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Volumn 10, Issue 4, 2010, Pages 771-784

Contribution of proteomics toward solving the fascinating mysteries of the biogenesis of the envelope of Escherichia coli

Author keywords

BamA; DsbA; DsbD; Microbiology; Skp; SurA

Indexed keywords

CHAPERONE; DEGP PROTEIN; DSBA PROTEIN; DSBB PROTEIN; DSBC PROTEIN; FKPA PROTEIN; LOLA PROTEIN; MEMBRANE PROTEIN; PEPTIDYLPROLYL ISOMERASE; S PHASE KINASE ASSOCIATED PROTEIN; SURA PROTEIN; UNCLASSIFIED DRUG;

EID: 77149177335     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900461     Document Type: Review
Times cited : (18)

References (120)
  • 1
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • Ruiz, N., Kahne, D., Silhavy, T. J., Advances in understanding bacterial outer-membrane biogenesis. Nat. Rev. Microbiol. 2006, 4, 57-66.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 57-66
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 2
    • 65349145827 scopus 로고    scopus 로고
    • Biogenesis of outer membranes in Gramnegative bacteria
    • Tokuda, H., Biogenesis of outer membranes in Gramnegative bacteria. Biosci. Biotechnol. Biochem. 2009, 73, 465-473.
    • (2009) Biosci. Biotechnol. Biochem , vol.73 , pp. 465-473
    • Tokuda, H.1
  • 3
    • 33645836299 scopus 로고    scopus 로고
    • Lipid trafficking to the outer membrane of Gram-negative bacteria
    • Doerrler, W. T., Lipid trafficking to the outer membrane of Gram-negative bacteria. Mol. Microbiol. 2006, 60, 542-552.
    • (2006) Mol. Microbiol , vol.60 , pp. 542-552
    • Doerrler, W.T.1
  • 5
    • 0022467729 scopus 로고
    • Lateral diffusion of proteins in the periplasm of Escherichia coli
    • Brass, J. M., Higgins, C. F., Foley, M., Rugman, P. A. et al., Lateral diffusion of proteins in the periplasm of Escherichia coli. J. Bacteriol. 1986, 165, 787-795.
    • (1986) J. Bacteriol , vol.165 , pp. 787-795
    • Brass, J.M.1    Higgins, C.F.2    Foley, M.3    Rugman, P.A.4
  • 6
    • 50049088184 scopus 로고    scopus 로고
    • ASM Press, Duisburg-Essen
    • Ehrmann, M., The Periplasm. ASM Press, Duisburg-Essen, 2006.
    • (2006) The Periplasm
    • Ehrmann, M.1
  • 7
    • 4444220092 scopus 로고    scopus 로고
    • The architecture of the murein (peptidoglycan) in gram-negative bacteria: Vertical scaffold or horizontal layer(s)?
    • Vollmer, W., Holtje, J. V., The architecture of the murein (peptidoglycan) in gram-negative bacteria: vertical scaffold or horizontal layer(s)? J. Bacteriol. 2004, 186, 5978-5987.
    • (2004) J. Bacteriol , vol.186 , pp. 5978-5987
    • Vollmer, W.1    Holtje, J.V.2
  • 8
  • 9
    • 50049135906 scopus 로고    scopus 로고
    • Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis
    • Weiner, J. H., Li, L., Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis. Biochim. Biophys. Acta 2008, 1778, 1698-1713.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1698-1713
    • Weiner, J.H.1    Li, L.2
  • 10
    • 57649119791 scopus 로고    scopus 로고
    • Mechanisms of YidCmediated insertion and assembly of multimeric membrane protein complexes
    • Kol, S., Nouwen, N., Driessen, A. J., Mechanisms of YidCmediated insertion and assembly of multimeric membrane protein complexes. J. Biol. Chem. 2008, 283, 31269-31273.
    • (2008) J. Biol. Chem , vol.283 , pp. 31269-31273
    • Kol, S.1    Nouwen, N.2    Driessen, A.J.3
  • 13
    • 47049106943 scopus 로고    scopus 로고
    • Effects of SecE depletion on the inner and outer membrane proteomes of Escherichia coli
    • Baars, L., Wagner, S., Wickstrom, D., Klepsch, M. et al., Effects of SecE depletion on the inner and outer membrane proteomes of Escherichia coli. J. Bacteriol. 2008, 190, 3505-3525.
    • (2008) J. Bacteriol , vol.190 , pp. 3505-3525
    • Baars, L.1    Wagner, S.2    Wickstrom, D.3    Klepsch, M.4
  • 14
    • 24044496176 scopus 로고    scopus 로고
    • Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth
    • Lopez-Campistrous, A., Semchuk, P., Burke, L., Palmer-Stone, T. et al., Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell. Proteomics 2005, 4, 1205-1209.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1205-1209
    • Lopez-Campistrous, A.1    Semchuk, P.2    Burke, L.3    Palmer-Stone, T.4
  • 15
    • 23344450195 scopus 로고    scopus 로고
    • Detection and identification of stable oligomeric protein complexes in Escherichia coli inner membranes: A proteomics approach
    • Spelbrink, R. E., Kolkman, A., Slijper, M., Killian, J. A., de Kruijff, B., Detection and identification of stable oligomeric protein complexes in Escherichia coli inner membranes: a proteomics approach. J. Biol. Chem. 2005, 280, 28742-28748.
