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Volumn 196, Issue 3, 2014, Pages 672-680

Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditions

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; FKPA PROTEIN; OUTER MEMBRANE PROTEIN; SURA PROTEIN; UNCLASSIFIED DRUG;

EID: 84892414880     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01069-13     Document Type: Article
Times cited : (33)

References (45)
  • 1
    • 0015182457 scopus 로고
    • Chloroplast structure and biogenesis
    • Kirk JT. 1971. Chloroplast structure and biogenesis. Annu. Rev. Biochem. 40:161-196. http://dx.doi.org/10.1146/annurev.bi.40.070171.001113.
    • (1971) Annu. Rev. Biochem. , vol.40 , pp. 161-196
    • Kirk, J.T.1
  • 2
    • 0001001129 scopus 로고
    • The fine structure of mitochondria
    • Palade GE. 1952. The fine structure of mitochondria. Anat. Rec. 114:427-451. http://dx.doi.org/10.1002/ar.1091140304.
    • (1952) Anat. Rec. , vol.114 , pp. 427-451
    • Palade, G.E.1
  • 3
    • 0014451685 scopus 로고
    • The topography of the bacterial cell wall
    • GlauertAM,Thornley MJ. 1969. The topography of the bacterial cell wall. Annu. Rev. Microbiol. 23:159-198. http://dx.doi.org/10.1146/annurev.mi.23.100169.001111.
    • (1969) Annu. Rev. Microbiol. , vol.23 , pp. 159-198
    • Glauert, A.M.1    Thornley, M.J.2
  • 4
    • 68949207040 scopus 로고    scopus 로고
    • Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence
    • Walther DM, Rapaport D, Tommassen J. 2009. Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence. Cell. Mol. Life Sci. 66:2789-2804. http://dx.doi.org/10.1007/s00018-009-0029-z.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2789-2804
    • Walther, D.M.1    Rapaport, D.2    Tommassen, J.3
  • 5
    • 25144452723 scopus 로고    scopus 로고
    • Biogenesis of beta-barrel membrane proteins of mitochondria
    • Paschen SA, Neupert W, Rapaport D. 2005. Biogenesis of beta-barrel membrane proteins of mitochondria. Trends Biochem. Sci. 30:575-582. http://dx.doi.org/10.1016/j.tibs.2005.08.009.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 575-582
    • Paschen, S.A.1    Neupert, W.2    Rapaport, D.3
  • 6
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • Bos MP, Robert V, Tommassen J. 2007. Biogenesis of the Gram-negative bacterial outer membrane. Annu. Rev. Microbiol. 61:191-214. http://dx.doi.org/10.1146/annurev.micro.61.080706.093245.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 8
    • 79959468179 scopus 로고    scopus 로고
    • Beta-barrel membrane protein assembly by the Bam complex
    • Hagan CL, Silhavy TJ, Kahne D. 2011. Beta-barrel membrane protein assembly by the Bam complex. Annu. Rev. Biochem. 80:189-210. http://dx.doi.org/10.1146/annurev-biochem-061408-144611.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3
  • 9
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H, Vaara M. 1985. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49:1-32.
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 10
    • 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. http://dx.doi.org/10.1128/JB.183.23.6794-6800.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 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. http://dx.doi.org/10.1101/gad.1581007.
    • (2007) Genes Dev. , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 12
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer T, Sawa J, Schafer E, Saibil HR, Ehrmann M, Clausen T. 2008. Structural basis for the regulated protease and chaperone function of DegP. Nature 453:885-890. http://dx.doi.org/10.1038/nature07004.
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 13
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidylprolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouvière PE, Gross CA. 1996. SurA, a periplasmic protein with peptidylprolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 10:3170-3182. http://dx.doi.org/10.1101/gad.10.24.3170.
    • (1996) Genes Dev. , vol.10 , pp. 3170-3182
    • Rouvière, P.E.1    Gross, C.A.2
  • 14
    • 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. http://dx.doi.org/10.1111/j.1365-2958.1996.tb02473.x.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 15
    • 80052158740 scopus 로고    scopus 로고
    • Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism
