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Volumn 195, Issue 16, 2013, Pages 3734-3742

Role for Skp in LptD assembly in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; OUTER MEMBRANE PROTEIN; PROTEIN LPTD; S PHASE KINASE ASSOCIATED PROTEIN; UNCLASSIFIED DRUG;

EID: 84880965951     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00431-13     Document Type: Article
Times cited : (42)

References (54)
  • 2
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality: a genetic strategy to probe organelle assembly
    • Ruiz N, Falcone B, Kahne D, Silhavy TJ. 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
  • 3
    • 0024690869 scopus 로고
    • Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability
    • Sampson BA, Misra R, Benson SA. 1989. Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability. Genetics 122:491-501.
    • (1989) Genetics , vol.122 , pp. 491-501
    • Sampson, B.A.1    Misra, R.2    Benson, S.A.3
  • 4
    • 0036046150 scopus 로고    scopus 로고
    • Imp/OstA is required for cell envelope biogenesis in Escherichia coli
    • Braun M, Silhavy TJ. 2002. Imp/OstA is required for cell envelope biogenesis in Escherichia coli. Mol. Microbiol. 45:1289-1302.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1289-1302
    • Braun, M.1    Silhavy, T.J.2
  • 5
    • 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 TJ, 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
  • 8
    • 77950438894 scopus 로고    scopus 로고
    • Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane
    • Chng S-S, Ruiz N, Chimalakonda G, Silhavy TJ, Kahne D. 2010. Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane. Proc. Natl. Acad. Sci. U. S. A. 107:5363-5368.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 5363-5368
    • Chng, S.-S.1    Ruiz, N.2    Chimalakonda, G.3    Silhavy, T.J.4    Kahne, D.5
  • 9
    • 77955463665 scopus 로고    scopus 로고
    • Nonconsecutive disulfide bond formation in an essential integral outer membrane protein
    • Ruiz N, Chng S-S, Hiniker A, Kahne D, Silhavy TJ. 2010. Nonconsecutive disulfide bond formation in an essential integral outer membrane protein. Proc. Natl. Acad. Sci. U. S. A. 107:12245-12250.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 12245-12250
    • Ruiz, N.1    Chng, S.-S.2    Hiniker, A.3    Kahne, D.4    Silhavy, T.J.5
  • 10
    • 79952300098 scopus 로고    scopus 로고
    • Lipoprotein LptE is required for the assembly of LptD by the β-barrel assembly machine in the outer membrane of Escherichia coli
    • Chimalakonda G, Ruiz N, Chng S-S, Garner RA, Kahne D, Silhavy TJ. 2011. Lipoprotein LptE is required for the assembly of LptD by the β-barrel assembly machine in the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 108:2492-2497.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 2492-2497
    • Chimalakonda, G.1    Ruiz, N.2    Chng, S.-S.3    Garner, R.A.4    Kahne, D.5    Silhavy, T.J.6
  • 11
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • Sklar JG, Wu T, Kahne D, Silhavy TJ. 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
  • 12
    • 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 TJ, Collet J. 2009. Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics. Proteomics 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.5
  • 13
    • 0035877593 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli sigma E regulon
    • Dartigalongue C, Missiakas D, Raina S. 2001. Characterization of the Escherichia coli sigma E regulon. J. Biol. Chem. 276:20866-20875.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20866-20875
    • Dartigalongue, C.1    Missiakas, D.2    Raina, S.3
  • 14
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • Rizzitello AE, Harper JR, Silhavy TJ. 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
  • 15
    • 84861172996 scopus 로고    scopus 로고
    • Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics
    • Denoncin K, Schwalm J, Vertommen D, Silhavy TJ, Collet J-F. 2012. Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics. Proteomics 12:1391-1401.
    • (2012) Proteomics , vol.12 , pp. 1391-1401
    • Denoncin, K.1    Schwalm, J.2    Vertommen, D.3    Silhavy, T.J.4    Collet, J.-F.5
  • 16
    • 0023663637 scopus 로고
    • Purification and characterization of the 17 K protein, a DNA-binding protein from Escherichia coli
    • Holck A, Lossius I, Aasland R, Kleppe K. 1987. Purification and characterization of the 17 K protein, a DNA-binding protein from Escherichia coli. Biochim. Biophys. Acta 914:49-54.
    • (1987) Biochim. Biophys. Acta , vol.914 , pp. 49-54
    • Holck, A.1    Lossius, I.2    Aasland, R.3    Kleppe, K.4
  • 17
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen R, Henning U. 1996. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol. Microbiol. 19: 1287-1294.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 18
    • 57649242773 scopus 로고    scopus 로고
    • Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp
    • Jarchow S, Lück C, Görg A, Skerra A. 2008. Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp. Proteomics 8:4987-4994.
