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Volumn 75, Issue 4, 2010, Pages 1033-1046

Involvement and necessity of the Cpx regulon in the event of aberrant β-barrel outer membrane protein assembly

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; OUTER MEMBRANE PROTEIN;

EID: 76449101997     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.07042.x     Document Type: Article
Times cited : (32)

References (66)
  • 1
    • 56949096401 scopus 로고    scopus 로고
    • e envelope stress response
    • E envelope stress response. Curr Opin Microbiol 11 : 535 540.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 535-540
    • Ades, S.E.1
  • 2
    • 0033568606 scopus 로고    scopus 로고
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-∑ factor
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-∑ factor. Genes Dev 13 : 2449 2461.
    • (1999) Genes Dev , vol.13 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 3
    • 2442563573 scopus 로고    scopus 로고
    • E-dependent envelope stress response
    • E-dependent envelope stress response. Mol Microbiol 52 : 613 619.
    • (2004) Mol Microbiol , vol.52 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 5
    • 23644456999 scopus 로고    scopus 로고
    • The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins OmpF and OmpC
    • Batchelor, E., Walthers, D., Kenney, L.J. Goulian, M. (2005) The Escherichia coli CpxA-CpxR envelope stress response system regulates expression of the porins OmpF and OmpC. J Bacteriol 187 : 5723 5731.
    • (2005) J Bacteriol , vol.187 , pp. 5723-5731
    • Batchelor, E.1    Walthers, D.2    Kenney, L.J.3    Goulian, M.4
  • 6
    • 3042554408 scopus 로고    scopus 로고
    • Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface
    • Bos, M.P., Tefsen, B., Geurtsen, J. Tommassen, J. (2004) Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface. Proc Natl Acad Sci USA 101 : 9417 9422.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9417-9422
    • Bos, M.P.1    Tefsen, B.2    Geurtsen, J.3    Tommassen, J.4
  • 7
    • 25144512854 scopus 로고    scopus 로고
    • Cpx signal transduction is influenced by a conserved N-terminal domain in the novel inhibitor CpxP and the periplasmic protease DegP
    • Buelow, D.R. Raivio, T.L. (2005) Cpx signal transduction is influenced by a conserved N-terminal domain in the novel inhibitor CpxP and the periplasmic protease DegP. J Bacteriol 187 : 6622 6630.
    • (2005) J Bacteriol , vol.187 , pp. 6622-6630
    • Buelow, D.R.1    Raivio, T.L.2
  • 8
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to select promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M.J. (1976) Transposition and fusion of the lac genes to select promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol 141 : 541 555.
    • (1976) J Mol Biol , vol.141 , pp. 541-555
    • Casadaban, M.J.1
  • 9
    • 0037214416 scopus 로고    scopus 로고
    • Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture
    • CastilloKeller, M. Misra, R. (2003) Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture. J Bacteriol 185 : 148 154.
    • (2003) J Bacteriol , vol.185 , pp. 148-154
    • Castillokeller, M.1    Misra, R.2
  • 10
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A.C.Y. Cohen, S.N. (1978) Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J Bacteriol 134 : 1141 1156.
    • (1978) J Bacteriol , vol.134 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 11
    • 33749593869 scopus 로고    scopus 로고
    • Differential effects of yfgL mutation on the biogenesis of Escherichia coli outer membrane proteins and lipopolysaccharide
    • Charlson, E.S., Werner, J.N. Misra, R. (2006) Differential effects of yfgL mutation on the biogenesis of Escherichia coli outer membrane proteins and lipopolysaccharide. J Bacteriol 188 : 7186 7194.
    • (2006) J Bacteriol , vol.188 , pp. 7186-7194
    • Charlson, E.S.1    Werner, J.N.2    Misra, R.3
  • 12
    • 0030763077 scopus 로고    scopus 로고
    • The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways
    • Connolly, L., Peñas, A.D.L., Alba, B.M. Gross, C.A. (1997) The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways. Genes Dev 11 : 2012 2021.