    • (2005) J. Biol. Chem , vol.280 , pp. 28742-28748
    • Spelbrink, R.E.1    Kolkman, A.2    Slijper, M.3    Killian, J.A.4    de Kruijff, B.5
  • 16
    • 33847681015 scopus 로고    scopus 로고
    • Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS
    • Zhang, N., Chen, R., Young, N., Wishart, D. et al., Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 2007, 7, 484-493.
    • (2007) Proteomics , vol.7 , pp. 484-493
    • Zhang, N.1    Chen, R.2    Young, N.3    Wishart, D.4
  • 17
    • 69249222678 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Love is possible, but so difficult
    • Rabilloud, T., Membrane proteins and proteomics: love is possible, but so difficult. Electrophoresis 2009, 30 S174-S180.
    • (2009) Electrophoresis , vol.30
    • Rabilloud, T.1
  • 18
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni, V., Molloy, M., Rabilloud, T., Membrane proteins and proteomics: un amour impossible? Electrophoresis 2000, 21, 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 19
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley, D. O., Rapp, M., Granseth, E., Melen, K. et al., Global topology analysis of the Escherichia coli inner membrane proteome. Science 2005, 308, 1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4
  • 20
    • 50049087513 scopus 로고    scopus 로고
    • Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-distinct translocases and mechanisms
    • Natale, P., Bruser, T., Driessen, A. J., Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane-distinct translocases and mechanisms. Biochim. Biophys. Acta 2008, 1778, 1735-1756.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1735-1756
    • Natale, P.1    Bruser, T.2    Driessen, A.J.3
  • 21
    • 33744522928 scopus 로고    scopus 로고
    • Defining the role of the Escherichia coli chaperone SecB using comparative proteomics
    • Baars, L., Ytterberg, A. J., Drew, D., Wagner, S. et al., Defining the role of the Escherichia coli chaperone SecB using comparative proteomics. J. Biol. Chem. 2006, 281, 10024-10034.
    • (2006) J. Biol. Chem , vol.281 , pp. 10024-10034
    • Baars, L.1    Ytterberg, A.J.2    Drew, D.3    Wagner, S.4
  • 22
    • 0026644011 scopus 로고
    • DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
    • Wild, J., Altman, E., Yura, T., Gross, C. A., DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli. Genes Dev. 1992, 6, 1165-1172.
    • (1992) Genes Dev , vol.6 , pp. 1165-1172
    • Wild, J.1    Altman, E.2    Yura, T.3    Gross, C.A.4
  • 23
    • 0029893301 scopus 로고    scopus 로고
    • Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli
    • Wild, J., Rossmeissl, P., Walter, W. A., Gross, C. A., Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli. J. Bacteriol. 1996, 178, 3608-3613.
    • (1996) J. Bacteriol , vol.178 , pp. 3608-3613
    • Wild, J.1    Rossmeissl, P.2    Walter, W.A.3    Gross, C.A.4
  • 24
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: Moving folded proteins across membranes
    • Sargent, F., The twin-arginine transport system: moving folded proteins across membranes. Biochem. Soc. Trans. 2007, 35, 835-847.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 835-847
    • Sargent, F.1
  • 25
    • 34247262581 scopus 로고    scopus 로고
    • Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides
    • Tullman-Ercek, D., DeLisa, M. P., Kawarasaki, Y., Iranpour, P. et al., Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides. J. Biol. Chem. 2007, 282, 8309-8316.
    • (2007) J. Biol. Chem , vol.282 , pp. 8309-8316
    • Tullman-Ercek, D.1    DeLisa, M.P.2    Kawarasaki, Y.3    Iranpour, P.4
  • 26
    • 0026343547 scopus 로고
    • Leader peptidase
    • Dalbey, R. E., Leader peptidase. Mol. Microbiol. 1991, 5, 2855-2860.
    • (1991) Mol. Microbiol , vol.5 , pp. 2855-2860
    • Dalbey, R.E.1
  • 27
    • 0037354386 scopus 로고    scopus 로고
    • Proteomic analysis of the cell envelope fraction of Escherichia coli
    • Fountoulakis, M., Gasser, R., Proteomic analysis of the cell envelope fraction of Escherichia coli. Amino Acids 2003, 24, 19-41.
    • (2003) Amino Acids , vol.24 , pp. 19-41
    • Fountoulakis, M.1    Gasser, R.2
  • 28
    • 0038271634 scopus 로고    scopus 로고
    • Chromatographic isolation of methionine-containing peptides for gel-free proteome analysis: Identification of more than 800 Escherichia coli proteins
    • Gevaert, K., Van Damme, J., Goethals, M., Thomas, G. R. et al., Chromatographic isolation of methionine-containing peptides for gel-free proteome analysis: identification of more than 800 Escherichia coli proteins. Mol. Cell. Proteomics 2002, 1, 896-903.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 896-903
    • Gevaert, K.1    Van Damme, J.2    Goethals, M.3    Thomas, G.R.4
  • 29
    • 0041462889 scopus 로고    scopus 로고
    • Proteomic analysis of the Escherichia coli outer membrane
    • Molloy, M. P., Herbert, B. R., Slade, M. B., Rabilloud, T. et al., Proteomic analysis of the Escherichia coli outer membrane. Eur. J. Biochem. 2000, 267, 2871-2881.
