메뉴 건너뛰기




Volumn 189, Issue 2, 2007, Pages 446-454

Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN LAMB; UNCLASSIFIED DRUG;

EID: 33846234653     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01103-06     Document Type: Article
Times cited : (77)

References (28)
  • 1
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens, S., R. Maier, H. de Cock, F. X. Schmid, and C. A. Gross. 2001. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 20:285-294.
    • (2001) EMBO J , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    de Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 2
    • 8844219773 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos, M. P., and J. Tommassen. 2004. Biogenesis of the Gram-negative bacterial outer membrane. Curr. Opin. Microbiol. 7:610-616.
    • (2004) Curr. Opin. Microbiol , vol.7 , pp. 610-616
    • Bos, M.P.1    Tommassen, J.2
  • 3
    • 8844237557 scopus 로고    scopus 로고
    • Quality control in the bacterial periplasm
    • Duguay, A. R., and T. J. Silhavy. 2004. Quality control in the bacterial periplasm. Biochim. Biophys. Acta 1694:121-134.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 121-134
    • Duguay, A.R.1    Silhavy, T.J.2
  • 4
    • 0036947253 scopus 로고    scopus 로고
    • Signal sequence mutations as tools for the characterization of LamB folding intermediates
    • Duguay, A. R., and T. J. Silhavy. 2002. Signal sequence mutations as tools for the characterization of LamB folding intermediates. J. Bacteriol. 184:6918-6928.
    • (2002) J. Bacteriol , vol.184 , pp. 6918-6928
    • Duguay, A.R.1    Silhavy, T.J.2
  • 5
    • 0030959069 scopus 로고    scopus 로고
    • Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
    • Duong, F., and W. Wickner. 1997. Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme. EMBO J. 16:2756-2768.
    • (1997) EMBO J , vol.16 , pp. 2756-2768
    • Duong, F.1    Wickner, W.2
  • 6
    • 0023035811 scopus 로고
    • An outer membrane protein (OmpA) of Escherichia coli K-12 undergoes a conformational change during export
    • Freudl, R., H. Schwarz, Y. D. Stierbof, K. Gamon, I. Hindennach, and U. Henning. 1986. An outer membrane protein (OmpA) of Escherichia coli K-12 undergoes a conformational change during export. J. Biol. Chem. 261:11355-11361.
    • (1986) J. Biol. Chem , vol.261 , pp. 11355-11361
    • Freudl, R.1    Schwarz, H.2    Stierbof, Y.D.3    Gamon, K.4    Hindennach, I.5    Henning, U.6
  • 7
    • 0025045470 scopus 로고
    • The secD locus of E. coli codes for two membrane proteins required for protein export
    • Gardel, C., K. Johnson, A. Jacq, and J. Beckwith. 1990. The secD locus of E. coli codes for two membrane proteins required for protein export. EMBO J. 9:3209-3216.
    • (1990) EMBO J , vol.9 , pp. 3209-3216
    • Gardel, C.1    Johnson, K.2    Jacq, A.3    Beckwith, J.4
  • 8
    • 0029822373 scopus 로고    scopus 로고
    • Folding intermediates of a β-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism
    • Kleinschmidt, J. H., and L. K. Tamm. 1996. Folding intermediates of a β-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism. Biochemistry 35:12993-13000.
    • (1996) Biochemistry , vol.35 , pp. 12993-13000
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 9
    • 0343939593 scopus 로고
    • Escherichia coli SecB protein associates with exported protein precursors in vivo
    • Kumamoto, C. A. 1989. Escherichia coli SecB protein associates with exported protein precursors in vivo. Proc. Natl. Acad. Sci. USA 86:5320-5324.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5320-5324
    • Kumamoto, C.A.1
  • 10
    • 0023710191 scopus 로고
    • Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics
    • Kumamoto, C. A., and P. M. Gannon. 1988. Effects of Escherichia coli secB mutations on pre-maltose binding protein conformation and export kinetics. J. Biol. Chem. 263:11554-11558.
    • (1988) J. Biol. Chem , vol.263 , pp. 11554-11558
    • Kumamoto, C.A.1    Gannon, P.M.2
  • 11
    • 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
  • 12
    • 0025370548 scopus 로고
    • ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein
    • Lecker, S. H., A. J. Driessen, and W. Wickner. 1990. ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein. EMBO J. 9:2309-2314.
    • (1990) EMBO J , vol.9 , pp. 2309-2314