    • (1997) Genes Dev , vol.11 , pp. 2012-2021
    • Connolly, L.1    Peñas, A.D.L.2    Alba, B.M.3    Gross, C.A.4
  • 13
    • 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 11 : 1183 1193.
    • (1997) Genes Dev , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 14
    • 0031905590 scopus 로고    scopus 로고
    • CpxP, a stress-combative member of the Cpx regulon
    • Danese, P.N. 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
  • 15
    • 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.B. 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.B.4    Silhavy, T.J.5
  • 16
    • 0031765192 scopus 로고    scopus 로고
    • Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli
    • Danese, P.N., Oliver, G.R., Barr, K., Bowman, G.D., Rick, P.D. Silhavy, T.J. (1998) Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli. J Bacteriol 180 : 5875 5884.
    • (1998) J Bacteriol , vol.180 , pp. 5875-5884
    • Danese, P.N.1    Oliver, G.R.2    Barr, K.3    Bowman, G.D.4    Rick, P.D.5    Silhavy, T.J.6
  • 17
    • 0032527831 scopus 로고    scopus 로고
    • A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
    • Dartigalongue, C. Raina, S. (1998) A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J 17 : 3968 3980.
    • (1998) EMBO J , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 18
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A. Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97 : 6640 6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 19
    • 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. Lin, E.C.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.C.4
  • 20
    • 0037384456 scopus 로고    scopus 로고
    • Signal detection and target gene induction by the CpxRA two-component system
    • DiGiuseppe, P.A. Silhavy, T.J. (2003) Signal detection and target gene induction by the CpxRA two-component system. J Bacteriol 185 : 2432 2440.
    • (2003) J Bacteriol , vol.185 , pp. 2432-2440
    • Digiuseppe, P.A.1    Silhavy, T.J.2
  • 21
    • 33646072467 scopus 로고    scopus 로고
    • The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities?
    • Dorel, C., Lejeune, P. Rodrigue, A. (2006) The Cpx system of Escherichia coli, a strategic signaling pathway for confronting adverse conditions and for settling biofilm communities? Res Microbiol 157 : 306 314.
    • (2006) Res Microbiol , vol.157 , pp. 306-314
    • Dorel, C.1    Lejeune, P.2    Rodrigue, A.3
  • 22
    • 0024727149 scopus 로고
    • e subunit of Escherichia coli RNA polymerase: A second alternate sigma factor involved in high-temperature gene expression
    • E subunit of Escherichia coli RNA polymerase: a second alternate sigma factor involved in high-temperature gene expression. Genes Dev 3 : 1462 1471.
    • (1989) Genes Dev , vol.3 , pp. 1462-1471
    • Erickson, J.1    Gross, C.A.2
  • 23
    • 34247880509 scopus 로고    scopus 로고
    • Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli
    • Fleischer, R., Heermann, R., Jung, K. Hunke, S. (2007) Purification, reconstitution, and characterization of the CpxRAP envelope stress system of Escherichia coli. J Biol Chem 282 : 8583 8593.
    • (2007) J Biol Chem , vol.282 , pp. 8583-8593
    • Fleischer, R.1    Heermann, R.2    Jung, K.3    Hunke, S.4
  • 25
    • 7544239890 scopus 로고    scopus 로고
    • E envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA
    • E envelope stress response relies on multiple mechanisms to inhibit signal-independent proteolysis of the transmembrane anti-sigma factor, RseA. EMBO J 18 : 2686 2697.
    • (2004) EMBO J , vol.18 , pp. 2686-2697
    • Grigorova, I.L.1    Chaba, R.2    Zhong, H.J.3    Alba, B.M.4    Rhodius, V.5    Herman, C.6    Gross, C.A.7
  • 27
    • 35348985928 scopus 로고    scopus 로고
    • e stress response by DegS: How the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress
    • E stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress. EMBO J 21 : 2659 2670.
    • (2007) EMBO J , vol.21 , pp. 2659-2670
    • Hasselblatt, H.1    Kurzbauer, R.2    Wilken, C.3    Krojer, T.4    Sawa, J.5    Kurt, J.6
  • 28
    • 0035794607 scopus 로고    scopus 로고
    • Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili
    • Hung, D.L., Ravio, T.L., Jones, C.H., Silhavy, T.J. Hultgren, S.J. (2001) Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili. EMBO J 20 : 1508 1518.