    • (2000) Eur. J. Biochem , vol.267 , pp. 2871-2881
    • Molloy, M.P.1    Herbert, B.R.2    Slade, M.B.3    Rabilloud, T.4
  • 30
    • 31544443526 scopus 로고    scopus 로고
    • Escherichia coli K-12: A cooperatively developed annotation snapshot - 2005
    • Riley, M., Abe, T., Arnaud, M. B., Berlyn, M. K. et al., Escherichia coli K-12: a cooperatively developed annotation snapshot - 2005. Nucleic Acids Res. 2006, 34, 1-9.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1-9
    • Riley, M.1    Abe, T.2    Arnaud, M.B.3    Berlyn, M.K.4
  • 31
    • 37349049610 scopus 로고    scopus 로고
    • The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner
    • Vertommen, D., Depuydt, M., Pan, J., Leverrier, P. et al., The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner. Mol. Microbiol. 2008, 67, 336-349.
    • (2008) Mol. Microbiol , vol.67 , pp. 336-349
    • Vertommen, D.1    Depuydt, M.2    Pan, J.3    Leverrier, P.4
  • 32
    • 66249114348 scopus 로고    scopus 로고
    • Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics
    • Vertommen, D., Ruiz, N., Leverrier, P., Silhavy, T. J., Collet, J. F., Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics. Proteomics 2009, 9, 2432-2443.
    • (2009) Proteomics , vol.9 , pp. 2432-2443
    • Vertommen, D.1    Ruiz, N.2    Leverrier, P.3    Silhavy, T.J.4    Collet, J.F.5
  • 33
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J. C., McGovern, K., Beckwith, J., Identification of a protein required for disulfide bond formation in vivo. Cell 1991, 67, 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1    McGovern, K.2    Beckwith, J.3
  • 34
    • 49549119981 scopus 로고    scopus 로고
    • The disulfide bond formation (Dsb) system
    • Ito, K., Inaba, K., The disulfide bond formation (Dsb) system. Curr. Opin. Struct. Biol. 2008, 18, 450-458.
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 450-458
    • Ito, K.1    Inaba, K.2
  • 35
    • 33645881071 scopus 로고    scopus 로고
    • Pathways of disulfide bond formation in Escherichia coli
    • Messens, J., Collet, J. F., Pathways of disulfide bond formation in Escherichia coli. Int. J. Biochem. Cell. Biol. 2006, 38, 1050-1062.
    • (2006) Int. J. Biochem. Cell. Biol , vol.38 , pp. 1050-1062
    • Messens, J.1    Collet, J.F.2
  • 36
    • 0028948780 scopus 로고
    • Redox states of DsbA in the periplasm of Escherichia coli
    • Kishigami, S., Akiyama, Y., Ito, K., Redox states of DsbA in the periplasm of Escherichia coli. FEBS Lett. 1995, 364, 55-58.
    • (1995) FEBS Lett , vol.364 , pp. 55-58
    • Kishigami, S.1    Akiyama, Y.2    Ito, K.3
  • 37
    • 0027254133 scopus 로고
    • The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
    • Zapun, A., Bardwell, J. C., Creighton, T. E., The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo. Biochemistry 1993, 32, 5083-5092.
    • (1993) Biochemistry , vol.32 , pp. 5083-5092
    • Zapun, A.1    Bardwell, J.C.2    Creighton, T.E.3
  • 38
    • 0032943018 scopus 로고    scopus 로고
    • On the non-respect of the thermodynamic cycle by DsbA variants
    • Moutiez, M., Burova, T. V., Haertle, T., Quemeneur, E., On the non-respect of the thermodynamic cycle by DsbA variants. Protein Sci. 1999, 8, 106-112.
    • (1999) Protein Sci , vol.8 , pp. 106-112
    • Moutiez, M.1    Burova, T.V.2    Haertle, T.3    Quemeneur, E.4
  • 39
    • 41449118757 scopus 로고    scopus 로고
    • Structure and mechanisms of the DsbBDsbA disulfide bond generation machine
    • Inaba, K., Ito, K., Structure and mechanisms of the DsbBDsbA disulfide bond generation machine. Biochim. Biophys. Acta 2008, 1783, 520-529.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 520-529
    • Inaba, K.1    Ito, K.2
  • 41
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader, M., Muse, W., Ballou, D. P., Gassner, C., Bardwell, J. C., Oxidative protein folding is driven by the electron transport system. Cell 1999, 98, 217-227.
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1    Muse, W.2    Ballou, D.P.3    Gassner, C.4    Bardwell, J.C.5
  • 42
    • 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., Martin, N. L., Beckwith, J., Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation. EMBO J. 1994, 13, 5121-5127.
    • (1994) EMBO J , vol.13 , pp. 5121-5127
    • Jander, G.1    Martin, N.L.2    Beckwith, J.3
  • 43
    • 8744256714 scopus 로고    scopus 로고
    • Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli
    • Takahashi, Y. H., Inaba, K., Ito, K., Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli. J. Biol. Chem. 2004, 279, 47057-47065.
