 281-284
    • Marletta, M.A.1
  • 41
    • 0027787823 scopus 로고
    • E, an Escherichia coli heat-inducible a-factor, is modulated by expression of outer membrane proteins
    • E, an Escherichia coli heat-inducible a-factor, is modulated by expression of outer membrane proteins. Genes & Dev. 7: 2618-2628.
    • (1993) Genes & Dev. , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouviere, P.E.2    Erickson, J.W.3    D., T.J.4    Gross, C.A.5
  • 42
    • 0030003139 scopus 로고    scopus 로고
    • Bacterial entry into epithelial cells: The paradigm of Shigella
    • Menard, R., C. Dehio, and P.J. Sansonetti. 1996. Bacterial entry into epithelial cells: The paradigm of Shigella. Trends Microbiol 4: 220-226.
    • (1996) Trends Microbiol , vol.4 , pp. 220-226
    • Menard, R.1    Dehio, C.2    Sansonetti, P.J.3
  • 43
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas, D., J. Betton, and S. Raina. 1996. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol. Microbiol. 21: 871-884.
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.2    Raina, S.3
  • 44
    • 0029146195 scopus 로고
    • Involvement of cpxA, a sensor of a two-component regulatory system, in the pH-dependent regulation of expression of Shigella sonnei virF gene
    • Nakayama, S. and H. Watanabe. 1995. Involvement of cpxA, a sensor of a two-component regulatory system, in the pH-dependent regulation of expression of Shigella sonnei virF gene. J. Bacteriol. 177: 5062-5069.
    • (1995) J. Bacteriol. , vol.177 , pp. 5062-5069
    • Nakayama, S.1    Watanabe, H.2
  • 45
    • 0026034432 scopus 로고
    • Role of nitric oxide synthesis in macrophage antimicrobial activity
    • Nathan, C.F. and J.B. Hibbs. 1991. Role of nitric oxide synthesis in macrophage antimicrobial activity. Curr. Opin. Immunol. 3: 65-70.
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 65-70
    • Nathan, C.F.1    Hibbs, J.B.2
  • 46
    • 0030582675 scopus 로고    scopus 로고
    • Transcription activation at class II CAP-dependent promoters: Two interactions between CAP and RNA polymerase
    • Niu, W., Y. Kim, G. Tau, T. Heyduk, and R.H. Ebright. 1996. Transcription activation at class II CAP-dependent promoters: Two interactions between CAP and RNA polymerase. Cell 87: 1123-1134.
    • (1996) Cell , vol.87 , pp. 1123-1134
    • Niu, W.1    Kim, Y.2    Tau, G.3    Heyduk, T.4    Ebright, R.H.5
  • 47
    • 0028171822 scopus 로고
    • The gene encoding the periplasmic cyclophilin homoloque, PPIase A, in Escherichia coli, is expressed from four promoters, three of which are activated by the cAMP-CRP complex and negatively regulated by the CytR repressor
    • Norregaard-Madsen, M., B. Mygind, R. Pedersen, P. Valentin-Hansen, and L. Sogaard-Andersen. 1994. The gene encoding the periplasmic cyclophilin homoloque, PPIase A, in Escherichia coli, is expressed from four promoters, three of which are activated by the cAMP-CRP complex and negatively regulated by the CytR repressor. Mol. Microbiol. 14: 989-997.
    • (1994) Mol. Microbiol. , vol.14 , pp. 989-997
    • Norregaard-Madsen, M.1    Mygind, B.2    Pedersen, R.3    Valentin-Hansen, P.4    Sogaard-Andersen, L.5
  • 48
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J.S. and E.C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26: 71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 49
    • 0026668342 scopus 로고
    • Characterization of a periplasmic thiol:Disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae
    • Peek, J.A. and R.K. Taylor. 1992. Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae. Proc. Natl. Acad. Sci. 89: 6210-6214.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 6210-6214
    • Peek, J.A.1    Taylor, R.K.2
  • 50
    • 0027457371 scopus 로고
    • The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself
    • Pogliano, K.J. and J. Beckwith. 1993. The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself. Genetics 133: 763-773.
    • (1993) Genetics , vol.133 , pp. 763-773
    • Pogliano, K.J.1    Beckwith, J.2
  • 51
    • 0028349613 scopus 로고
    • A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli
    • Rahfeld, J., A. Schierhorn, K. Mann, and G. Fischer. 1994. A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli. FEBS Lett. 343: 65-69.