    • Lecker, S.H.1    Driessen, A.J.2    Wickner, W.3
  • 13
    • 0027458691 scopus 로고
    • SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli
    • Matsuyama, S., Y. Fujita, and S. Mizushima. 1993. SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli. EMBO J. 12:265-270.
    • (1993) EMBO J , vol.12 , pp. 265-270
    • Matsuyama, S.1    Fujita, Y.2    Mizushima, S.3
  • 14
    • 0025768542 scopus 로고
    • A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli
    • Misra, R., A. Peterson, T. Ferenci, and T. J. Silhavy. 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
  • 15
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between folding factors and bacterial outer membrane proteins
    • Mogensen, J. E., and D. E. Otzen. 2005. Interactions between folding factors and bacterial outer membrane proteins. Mol. Microbiol. 57:326-346.
    • (2005) Mol. Microbiol , vol.57 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 16
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-656.
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 17
    • 0002431489 scopus 로고    scopus 로고
    • Outer membrane
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger ed, 2nd ed. ASM Press, Washington, DC
    • Nikaido, H. 1996. Outer membrane, p. 29-47. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella typhimurium: Cellular and molecular biology , pp. 29-47
    • Nikaido, H.1
  • 18
    • 0036809395 scopus 로고    scopus 로고
    • SecB, one small chaperone in the complex milieu of the cell
    • Randall, L. L., and S. J. Hardy. 2002. SecB, one small chaperone in the complex milieu of the cell. Cell. Mol. Life Sci. 59:1617-1623.
    • (2002) Cell. Mol. Life Sci , vol.59 , pp. 1617-1623
    • Randall, L.L.1    Hardy, S.J.2
  • 19
    • 0023880052 scopus 로고
    • A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene
    • Riggs, P. D., A. I. Derman, and J. Beckwith. 1988. A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene. Genetics 118:571-579.
    • (1988) Genetics , vol.118 , pp. 571-579
    • Riggs, P.D.1    Derman, A.I.2    Beckwith, J.3
  • 20
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • Rizzitello, A. E., J. R. Harper, and T. J. Silhavy. 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
  • 21
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouviere, 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
    • Rouviere, P.E.1    Gross, C.A.2
  • 22
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality; a genetic strategy to probe organelle assembly
    • Ruiz, N., B. Falcone, D. Kahne, and T. J. Silhavy. 2005. Chemical conditionality; a genetic strategy to probe organelle assembly. Cell 121:307-317.
    • (2005) Cell , vol.121 , pp. 307-317
    • Ruiz, N.1    Falcone, B.2    Kahne, D.3    Silhavy, T.J.4
  • 23
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • Ruiz, N., D. Kahne, and T. J. Silhavy. 2006. Advances in understanding bacterial outer-membrane biogenesis. Nat. Rev. Microbiol. 4:57-66.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 57-66
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 25
    • 0025309069 scopus 로고
    • surA, an Escherichia coli gene essential for survival in stationary phase
    • Torino, A., M. Almiron, and R. Kolter. 1990. surA, an Escherichia coli gene essential for survival in stationary phase. J. Bacteriol. 172:4339-4347.
    • (1990) J. Bacteriol , vol.172 , pp. 4339-4347
    • Torino, A.1    Almiron, M.2    Kolter, R.3
  • 26
    • 8844230242 scopus 로고    scopus 로고
    • Veenendaal, A. K., C. van der Does, and A. J. Driessen. 2004. The protein-conducting channel SecYEG. Biochim. Biophys. Acta 1694:81-95.
    • Veenendaal, A. K., C. van der Does, and A. J. Driessen. 2004. The protein-conducting channel SecYEG. Biochim. Biophys. Acta 1694:81-95.
  • 27
    • 4444290475 scopus 로고    scopus 로고
    • Structure and function of SecA, the preprotein translocase nanomotor
    • Vrontou, E., and A. Economou. 2004. Structure and function of SecA, the preprotein translocase nanomotor. Biochim. Biophys. Acta 1694:67-80.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 67-80
    • Vrontou, E.1    Economou, A.2
  • 28
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu, T., J. Malinverni, N. Ruiz, S. Kim, T. J. Silhavy, and D. Kahne. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.