    • (2004) J. Biol. Chem , vol.279 , pp. 47057-47065
    • Takahashi, Y.H.1    Inaba, K.2    Ito, K.3
  • 44
    • 0031010755 scopus 로고    scopus 로고
    • The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding
    • Guddat, L. W., Bardwell, J. C., Zander, T., Martin, J. L., The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding. Protein Sci. 1997, 6, 1148-1156.
    • (1997) Protein Sci , vol.6 , pp. 1148-1156
    • Guddat, L.W.1    Bardwell, J.C.2    Zander, T.3    Martin, J.L.4
  • 45
    • 50149109183 scopus 로고    scopus 로고
    • Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation
    • Dutton, R. J., Boyd, D., Berkmen, M., Beckwith, J., Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. Proc. Natl. Acad. Sci. USA 2008, 105, 11933-11938.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11933-11938
    • Dutton, R.J.1    Boyd, D.2    Berkmen, M.3    Beckwith, J.4
  • 46
    • 1642556877 scopus 로고    scopus 로고
    • Snapshots of DsbA in action: Detection of proteins in the process of oxidative folding
    • Kadokura, H., Tian, H., Zander, T., Bardwell, J. C., Beckwith, J., Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science 2004, 303, 534-537.
    • (2004) Science , vol.303 , pp. 534-537
    • Kadokura, H.1    Tian, H.2    Zander, T.3    Bardwell, J.C.4    Beckwith, J.5
  • 47
    • 4744363388 scopus 로고    scopus 로고
    • Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis
    • Brennan, J. P., Wait, R., Begum, S., Bell, J. R. et al., Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis. J. Biol. Chem. 2004, 279, 41352-41360.
    • (2004) J. Biol. Chem , vol.279 , pp. 41352-41360
    • Brennan, J.P.1    Wait, R.2    Begum, S.3    Bell, J.R.4
  • 48
    • 66149109179 scopus 로고    scopus 로고
    • Diagonal electrophoresis for detection of protein disulphide bridges
    • McDonagh, B., Diagonal electrophoresis for detection of protein disulphide bridges. Methods Mol. Biol. 2009, 519, 305-310.
    • (2009) Methods Mol. Biol , vol.519 , pp. 305-310
    • McDonagh, B.1
  • 49
    • 1842477219 scopus 로고    scopus 로고
    • In vivo substrate specificity of periplasmic disulfide oxidoreductases
    • Hiniker, A., Bardwell, J. C., In vivo substrate specificity of periplasmic disulfide oxidoreductases. J. Biol. Chem. 2004, 279, 12967-12973.
    • (2004) J. Biol. Chem , vol.279 , pp. 12967-12973
    • Hiniker, A.1    Bardwell, J.C.2
  • 50
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert, L. I., Jakob, U., Protein thiol modifications visualized in vivo. PLoS Biol. 2004, 2, 1723-1737.
    • (2004) PLoS Biol , vol.2 , pp. 1723-1737
    • Leichert, L.I.1    Jakob, U.2
  • 51
    • 43849099548 scopus 로고    scopus 로고
    • Overproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: Disulfide oxidoreductase DsbA
    • Onder, O., Turkarslan, S., Sun, D., Daldal, F., Overproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: disulfide oxidoreductase DsbA. Mol. Cell. Proteomics 2008, 7, 875-890.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 875-890
    • Onder, O.1    Turkarslan, S.2    Sun, D.3    Daldal, F.4
  • 52
    • 35748965031 scopus 로고    scopus 로고
    • The oxidase DsbA folds a protein with a nonconsecutive disulfide
    • Messens, J., Collet, J. F., Van Belle, K., Brosens, E. et al., The oxidase DsbA folds a protein with a nonconsecutive disulfide. J. Biol. Chem. 2007, 282, 31302-31307.
    • (2007) J. Biol. Chem , vol.282 , pp. 31302-31307
    • Messens, J.1    Collet, J.F.2    Van Belle, K.3    Brosens, E.4
  • 53
    • 0033230589 scopus 로고    scopus 로고
    • Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
    • Stewart, E. J., Katzen, F., Beckwith, J., Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. EMBO J. 1999, 18, 5963-5971.
    • (1999) EMBO J , vol.18 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 54
    • 0037178798 scopus 로고    scopus 로고
    • Reconstitution of a disulfide isomerization system
    • Collet, J. F., Riemer, J., Bader, M. W., Bardwell, J. C., Reconstitution of a disulfide isomerization system. J. Biol. Chem. 2002, 277, 26886-26892.
    • (2002) J. Biol. Chem , vol.277 , pp. 26886-26892
    • Collet, J.F.1    Riemer, J.2    Bader, M.W.3    Bardwell, J.C.4
  • 55
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen, F., Beckwith, J., Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 2000, 103, 769-779.
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 56
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch, A., Bessette, P., Georgiou, G., Beckwith, J., Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 1997, 179, 6602-6608.