    • Wu S, Ge X, Lv Z, Zhi Z, Chang Z, Zhao XS. 2011. Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism. Biochem. J. 438:505-511. http://dx.doi.org/10.1042/BJ20110264.
    • (2011) Biochem. J. , vol.438 , pp. 505-511
    • Wu, S.1    Ge, X.2    Lv, Z.3    Zhi, Z.4    Chang, Z.5    Zhao, X.S.6
  • 16
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar SW, Kolter R. 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
  • 17
    • 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 JF. 2009. Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics. Proteomics 9:2432-2443. http://dx.doi.org/10.1002/pmic.200800794.
    • (2009) Proteomics , vol.9 , pp. 2432-2443
    • Vertommen, D.1    Ruiz, N.2    Leverrier, P.3    Silhavy, T.J.4    Collet, J.F.5
  • 18
    • 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 FX, Gross CA. 2001. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 20:285-294. http://dx.doi.org/10.1093/emboj/20.1.285.
    • (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
  • 19
    • 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 DB. 2003. The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins. J. Biol. Chem. 278:49316-49322. http://dx.doi.org/10.1074/jbc.M308853200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49316-49322
    • Bitto, E.1    McKay, D.B.2
  • 20
    • 21244447713 scopus 로고    scopus 로고
    • The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
    • Hennecke G, Nolte J, Volkmer-Engert R, Schneider-Mergener J, Behrens S. 2005. The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition. J. Biol. Chem. 280:23540-23548. http://dx.doi.org/10.1074/jbc.M413742200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23540-23548
    • Hennecke, G.1    Nolte, J.2    Volkmer-Engert, R.3    Schneider-Mergener, J.4    Behrens, S.5
  • 21
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R, Bos MP, Geurtsen J, Mols M, Tommassen J. 2003. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299:262-265. http://dx.doi.org/10.1126/science.1078973.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 22
    • 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. http://dx.doi.org/10.1016/j.cell.2005.02.015.
    • (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
  • 23
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • Hagan CL, Kim S, Kahne D. 2010. Reconstitution of outer membrane protein assembly from purified components. Science 328:890-892. http://dx.doi.org/10.1126/science.1188919.
    • (2010) Science , vol.328 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 24
    • 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, Muller 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. http://dx.doi.org/10.1074/jbc.274.35.24567.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schäfer, U.1    Beck, K.2    Muller, M.3
  • 25
    • 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. http://dx.doi.org/10.1074/jbc.M211177200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 26
    • 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. http://dx.doi.org/10.1073/pnas.0809275106.
    • (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
  • 27
    • 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. http://dx.doi.org/10.1016/S0092-8674(00)80743-6.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 28
    • 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 KL, 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
  • 29
    • 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
  • 30
    • 0033870158 scopus 로고    scopus 로고
    • Overexpression of proteasedeficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background
    • Misra R, CastilloKeller M, Deng M. 2000. Overexpression of proteasedeficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background. J. Bacteriol. 182:4882-4888. http://dx.doi.org/10.1128/JB.182.17.4882-4888.2000.
    • (2000) J. Bacteriol. , vol.182 , pp. 4882-4888
    • Misra, R.1    CastilloKeller, M.2    Deng, M.3
  • 31
    • 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. http://dx.doi.org/10.1128/JB.185.1.148-154.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 148-154
    • CastilloKeller, M.1    Misra, R.2
  • 33
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arié JP, Sassoon N, Betton JM. 2001. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 39:199-210. http://dx.doi.org/10.1046/j.1365-2958.2001.02250.x.