    • (2008) Proteomics , vol.8 , pp. 4987-4994
    • Jarchow, S.1    Lück, C.2    Görg, A.3    Skerra, A.4
  • 19
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • Walton TA, Sousa MC. 2004. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell 15:367-374.
    • (2004) Mol. Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 20
    • 0033556141 scopus 로고    scopus 로고
    • Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein.
    • De Cock H, Schäfer U, Potgeter M, Demel R, Müller M, Tommassen J. 1999. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur. J. Biochem. 259:96-103.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 96-103
    • De Cock, H.1    Schäfer, U.2    Potgeter, M.3    Demel, R.4    Müller, M.5    Tommassen, J.6
  • 21
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of Gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schäfer U, Beck K, Müller M. 1999. Skp, a molecular chaperone of Gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274:24567-24574.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schäfer, U.1    Beck, K.2    Müller, M.3
  • 22
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • Bulieris PV, Behrens S, Holst O, Kleinschmidt JH. 2003. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 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
  • 23
    • 60549101514 scopus 로고    scopus 로고
    • The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
    • Walton TA, Sandoval CM, Fowler CA, Pardi A, Sousa MC. 2009. The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc. Natl. Acad. Sci. U. S. A. 106:1772-1777.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 1772-1777
    • Walton, T.A.1    Sandoval, C.M.2    Fowler, C.A.3    Pardi, A.4    Sousa, M.C.5
  • 24
    • 79961225871 scopus 로고    scopus 로고
    • Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain
    • Ieva R, Tian P, Peterson JH, Bernstein HD. 2011. Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain. Proc. Natl. Acad. Sci. U. S. A. 108:E383-E391.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108
    • Ieva, R.1    Tian, P.2    Peterson, J.H.3    Bernstein, H.D.4
  • 25
    • 73149118024 scopus 로고    scopus 로고
    • Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane
    • Ieva R, Bernstein HD. 2009. Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane. Proc. Natl. Acad. Sci. U. S. A. 106:19120-19125.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 19120-19125
    • Ieva, R.1    Bernstein, H.D.2
  • 26
    • 79952789687 scopus 로고    scopus 로고
    • Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis
    • Volokhina EB, Grijpstra J, Stork M, Schilders I, Tommassen J, Bos MP. 2011. Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis. J. Bacteriol. 193: 1612-1621.
    • (2011) J. Bacteriol. , vol.193 , pp. 1612-1621
    • Volokhina, E.B.1    Grijpstra, J.2    Stork, M.3    Schilders, I.4    Tommassen, J.5    Bos, M.P.6
  • 27
    • 60649107938 scopus 로고    scopus 로고
    • Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri
    • Wagner JK, Heindl JE, Gray AN, Jain S, Goldberg MB. 2009. Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri. J. Bacteriol. 191: 815-821.
    • (2009) J. Bacteriol. , vol.191 , pp. 815-821
    • Wagner, J.K.1    Heindl, J.E.2    Gray, A.N.3    Jain, S.4    Goldberg, M.B.5
  • 29
    • 77950630983 scopus 로고    scopus 로고
    • Co-expression of Skp and FkpA chaperones improves cell viability and alters the global expression of stress response genes during scFvD1.3 production
    • Ow DS-W, Lim DY-X, Nissom PM, Camattari A, Wong VV-T. 2010. Co-expression of Skp and FkpA chaperones improves cell viability and alters the global expression of stress response genes during scFvD1.3 production. Microb. Cell Fact. 9:22.
    • (2010) Microb. Cell Fact. , vol.9 , pp. 22
    • Ow, D.S.-W.1    Lim, D.Y.-X.2    Nissom, P.M.3    Camattari, A.4    Wong, V.V.-T.5
  • 30
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • Saul FA, Arié J-P, Vulliez-le Normand B, Kahn R, Betton J-M, Bentley GA. 2004. Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335:595-608.
    • (2004) J. Mol. Biol. , vol.335 , pp. 595-608
    • Saul, F.A.1    Arié, J.-P.2    Vulliez-le Normand, B.3    Kahn, R.4    Betton, J.-M.5    Bentley, G.A.6
  • 32
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • Hullmann J, Patzer SI, Römer C, Hantke K, Braun V. 2008. Periplasmic chaperone FkpA is essential for imported colicin M toxicity. Mol. Microbiol. 69:926-937.
    • (2008) Mol. Microbiol. , vol.69 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Römer, C.3    Hantke, K.4    Braun, V.5
  • 35
    • 77957678381 scopus 로고    scopus 로고
    • Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein
    • Ruiz-Perez F, Henderson IR, Nataro JP. 2010. Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein. Gut Microbes 1:339-344.