    • (1997) J. Bacteriol , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 57
    • 0031919407 scopus 로고    scopus 로고
    • The activesite cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo
    • Fabianek, R. A., Hennecke, H., Thony-Meyer, L., The activesite cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo. J. Bacteriol. 1998, 180, 1947-1950.
    • (1998) J. Bacteriol , vol.180 , pp. 1947-1950
    • Fabianek, R.A.1    Hennecke, H.2    Thony-Meyer, L.3
  • 58
    • 0033583239 scopus 로고    scopus 로고
    • In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG
    • Bessette, P. H., Cotto, J. J., Gilbert, H. F., Georgiou, G., In vivo and in vitro function of the Escherichia coli periplasmic cysteine oxidoreductase DsbG. J. Biol. Chem. 1999, 274, 7784-7792.
    • (1999) J. Biol. Chem , vol.274 , pp. 7784-7792
    • Bessette, P.H.1    Cotto, J.J.2    Gilbert, H.F.3    Georgiou, G.4
  • 59
    • 70450160847 scopus 로고    scopus 로고
    • A periplasmic reducing system protects single cysteine residues from oxidation
    • Depuydt, M., Leonard, S. E., Vertommen, D., Denoncin, K. et al., A periplasmic reducing system protects single cysteine residues from oxidation. Science 2009, 326, 1109-1111.
    • (2009) Science , vol.326 , pp. 1109-1111
    • Depuydt, M.1    Leonard, S.E.2    Vertommen, D.3    Denoncin, K.4
  • 60
    • 15744375548 scopus 로고    scopus 로고
    • The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC
    • Berkmen, M., Boyd, D., Beckwith, J., The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC. J. Biol. Chem. 2005, 280, 11387-11394.
    • (2005) J. Biol. Chem , vol.280 , pp. 11387-11394
    • Berkmen, M.1    Boyd, D.2    Beckwith, J.3
  • 61
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • Gothel, S. F., Marahiel, M. A., Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell. Mol. Life Sci. 1999, 55, 423-436.
    • (1999) Cell. Mol. Life Sci , vol.55 , pp. 423-436
    • Gothel, S.F.1    Marahiel, M.A.2
  • 62
    • 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., Walsh, C. T., Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A. Proc. Natl. Acad. Sci. USA 1990, 87, 4028-4032.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4028-4032
    • Liu, J.1    Walsh, C.T.2
  • 63
    • 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., Young, K. D., Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins. Arch. Microbiol. 1995, 163, 357-365.
    • (1995) Arch. Microbiol , vol.163 , pp. 357-365
    • Horne, S.M.1    Young, K.D.2
  • 64
    • 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., A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J. 1998, 17, 3968-3980.
    • (1998) EMBO J , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 65
    • 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., Gross, C. A., SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 1996, 10, 3170-3182.
    • (1996) Genes Dev , vol.10 , pp. 3170-3182
    • Rouviere, P.E.1    Gross, C.A.2
  • 66
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arie, J. P., Sassoon, N., Betton, J. M., Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 2001, 39, 199-210.
    • (2001) Mol. Microbiol , vol.39 , pp. 199-210
    • Arie, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 67
    • 27744565064 scopus 로고    scopus 로고
    • Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
    • Justice, S. S., Hunstad, D. A., Harper, J. R., Duguay, A. R. et al., Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J. Bacteriol. 2005, 187, 7680-7686.
    • (2005) J. Bacteriol , vol.187 , pp. 7680-7686
    • Justice, S.S.1    Hunstad, D.A.2    Harper, J.R.3    Duguay, A.R.4
  • 68
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M., Tommassen, J., Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 2003, 299, 262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 69
    • 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., YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol. Microbiol. 2005, 57, 1450-1459.
    • (2005) Mol. Microbiol , vol.57 , pp. 1450-1459
    • Werner, J.1    Misra, R.2
  • 70
    • 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. et al., Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 2005, 121, 235-245.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4
  • 71
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: The role of the BAM complex in outer membrane protein assembly
    • Knowles, T. J., Scott-Tucker, A., Overduin, M., Henderson, I. R., Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat. Rev. Microbiol. 2009, 7, 206-214.
    • (2009) Nat. Rev. Microbiol , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 72
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial outer membrane
    • Bos, M. P., Robert, V., Tommassen, J., Biogenesis of the gram-negative bacterial outer membrane. Annu. Rev. Microbiol. 2007, 61, 191-214.
    • (2007) Annu. Rev. Microbiol , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 73
    • 0025309069 scopus 로고
    • surA, an Escherichia coli gene essential for survival in stationary phase
    • Tormo, A., Almiron, M., Kolter, R., surA, an Escherichia coli gene essential for survival in stationary phase. J. Bacteriol. 1990, 172, 4339-4347.
    • (1990) J. Bacteriol , vol.172 , pp. 4339-4347
    • Tormo, A.1    Almiron, M.2    Kolter, R.3
  • 74
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas, D., Betton, J. M., Raina, S., New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol. Microbiol. 1996, 21, 871-884.
    • (1996) Mol. Microbiol , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 75
    • 2442563573 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli sigma-dependent envelope stress response
    • Alba, B. M., Gross, C. A., Regulation of the Escherichia coli sigma-dependent envelope stress response. Mol. Microbiol. 2004, 52, 613-619.