    • (2001) Mol. Microbiol. , vol.39 , pp. 199-210
    • Arié, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 34
    • 73449097174 scopus 로고    scopus 로고
    • Gene doctoring: a method for recombineering in laboratory and pathogenic Escherichia coli strains
    • Lee DJ, Bingle LE, Heurlier K, Pallen MJ, Penn CW, Busby SJ, Hobman JL. 2009. Gene doctoring: a method for recombineering in laboratory and pathogenic Escherichia coli strains. BMC Microbiol. 9:252. http://dx.doi.org/10.1186/1471-2180-9-252.
    • (2009) BMC Microbiol. , vol.9 , pp. 252
    • Lee, D.J.1    Bingle, L.E.2    Heurlier, K.3    Pallen, M.J.4    Penn, C.W.5    Busby, S.J.6    Hobman, J.L.7
  • 35
    • 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 TJ. 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
  • 36
    • 0029618716 scopus 로고
    • A conserved histidine residue of Escherichia coli outer-membrane phospholipase A is important for activity
    • Brok RG, Dekker N, Gerrits N, Verheij HM, Tommassen J. 1995. A conserved histidine residue of Escherichia coli outer-membrane phospholipase A is important for activity. Eur. J. Biochem. 234:934-938. http://dx.doi.org/10.1111/j.1432-1033.1995.934_a.x.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 934-938
    • Brok, R.G.1    Dekker, N.2    Gerrits, N.3    Verheij, H.M.4    Tommassen, J.5
  • 37
    • 0023808092 scopus 로고
    • 32-independent mechanism of heat-inducible transcription
    • 32-independent mechanism of heat-inducible transcription. Nucleic Acids Res. 16:10053-10067. http://dx.doi.org/10.1093/nar/16.21.10053.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10053-10067
    • Lipinska, B.1    Sharma, S.2    Georgopoulos, C.3
  • 38
    • 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. http://dx.doi.org/10.1093/emboj/17.14.3968.
    • (1998) EMBO J. , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 39
    • 77957135569 scopus 로고    scopus 로고
    • PpiD is a player in the network of periplasmic chaperones in Escherichia coli
    • Matern Y, Barion B, Behrens-Kneip S. 2010. PpiD is a player in the network of periplasmic chaperones in Escherichia coli. BMC Microbiol. 10:251. http://dx.doi.org/10.1186/1471-2180-10-251.
    • (2010) BMC Microbiol. , vol.10 , pp. 251
    • Matern, Y.1    Barion, B.2    Behrens-Kneip, S.3
  • 40
    • 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 SS, Hunstad DA, Harper JR, Duguay AR, Pinkner JS, Bann J, Frieden C, Silhavy TJ, Hultgren SJ. 2005. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J. Bacteriol. 187:7680-7686. http://dx.doi.org/10.1128/JB.187.22.7680-7686.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 7680-7686
    • Justice, S.S.1    Hunstad, D.A.2    Harper, J.R.3    Duguay, A.R.4    Pinkner, J.S.5    Bann, J.6    Frieden, C.7    Silhavy, T.J.8    Hultgren, S.J.9
  • 42
    • 2942536628 scopus 로고    scopus 로고
    • Protein quality control in the bacterial periplasm
    • Miot M, Betton JM. 2004. Protein quality control in the bacterial periplasm. Microb. Cell Fact. 3:4. http://dx.doi.org/10.1186/1475-2859-3-4.
    • (2004) Microb. Cell Fact. , vol.3 , pp. 4
    • Miot, M.1    Betton, J.M.2
  • 43
    • 8844237557 scopus 로고    scopus 로고
    • Quality control in the bacterial periplasm
    • Duguay AR, Silhavy TJ. 2004. Quality control in the bacterial periplasm. Biochim. Biophys. Acta 1694:121-134. http://dx.doi.org/10.1016/j.bbamcr.2004.04.012.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 121-134
    • Duguay, A.R.1    Silhavy, T.J.2
  • 44
    • 0034780493 scopus 로고    scopus 로고
    • Periplasmic stress and ECF sigma factors
    • Raivio TL, Silhavy TJ. 2001. Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol. 55:591-624. http://dx.doi.org/10.1146/annurev.micro.55.1.591.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 591-624
    • Raivio, T.L.1    Silhavy, T.J.2
  • 45
    • 84880965951 scopus 로고    scopus 로고
    • Role for Skp in LptD assembly in Escherichia coli
    • Schwalm J, Mahoney TF, Soltes GR, Silhavy TJ. 2013. Role for Skp in LptD assembly in Escherichia coli. J. Bacteriol. 195:3734-3742. http://dx.doi.org/10.1128/JB.00431-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 3734-3742
    • Schwalm, J.1    Mahoney, T.F.2    Soltes, G.R.3    Silhavy, T.J.4


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