    • (1994) FEBS Lett. , vol.343 , pp. 65-69
    • Rahfeld, J.1    Schierhorn, A.2    Mann, K.3    Fischer, G.4
  • 53
    • 0025355396 scopus 로고
    • The Cpx proteins of Escherichia coli K-12: Evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene
    • Rainwater, S. and P. Silverman. 1990. The Cpx proteins of Escherichia coli K-12: Evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene. J. Bacteriol. 172: 2456-2461.
    • (1990) J. Bacteriol. , vol.172 , pp. 2456-2461
    • Rainwater, S.1    Silverman, P.2
  • 54
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch, A., D. Belin, N. Martin, and J. Beckwith. 1996. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. 93: 13048-13053.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 13048-13053
    • Rietsch, A.1    Belin, D.2    Martin, N.3    Beckwith, J.4
  • 55
    • 0028070767 scopus 로고
    • slyD, a host gene required for ΦX174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans isomerases
    • Roof, W.D., S.M. Horne, K.D. Young, and Y. Young. 1994. slyD, a host gene required for ΦX174 lysis, is related to the FK506-binding protein family of peptidyl-prolyl cis-trans isomerases. J. Biol. Chem. 269: 2902-2910.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2902-2910
    • Roof, W.D.1    Horne, S.M.2    Young, K.D.3    Young, Y.4
  • 56
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouvière, P.E. and C.A. Gross. 1996. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes & Dev. 10: 3170-3182.
    • (1996) Genes & Dev. , vol.10 , pp. 3170-3182
    • Rouvière, P.E.1    Gross, C.A.2
  • 59
    • 0026510141 scopus 로고
    • Peptidyl-prolyl cistrans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding
    • Schonbrunner, E.R. and F.X. Schmid. 1992. Peptidyl-prolyl cistrans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding. Proc. Natl. Acad. Sci. 89: 4510-4513.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 4510-4513
    • Schonbrunner, E.R.1    Schmid, F.X.2
  • 60
    • 0028983261 scopus 로고
    • Overproduction of N1pE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway
    • Snyder, W.B., L.J. Davis, P.N. Danese, C.L. Cosma, and T.J. Silhavy. 1995. Overproduction of N1pE, 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
  • 61
    • 0023974826 scopus 로고
    • An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins
    • Strauch, K.L. and J. Beckwith. 1988. An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc. Natl. Acad. Sci. 85: 1576-1580.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 1576-1580
    • Strauch, K.L.1    Beckwith, J.2
  • 62
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • Strauch, K.L., K. Johnson, and J. Beckwith. 1989. Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J. Bacteriol. 171: 2689-2696.
    • (1989) J. Bacteriol. , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 63
    • 0028979581 scopus 로고
    • Repair, refold, recycle: How bacteria can deal with spontaneous and environmental damage to proteins
    • Visick, J.E. and S. Clarke. 1995. Repair, refold, recycle: How bacteria can deal with spontaneous and environmental damage to proteins. Mol. Microbiol. 16: 835-845.
    • (1995) Mol. Microbiol. , vol.16 , pp. 835-845
    • Visick, J.E.1    Clarke, S.2
  • 64
    • 0029025060 scopus 로고
    • Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells
    • Watarai, M., T. Tobe, M. Yoshikawa, and C. Sasakawa. 1995. Disulfide oxidoreductase activity of Shigella flexneri is required for release of Ipa proteins and invasion of epithelial cells. Proc. Natl Acad. Sci. 92: 4927-4931.
    • (1995) Proc. Natl Acad. Sci. , vol.92 , pp. 4927-4931
    • Watarai, M.1    Tobe, T.2    Yoshikawa, M.3    Sasakawa, C.4
  • 65
    • 0028286019 scopus 로고
    • Protein folding in the periplasm of Escherichia coli
    • Wulfing, C. and A. Pluckthun. 1994. Protein folding in the periplasm of Escherichia coli. Mol. Microbiol. 12: 685-692.
    • (1994) Mol. Microbiol. , vol.12 , pp. 685-692
    • Wulfing, C.1    Pluckthun, A.2
  • 66
    • 0027934203 scopus 로고
    • An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif
    • Wulfing, C., J. Lombardero, and A. Pluckthun. 1994. An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. J. Biol. Chem. 269: 2895-2901.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2895-2901
    • Wulfing, C.1    Lombardero, J.2    Pluckthun, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.