    • (2004) Mol. Microbiol , vol.52 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 76
    • 56949096401 scopus 로고    scopus 로고
    • Regulation by destruction: Design of the sigmaE envelope stress response
    • Ades, S. E., Regulation by destruction: design of the sigmaE envelope stress response. Curr. Opin. Microbiol. 2008, 11, 535-540.
    • (2008) Curr. Opin. Microbiol , vol.11 , pp. 535-540
    • Ades, S.E.1
  • 77
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens, S., Maier, R., de Cock, H., Schmid, F. X., Gross, C. A., The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 2001, 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
  • 78
    • 0036849659 scopus 로고    scopus 로고
    • Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins
    • Bitto, E., McKay, D. B., Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure 2002, 10, 1489-1498.
    • (2002) Structure , vol.10 , pp. 1489-1498
    • Bitto, E.1    McKay, D.B.2
  • 79
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S. W., Kolter, R., SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 1996, 178, 1770-1773.
    • (1996) J. Bacteriol , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 80
    • 17444392068 scopus 로고    scopus 로고
    • Characterization of six lipoproteins in the sigmaE regulon
    • Onufryk, C., Crouch, M. L., Fang, F. C., Gross, C. A., Characterization of six lipoproteins in the sigmaE regulon. J. Bacteriol. 2005, 187, 4552-4561.
    • (2005) J. Bacteriol , vol.187 , pp. 4552-4561
    • Onufryk, C.1    Crouch, M.L.2    Fang, F.C.3    Gross, C.A.4
  • 81
    • 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., Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev. 2007, 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
  • 82
    • 1542571983 scopus 로고    scopus 로고
    • The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins
    • Bitto, E., McKay, D. B., The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins. J. Biol. Chem. 2003, 278, 49316-49322.
    • (2003) J. Biol. Chem , vol.278 , pp. 49316-49322
    • Bitto, E.1    McKay, D.B.2
  • 83
    • 60549101514 scopus 로고    scopus 로고
    • The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
    • Walton, T. A., Sandoval, C. M., Fowler, C. A., Pardi, A., Sousa, M. C., The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc. Natl. Acad. Sci. USA 2009, 106, 1772-1777.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1772-1777
    • Walton, T.A.1    Sandoval, C.M.2    Fowler, C.A.3    Pardi, A.4    Sousa, M.C.5
  • 84
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • Walton, T. A., Sousa, M. C., Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell 2004, 15, 367-374.
    • (2004) Mol. Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 85
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen, R., Henning, U., A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol. Microbiol. 1996, 19, 1287-1294.
    • (1996) Mol. Microbiol , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 86
    • 0035374452 scopus 로고    scopus 로고
    • The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane
    • Harms, N., Koningstein, G., Dontje, W., Muller, M. et al., The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J. Biol. Chem. 2001, 276, 18804-18811.
    • (2001) J. Biol. Chem , vol.276 , pp. 18804-18811
    • Harms, N.1    Koningstein, G.2    Dontje, W.3    Muller, M.4
  • 87
    • 35348966245 scopus 로고    scopus 로고
    • The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions
    • Qu, J., Mayer, C., Behrens, S., Holst, O., Kleinschmidt, J. H., The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions. J. Mol. Biol. 2007, 374, 91-105.
    • (2007) J. Mol. Biol , vol.374 , pp. 91-105
    • Qu, J.1    Mayer, C.2    Behrens, S.3    Holst, O.4    Kleinschmidt, J.H.5
  • 88
    • 0038105593 scopus 로고    scopus 로고
    • Schafer, U., Beck, K., Muller, M., Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 1999, 274, 24567-24574.
    • Schafer, U., Beck, K., Muller, M., Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 1999, 274, 24567-24574.
  • 89
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • Bulieris, P. V., Behrens, S., Holst, O., Kleinschmidt, J. H., Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 2003, 278, 9092-9099.
    • (2003) J. Biol. Chem , vol.278 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 90
    • 57649242773 scopus 로고    scopus 로고
    • Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp
    • Jarchow, S., Luck, C., Gorg, A., Skerra, A., Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp. Proteomics 2008, 8, 4987-4994.
    • (2008) Proteomics , vol.8 , pp. 4987-4994
    • Jarchow, S.1    Luck, C.2    Gorg, A.3    Skerra, A.4
  • 91
    • 40549093296 scopus 로고    scopus 로고
    • Proteomic analysis of heatstable proteins in
    • Kwon, S., Jung, Y., Lim, D., Proteomic analysis of heatstable proteins in Escherichia coli. BMB Rep. 2008, 41, 108-111.
    • (2008) Escherichia coli. BMB Rep , vol.41 , pp. 108-111
    • Kwon, S.1    Jung, Y.2    Lim, D.3
  • 92
    • 10744219572 scopus 로고    scopus 로고
    • Production of soluble and functional engineered antibodies in Escherichia coli improved by FkpA
    • 1032-1038
    • Zhang, Z., Song, L. P., Fang, M., Wang, F. et al., Production of soluble and functional engineered antibodies in Escherichia coli improved by FkpA. Biotechniques 2003, 35, 1032-1038, 1041-1032.