    • (2010) Gut Microbes , vol.1 , pp. 339-344
    • Ruiz-Perez, F.1    Henderson, I.R.2    Nataro, J.P.3
  • 36
    • 3142680440 scopus 로고    scopus 로고
    • Structural tolerance of bacterial autotransporters for folded passenger protein domains
    • Veiga E, de Lorenzo V, Fernández LA. 2004. Structural tolerance of bacterial autotransporters for folded passenger protein domains. Mol. Microbiol. 52:1069-1080.
    • (2004) Mol. Microbiol. , vol.52 , pp. 1069-1080
    • Veiga, E.1    de Lorenzo, V.2    Fernández, L.A.3
  • 39
    • 0029065955 scopus 로고
    • Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant
    • Cherepanov PP, Wackernagel W. 1995. Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 41
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli
    • Amann E, Ochs B, Abel KJ. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.J.3
  • 43
    • 77956276068 scopus 로고    scopus 로고
    • Staining proteins in gels with Coomassie blue
    • pdbprot4719
    • Simpson RJ. 2007. Staining proteins in gels with Coomassie blue. Cold Spring Harb. Protoc. 2007:pdb.prot4719.
    • (2007) Cold Spring Harb. Protoc. , vol.2007
    • Simpson, R.J.1
  • 44
    • 0024519269 scopus 로고
    • Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures
    • Lipinska B, Fayet O, Baird L, Georgopoulos C. 1989. Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J. Bacteriol. 171:1574-1584.
    • (1989) J. Bacteriol. , vol.171 , pp. 1574-1584
    • Lipinska, B.1    Fayet, O.2    Baird, L.3    Georgopoulos, C.4
  • 45
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess C, Beil A, Ehrmann M. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 46
    • 33749593869 scopus 로고    scopus 로고
    • Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide
    • Charlson ES, Werner JN, Misra R. 2006. Differential effects of yfgL mutation on 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
  • 47
    • 33846234653 scopus 로고    scopus 로고
    • 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
    • Ureta AR, Endres RG, Wingreen NS, Silhavy TJ. 2007. 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. J. Bacteriol. 189:446-454.
    • (2007) J. Bacteriol. , vol.189 , pp. 446-454
    • Ureta, A.R.1    Endres, R.G.2    Wingreen, N.S.3    Silhavy, T.J.4
  • 48
    • 0033535603 scopus 로고    scopus 로고
    • Membrane proteins: a tale of barrels and corks
    • Sansom MS. 1999. Membrane proteins: a tale of barrels and corks. Curr. Biol. 9:R254-R257.
    • (1999) Curr. Biol. , vol.9
    • Sansom, M.S.1
  • 49
    • 0036033555 scopus 로고    scopus 로고
    • A third envelope stress signal transduction pathway in Escherichia coli
    • Raffa RG, Raivio TL. 2002. A third envelope stress signal transduction pathway in Escherichia coli. Mol. Microbiol. 45:1599-1611.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1599-1611
    • Raffa, R.G.1    Raivio, T.L.2
  • 50
    • 79959326633 scopus 로고    scopus 로고
    • Characterization of the induction and cellular role of the BaeSR two-component envelope stress response of Escherichia coli
    • Leblanc SKD, Oates CW, Raivio TL. 2011. Characterization of the induction and cellular role of the BaeSR two-component envelope stress response of Escherichia coli. J. Bacteriol. 193:3367-3375.
    • (2011) J. Bacteriol. , vol.193 , pp. 3367-3375
    • Leblanc, S.K.D.1    Oates, C.W.2    Raivio, T.L.3
  • 51
    • 0030834844 scopus 로고    scopus 로고
    • Transduction of envelope stress in Escherichia coli by the Cpx two-component system
    • Raivio TL, Silhavy TJ. 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
  • 52
    • 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, Oudega B, Luirink J, de Cock H. 2001. The early interaction of the outer membrane protein Phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J. Biol. Chem. 276:18804-18811.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18804-18811
    • Harms, N.1    Koningstein, G.2    Dontje, W.3    Muller, M.4    Oudega, B.5    Luirink, J.6    de Cock, H.7
  • 53
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and mu
    • Casadaban MJ. 1976. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and mu. J. Mol. Biol. 104:541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 54
    • 84857158724 scopus 로고    scopus 로고
    • BamE modulates the Escherichia coli beta-barrel assembly machine component BamA
    • Rigel NW, Schwalm J, Ricci DP, Silhavy TJ. 2012. BamE modulates the Escherichia coli beta-barrel assembly machine component BamA. J. Bacteriol. 194:1002-1008.
    • (2012) J. Bacteriol. , vol.194 , pp. 1002-1008
    • Rigel, N.W.1    Schwalm, J.2    Ricci, D.P.3    Silhavy, T.J.4


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