    • (2001) EMBO J , vol.20 , pp. 1508-1518
    • Hung, D.L.1    Ravio, T.L.2    Jones, C.H.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 29
    • 58049199407 scopus 로고    scopus 로고
    • A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli
    • Inaba, K., Suzuki, M., Maegawa, K.-I., Akiyama, S., Ito, K. Akiyama, Y. (2008) A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli. J Biol Chem 283 : 35042 35042.
    • (2008) J Biol Chem , vol.283 , pp. 35042-35042
    • Inaba, K.1    Suzuki, M.2    Maegawa, K.-I.3    Akiyama, S.4    Ito, K.5    Akiyama, Y.6
  • 30
    • 29144519709 scopus 로고    scopus 로고
    • The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP
    • Isaac, D.D., Pinkner, J.S., Hultgren, S.J. Silhavy, T.J. (2005) The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP. Proc Natl Acd Sci USA 102 : 17775 17779.
    • (2005) Proc Natl Acd Sci USA , vol.102 , pp. 17775-17779
    • Isaac, D.D.1    Pinkner, J.S.2    Hultgren, S.J.3    Silhavy, T.J.4
  • 32
    • 0030775342 scopus 로고    scopus 로고
    • The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
    • Jones, C.H., Danese, P.N., Pinkner, J.S., Silhavy, T.J. Hultgren, S.J. (1997) The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems. EMBO J 16 : 6394 6406.
    • (1997) EMBO J , vol.16 , pp. 6394-6406
    • Jones, C.H.1    Danese, P.N.2    Pinkner, J.S.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 33
    • 14644435718 scopus 로고    scopus 로고
    • CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli
    • Jubelin, G., Vianney, A., Beloin, C., Ghigo, J.-M., Lazzaroni, J.-C., Lejeune, P. Dorel, C. (2005) CpxR/OmpR interplay regulates curli gene expression in response to osmolarity in Escherichia coli. J Bactetiol 187 : 2038 2049.
    • (2005) J Bactetiol , vol.187 , pp. 2038-2049
    • Jubelin, G.1    Vianney, A.2    Beloin, C.3    Ghigo, J.-M.4    Lazzaroni, J.-C.5    Lejeune, P.6    Dorel, C.7
  • 34
    • 69049106304 scopus 로고    scopus 로고
    • Misfolded maltose binding protein MalE219 induces the CpxRA envelope stress response by stimulating phosphoryl transfer from CpxA to CpxR
    • Keller, R.F. Hunke, S. (2009) Misfolded maltose binding protein MalE219 induces the CpxRA envelope stress response by stimulating phosphoryl transfer from CpxA to CpxR. Res Microbiol 160 : 396 400.
    • (2009) Res Microbiol , vol.160 , pp. 396-400
    • Keller, R.F.1    Hunke, S.2
  • 35
    • 0028809455 scopus 로고    scopus 로고
    • Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase
    • Kleerebezem, M., Heutink, M. Tommassen, J. (2004) Characterization of an Escherichia coli rotA mutant, affected in periplasmic peptidyl-prolyl cis/trans isomerase. Mol Microbiol 18 : 313 320.
    • (2004) Mol Microbiol , vol.18 , pp. 313-320
    • Kleerebezem, M.1    Heutink, M.2    Tommassen, J.3
  • 36
    • 67649561853 scopus 로고    scopus 로고
    • Escherichia coli K-12 suppressor-free mutants lacking early glycosyltransferases and late acyltransferases: Minimal lipopolysaccharide structure and induction of envelope stress response
    • Klein, G., Lindner, B., Brabetz, W., Brade, H. Raina, S. (2009) Escherichia coli K-12 suppressor-free mutants lacking early glycosyltransferases and late acyltransferases: minimal lipopolysaccharide structure and induction of envelope stress response. J Biol Chem 284 : 15369 15389.