    • (2003) Biotechniques , vol.35 , pp. 1041-1032
    • Zhang, Z.1    Song, L.P.2    Fang, M.3    Wang, F.4
  • 93
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • Hullmann, J., Patzer, S. I., Romer, C., Hantke, K., Braun, V., Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol. Microbiol. 2008, 69, 926-937.
    • (2008) Mol. Microbiol , vol.69 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Romer, C.3    Hantke, K.4    Braun, V.5
  • 94
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • Saul, F. A., Arie, J. P., Vulliez-le Normand, B., Kahn, R. et al., Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 2004, 335, 595-608.
    • (2004) J. Mol. Biol , vol.335 , pp. 595-608
    • Saul, F.A.1    Arie, J.P.2    Vulliez-le Normand, B.3    Kahn, R.4
  • 95
    • 0025317783 scopus 로고
    • The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase
    • Lipinska, B., Zylicz, M., Georgopoulos, C., The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J. Bacteriol. 1990, 172, 1791-1797.
    • (1990) J. Bacteriol , vol.172 , pp. 1791-1797
    • Lipinska, B.1    Zylicz, M.2    Georgopoulos, C.3
  • 96
    • 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., Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J. Bacteriol. 1989, 171, 2689-2696.
    • (1989) J. Bacteriol , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 97
    • 0034797891 scopus 로고    scopus 로고
    • Efficient export of alkaline phosphatase overexpressed from a multicopy plasmid requires degP, a gene encoding a periplasmic protease of Escherichia coli
    • Kadokura, H., Kawasaki, H., Yoda, K., Yamasaki, M., Kitamoto, K., Efficient export of alkaline phosphatase overexpressed from a multicopy plasmid requires degP, a gene encoding a periplasmic protease of Escherichia coli. J. Gen. Appl. Microbiol. 2001, 47, 133-141.
    • (2001) J. Gen. Appl. Microbiol , vol.47 , pp. 133-141
    • Kadokura, H.1    Kawasaki, H.2    Yoda, K.3    Yamasaki, M.4    Kitamoto, K.5
  • 98
    • 0036786221 scopus 로고    scopus 로고
    • Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: The PapA pilin
    • Jones, C. H., Dexter, P., Evans, A. K., Liu, C. et al., Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin. J. Bacteriol. 2002, 184, 5762-5771.
    • (2002) J. Bacteriol , vol.184 , pp. 5762-5771
    • Jones, C.H.1    Dexter, P.2    Evans, A.K.3    Liu, C.4
  • 99
    • 0024457020 scopus 로고
    • The acylated precursor form of the colicin A lysis protein is a natural substrate of the DegP protease
    • Cavard, D., Lazdunski, C., Howard, S. P., The acylated precursor form of the colicin A lysis protein is a natural substrate of the DegP protease. J. Bacteriol. 1989, 171, 6316-6322.
    • (1989) J. Bacteriol , vol.171 , pp. 6316-6322
    • Cavard, D.1    Lazdunski, C.2    Howard, S.P.3
  • 100
    • 34447644224 scopus 로고    scopus 로고
    • Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock
    • Skorko-Glonek, J., Laskowska, E., Sobiecka-Szkatula, A., Lipinska, B., Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock. Arch. Biochem. Biophys. 2007, 464, 80-89.
    • (2007) Arch. Biochem. Biophys , vol.464 , pp. 80-89
    • Skorko-Glonek, J.1    Laskowska, E.2    Sobiecka-Szkatula, A.3    Lipinska, B.4
  • 101
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer, T., Sawa, J., Schafer, E., Saibil, H. R. et al., Structural basis for the regulated protease and chaperone function of DegP. Nature 2008, 453, 885-890.
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4
  • 102
    • 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., The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP. Proc. Natl. Acad. Sci. USA 2005, 102, 17775-17779.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17775-17779
    • Isaac, D.D.1    Pinkner, J.S.2    Hultgren, S.J.3    Silhavy, T.J.4
  • 103
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M., Clausen, T., Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 2002, 416, 455-459.
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 104
    • 50149107174 scopus 로고    scopus 로고
    • Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins
    • Jiang, J., Zhang, X., Chen, Y., Wu, Y. et al., Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proc. Natl. Acad. Sci. USA 2008, 105, 11939-11944.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11939-11944
    • Jiang, J.1    Zhang, X.2    Chen, Y.3    Wu, Y.4
  • 105
    • 2342660218 scopus 로고    scopus 로고
    • Genome-wide analysis of lipoprotein expression in Escherichia coli MG1655
    • Brokx, S. J., Ellison, M., Locke, T., Bottorff, D. et al., Genome-wide analysis of lipoprotein expression in Escherichia coli MG1655. J. Bacteriol. 2004, 186, 3254-3258.
    • (2004) J. Bacteriol , vol.186 , pp. 3254-3258
    • Brokx, S.J.1    Ellison, M.2    Locke, T.3    Bottorff, D.4
  • 106
    • 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., Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm. J. Biol. Chem. 2004, 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
  • 107
    • 3242743729 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda, H., Matsuyama, S., Sorting of lipoproteins to the outer membrane in E. coli. Biochim. Biophys. Acta 2004, 1693, 5-13.