    • (2009) J Biol Chem , vol.284 , pp. 15369-15389
    • Klein, G.1    Lindner, B.2    Brabetz, W.3    Brade, H.4    Raina, S.5
  • 37
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer, T., Sawa, J., Schäfer, E., Saibil, H.R., Ehrmann, M. Clausen, T. (2008) Structural basis for the regulated protease and chaperone function of DegP. Nature 453 : 885 891.
    • (2008) Nature , vol.453 , pp. 885-891
    • Krojer, T.1    Sawa, J.2    Schäfer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 39
    • 0020581487 scopus 로고
    • Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli
    • Michaelis, S., Inouye, H., Oliver, D. Beckwith, J. (1983) Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. J Bacteriol 154 : 366 374.
    • (1983) J Bacteriol , vol.154 , pp. 366-374
    • Michaelis, S.1    Inouye, H.2    Oliver, D.3    Beckwith, J.4
  • 40
    • 0031039158 scopus 로고    scopus 로고
    • The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine
    • Mileykovskaya, E. Dowhan, W. (1997) The Cpx two-component signal transduction pathway is activated in Escherichia coli mutant strains lacking phosphatidylethanolamine. J Bacteriol 179 : 1029 1034.
    • (1997) J Bacteriol , vol.179 , pp. 1029-1034
    • Mileykovskaya, E.1    Dowhan, W.2
  • 42
    • 0027730653 scopus 로고
    • A novel ompC mutation of Escherichia coli K-12 that reduces OmpC and OmpF levels in the outer membrane
    • Misra, R. (1993) A novel ompC mutation of Escherichia coli K-12 that reduces OmpC and OmpF levels in the outer membrane. Mol Microbiol 10 : 1029 1035.
    • (1993) Mol Microbiol , vol.10 , pp. 1029-1035
    • Misra, R.1
  • 43
    • 0025768542 scopus 로고
    • A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli
    • Misra, R., Peterson, A., Ferenci, T. Silhavy, T.J. (1991) A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli. J Biol Chem 266 : 13592 13597.
    • (1991) J Biol Chem , vol.266 , pp. 13592-13597
    • Misra, R.1    Peterson, A.2    Ferenci, T.3    Silhavy, T.J.4
  • 44
    • 0033870158 scopus 로고    scopus 로고
    • S210A rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background
    • S210A rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background. J Bacteriol 182 : 4882 4888.
    • (2000) J Bacteriol , vol.182 , pp. 4882-4888
    • Misra, R.1    Castillokeller, M.2    Deng, M.3
  • 45
    • 4544222062 scopus 로고    scopus 로고
    • Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm
    • Miyadai, H., Tanaka-Masuda, K., Matsuyama, S. Tokuda, H. (2004) Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm. J Biol Chem 279 : 39807 39813.
    • (2004) J Biol Chem , vol.279 , pp. 39807-39813
    • Miyadai, H.1    Tanaka-Masuda, K.2    Matsuyama, S.3    Tokuda, H.4
  • 47
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • Pogliano, J., Lynch, A.S., Belin, D., Lin, E.C.C. Beckwith, J. (1997) Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev 11 : 1169 1182.
    • (1997) Genes Dev , vol.11 , pp. 1169-1182
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lin, E.C.C.4    Beckwith, J.5
  • 48
    • 63049096052 scopus 로고    scopus 로고
    • Characterization of the Cpx regulon in Escherichia coli strain MC4100
    • Price, N.L. 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
  • 49
    • 0030834844 scopus 로고    scopus 로고
    • Transduction of envelope stress in Escherichia coli by the Cpx two-component system
    • Raivio, T.L. Silhavy, T.J. (1997) Transduction of envelope stress in Escherichia coli by the Cpx two-component system. J Bacteriol 179 : 7724 7733.
    • (1997) J Bacteriol , vol.179 , pp. 7724-7733
    • Raivio, T.L.1    Silhavy, T.J.2
  • 50
    • 0033106492 scopus 로고    scopus 로고
    • e and Cpx regulatory pathways: Overlapping but distinct envelope stress responses
    • E and Cpx regulatory pathways: overlapping but distinct envelope stress responses. Curr Opin Microbiol 2 : 159 165.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 159-165
    • Raivio, T.L.1    Silhavy, T.J.2
  • 51
    • 0032851357 scopus 로고    scopus 로고
    • The Cpx envelope stress response is controlled by amplification and feedback inhibition
    • Raivio, T.L., Popkin, D.L. Silhavy, T.J. (1999) The Cpx envelope stress response is controlled by amplification and feedback inhibition. J Bacteriol 181 : 5263 5272.
    • (1999) J Bacteriol , vol.181 , pp. 5263-5272
    • Raivio, T.L.1    Popkin, D.L.2    Silhavy, T.J.3
  • 53
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • Rizzitello, A.E., Harper, J.R. Silhavy, T.J. (2001) Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J Bacteriol 183 : 6794 6800.
    • (2001) J Bacteriol , vol.183 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 54
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: Watchdogs of the Escherichia coli cell envelope
    • Ruiz, N. Silhavy, T.J. (2005) Sensing external stress: watchdogs of the Escherichia coli cell envelope. Curr Opin Microbiol 8 : 122 126.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 122-126
    • Ruiz, N.1    Silhavy, T.J.2
  • 55
    • 33846571920 scopus 로고    scopus 로고
    • SecY alterations that impair membrane protein folding and generate a membrane stress
    • Shimohata, N., Nagamori, S., Akiyama, Y., Kaback, H.R. Ito, K. (2007) SecY alterations that impair membrane protein folding and generate a membrane stress. J Cell Biol 176 : 307 317.
    • (2007) J Cell Biol , vol.176 , pp. 307-317
    • Shimohata, N.1    Nagamori, S.2    Akiyama, Y.3    Kaback, H.R.4    Ito, K.5
  • 57
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • Sklar, J.G., Wu, T., Kahne, D. Silhavy, T.J. (2007) Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev 21 : 2473 2484.
    • (2007) Genes Dev , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 58
    • 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.B., Danese, P.N., Cosma, C.L. 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.B.2    Danese, P.N.3    Cosma, C.L.4    Silhavy, T.J.5
  • 59
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperones to protease in a widely conserved heat shock protein
    • Spiess, C., Bell, A. Ehrmann, M. (1999) A temperature-dependent switch from chaperones to protease in a widely conserved heat shock protein. Cell 97 : 339 347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Bell, A.2    Ehrmann, M.3
  • 60
    • 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., Johnson, K. Beckwith, J. (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
  • 61
    • 0025976068 scopus 로고
    • Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • Struyvé, M., Moons, M. Tommassen, J. (1991) Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J Mol Biol 218 : 141 148.
    • (1991) J Mol Biol , vol.218 , pp. 141-148
    • Struyvé, M.1    Moons, M.2    Tommassen, J.3
  • 62
    • 39749086276 scopus 로고    scopus 로고
    • Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry
    • Vuong, P., Bennion, D., Mantei, J., Frost, D. Misra, R. (2008) Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry. J Bacteriol 190 : 1507 1517.
    • (2008) J Bacteriol , vol.190 , pp. 1507-1517
    • Vuong, P.1    Bennion, D.2    Mantei, J.3    Frost, D.4    Misra, R.5
  • 63
    • 0344953579 scopus 로고    scopus 로고
    • Peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • Walsh, N.P., Alba, B.M., Bose, B., Gross, C.A. Sauer, R.T. (2003) Peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113 : 61 71.
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 64
    • 23844507131 scopus 로고    scopus 로고
    • YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli
    • Werner, J. Misra, R. (2005) YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol Microbiol 57 : 1450 1459.
    • (2005) Mol Microbiol , vol.57 , pp. 1450-1459
    • Werner, J.1    Misra, R.2
  • 65
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu, T., Malinverni, J., Ruiz, N., Kim, S., Silhavy, T.J. Kahne, D. (2005) Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 121 : 235 245.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 66
    • 33746462208 scopus 로고    scopus 로고
    • Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli
    • Yamamoto, K. Ishihama, A. (2006) Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli. Biosci Biotechnol Biochem 70 : 1688 1695.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 1688-1695
    • Yamamoto, K.1    Ishihama, A.2


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