    • (2004) Biochim. Biophys. Acta , vol.1693 , pp. 5-13
    • Tokuda, H.1    Matsuyama, S.2
  • 108
    • 65249085615 scopus 로고    scopus 로고
    • Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB
    • Okuda, S., Tokuda, H., Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB. Proc. Natl. Acad. Sci. USA 2009, 106, 5877-5882.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 109
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi, T., Masuda, K., Narita, S., Matsuyama, S., Tokuda, H., A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat. Cell Biol. 2000, 2, 212-218.
    • (2000) Nat. Cell Biol , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 110
    • 0038602740 scopus 로고    scopus 로고
    • Crystal structures of bacterial lipoprotein localization factors, LolA and LolB
    • Takeda, K., Miyatake, H., Yokota, N., Matsuyama, S. et al., Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. EMBO J. 2003, 22, 3199-3209.
    • (2003) EMBO J , vol.22 , pp. 3199-3209
    • Takeda, K.1    Miyatake, H.2    Yokota, N.3    Matsuyama, S.4
  • 111
    • 36448995763 scopus 로고    scopus 로고
    • Largescale preparation of the homogeneous LolA lipoprotein complex and efficient in vitro transfer of lipoproteins to the outer membrane in a LolB-dependent manner
    • Watanabe, S., Oguchi, Y., Yokota, N., Tokuda, H., Largescale preparation of the homogeneous LolA lipoprotein complex and efficient in vitro transfer of lipoproteins to the outer membrane in a LolB-dependent manner. Protein Sci. 2007, 16, 2741-2749.
    • (2007) Protein Sci , vol.16 , pp. 2741-2749
    • Watanabe, S.1    Oguchi, Y.2    Yokota, N.3    Tokuda, H.4
  • 112
    • 54449093948 scopus 로고    scopus 로고
    • Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA
    • Watanabe, S., Oguchi, Y., Takeda, K., Miki, K., Tokuda, H., Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA. J. Biol. Chem. 2008, 283, 25421-25427.
    • (2008) J. Biol. Chem , vol.283 , pp. 25421-25427
    • Watanabe, S.1    Oguchi, Y.2    Takeda, K.3    Miki, K.4    Tokuda, H.5
  • 113
    • 0034051753 scopus 로고    scopus 로고
    • Assembly of complex organelles: Pilus biogenesis in Gram-negative bacteria as a model system
    • Thanassi, D. G., Hultgren, S. J., Assembly of complex organelles: pilus biogenesis in Gram-negative bacteria as a model system. Methods 2000, 20, 111-126.
    • (2000) Methods , vol.20 , pp. 111-126
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 114
    • 60149111839 scopus 로고    scopus 로고
    • Pili in Gram-negative and Grampositive bacteria - structure, assembly and their role in disease
    • Proft, T., Baker, E. N., Pili in Gram-negative and Grampositive bacteria - structure, assembly and their role in disease. Cell Mol. Life Sci. 2009, 66, 613-635.
    • (2009) Cell Mol. Life Sci , vol.66 , pp. 613-635
    • Proft, T.1    Baker, E.N.2
  • 115
    • 0033551911 scopus 로고    scopus 로고
    • X-ray structure of the FimC-FimH chaperoneadhesin complex from uropathogenic Escherichia coli
    • Choudhury, D., Thompson, A., Stojanoff, V., Langermann, S. et al., X-ray structure of the FimC-FimH chaperoneadhesin complex from uropathogenic Escherichia coli. Science 1999, 285, 1061-1066.
    • (1999) Science , vol.285 , pp. 1061-1066
    • Choudhury, D.1    Thompson, A.2    Stojanoff, V.3    Langermann, S.4
  • 116
    • 0039843096 scopus 로고    scopus 로고
    • Structural basis of chaperone function and pilus biogenesis
    • Sauer, F. G., Futterer, K., Pinkner, J. S., Dodson, K. W. et al., Structural basis of chaperone function and pilus biogenesis. Science 1999, 285, 1058-1061.
    • (1999) Science , vol.285 , pp. 1058-1061
    • Sauer, F.G.1    Futterer, K.2    Pinkner, J.S.3    Dodson, K.W.4
  • 117
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • Sauer, F. G., Pinkner, J. S., Waksman, G., Hultgren, S. J., Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell 2002, 111, 543-551.
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 118
    • 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., Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J. Bacteriol. 2001, 183, 6794-6800.
    • (2001) J. Bacteriol , vol.183 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 119
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between folding factors and bacterial outer membrane proteins
    • Mogensen, J. E., Otzen, D. E., Interactions between folding factors and bacterial outer membrane proteins. Mol. Microbiol. 2005, 57, 326-346.
    • (2005) Mol. Microbiol , vol.57 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 120
    • 33749846008 scopus 로고    scopus 로고
    • Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli
    • Skorko-Glonek, J., Sobiecka-Szkatula, A., Lipinska, B., Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli. Acta Biochim. Pol. 2006, 53, 585-589.
    • (2006) Acta Biochim. Pol , vol.53 , pp. 585-589
    • Skorko-Glonek, J.1    Sobiecka-Szkatula, A.2    Lipinska, B.3


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