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Volumn 65, Issue , 2011, Pages 149-168

Protein quality control in the bacterial periplasm

Author keywords

Chaperones; Cpx; Folding catalysts; Proteases; SigmaE

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; DETERGENT; DISULFIDE OXIDOREDUCTASE; PEPTIDYLPROLYL ISOMERASE; PROTEIN CPXA; PROTEIN CPXR; PROTEIN DEGP; PROTEIN DEGS; PROTEIN FKPA; PROTEIN HDEA; PROTEIN PPIA; PROTEIN PPID; PROTEIN PTRA; PROTEIN RPOE; PROTEIN RSEA; PROTEIN RSEP; PROTEIN SIGMAE; PROTEIN SPY; PROTEIN SURA; PROTEIN TSP; PROTEINASE; S PHASE KINASE ASSOCIATED PROTEIN; UNCLASSIFIED DRUG;

EID: 80053271174     PISSN: 00664227     EISSN: 15453251     Source Type: Book Series    
DOI: 10.1146/annurev-micro-090110-102925     Document Type: Review
Times cited : (132)

References (93)
  • 1
    • 0037516675 scopus 로고    scopus 로고
    • n-Hexane sensitivity of Escherichia coli due to low expression of imp/ ostA encoding an 87 kDa minor protein associated with the outer membrane
    • DOI 10.1099/mic.0.25927-0
    • Abe S, Okutsu T, Nakajima H, Kakuda N, Ohtsu I, Aono R. 2003. n-Hexane sensitivity of Escherichia coli due to low expression of imp/ostA encoding an 87 kDaminor protein associated with the outer membrane. Microbiology 149:1265-73 (Pubitemid 36626175)
    • (2003) Microbiology , vol.149 , Issue.5 , pp. 1265-1273
    • Abe, S.1    Okutsu, T.2    Nakajima, H.3    Kakuda, N.4    Ohtsu, I.5    Aono, R.6
  • 2
    • 43949125856 scopus 로고    scopus 로고
    • The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon
    • DOI 10.1021/bi800233w
    • Antonoaea R, Furst M, Nishiyama K, Muller M. 2008. The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon. Biochemistry 47:5649-56 (Pubitemid 351705176)
    • (2008) Biochemistry , vol.47 , Issue.20 , pp. 5649-5656
    • Antonoaea, R.1    Furst, M.2    Nishiyama, K.-I.3    Muller, M.4
  • 3
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • DOI 10.1046/j.1365-2958.2001.02250.x
    • Arie 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 (Pubitemid 32063107)
    • (2001) Molecular Microbiology , vol.39 , Issue.1 , pp. 199-210
    • Arie, J.-P.1    Sassoon, N.2    Betton, J.-M.3
  • 4
    • 0025855940 scopus 로고
    • Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: Protease III degrades high-molecular-weight substrates in vivo
    • Baneyx F, Georgiou G. 1991. Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo. J. Bacteriol. 173:2696-703
    • (1991) J. Bacteriol. , vol.173 , pp. 2696-703
    • Baneyx, F.1    Georgiou, G.2
  • 5
    • 0029670766 scopus 로고    scopus 로고
    • Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA
    • Bass S, Gu Q, Christen A. 1996. Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA. J. Bacteriol. 178:1154-61
    • (1996) J. Bacteriol. , vol.178 , pp. 1154-61
    • Bass, S.1    Gu, Q.2    Christen, A.3
  • 6
    • 0034696581 scopus 로고    scopus 로고
    • Substrate recognition through a PDZ domain in tail-specific protease
    • DOI 10.1021/bi992709s
    • Beebe KD, Shin J, Peng J, Chaudhury C, Khera J, Pei D. 2000. Substrate recognition through a PDZ domain in tail-specific protease. Biochemistry 39:3149-55 (Pubitemid 30159422)
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 3149-3155
    • Beebe, K.D.1    Shin, J.2    Peng, J.3    Chaudhury, C.4    Khera, J.5    Pei, D.6
  • 7
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • DOI 10.1093/emboj/20.1.285
    • 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. 20:285-94 (Pubitemid 32099124)
    • (2001) EMBO Journal , vol.20 , Issue.1-2 , pp. 285-294
    • Behrens, S.1    Maier, R.2    De Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 8
    • 77957204818 scopus 로고    scopus 로고
    • The role of SurA factor in outer membrane protein transport and virulence
    • Behrens-Kneip S. 2010. The role of SurA factor in outer membrane protein transport and virulence. Int. J. Med. Microbiol. 300:421-28
    • (2010) Int. J. Med. Microbiol. , vol.300 , pp. 421-28
    • Behrens-Kneip, S.1
  • 10
    • 0032502781 scopus 로고    scopus 로고
    • Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli
    • DOI 10.1074/jbc.273.15.8897
    • Betton JM, Sassoon N, Hofnung M, Laurent M. 1998. Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli. J. Biol. Chem. 273:8897-902 (Pubitemid 28176172)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8897-8902
    • Betton, J.-M.1    Sassoon, N.2    Hofnung, M.3    Laurent, M.4
  • 11
    • 0036849659 scopus 로고    scopus 로고
    • Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins
    • DOI 10.1016/S0969-2126(02)00877-8, PII S0969212602008778
    • Bitto E, McKay DB. 2002. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure 10:1489-98 (Pubitemid 35351489)
    • (2002) Structure , vol.10 , Issue.11 , pp. 1489-1498
    • Bitto, E.1    McKay, D.B.2
  • 12
    • 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. 278:49316-22
    • (2003) J. Biol. Chem. , vol.278 , pp. 49316-22
    • Bitto, E.1    McKay, D.B.2
  • 13
    • 70349664195 scopus 로고    scopus 로고
    • Global analysis of extracytoplasmic stress signaling in Escherichia coli
    • Bury-Mone S, Nomane Y, Reymond N, Barbet R, Jacquet E, et al. 2009. Global analysis of extracytoplasmic stress signaling in Escherichia coli. PLoS Genet. 5:e1000651
    • (2009) PLoS Genet. , vol.5
    • Bury-Mone, S.1    Nomane, Y.2    Reymond, N.3    Barbet, R.4    Jacquet, E.5
  • 15
    • 33846134757 scopus 로고    scopus 로고
    • E-mediated envelope stress response in Escherichia coli: Keys to graded, buffered, and rapid signal transduction
    • DOI 10.1101/gad.1496707
    • Chaba R, Grigorova I, Flynn J, Baker T, Gross C. 2007. Design principles of the proteolytic cascade governing the sE-mediated envelope stress response in Escherichia coli: keys to graded, buffered and rapid signal transduction. Genes Dev. 21:124-36 (Pubitemid 46089713)
    • (2007) Genes and Development , vol.21 , Issue.1 , pp. 124-136
    • Chaba, R.1    Grigorova, I.L.2    Flynn, J.M.3    Baker, T.A.4    Gross, C.A.5
  • 16
    • 33749593869 scopus 로고    scopus 로고
    • Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide
    • DOI 10.1128/JB.00571-06
    • Charlson ES, Werner JN, Misra R. 2006. Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide. J. Bacteriol. 188:7186-94 (Pubitemid 44547623)
    • (2006) Journal of Bacteriology , vol.188 , Issue.20 , pp. 7186-7194
    • Charlson, E.S.1    Werner, J.N.2    Misra, R.3
  • 17
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • DOI 10.1111/j.1365-2958.1996.tb02473.x
    • Chen R, Henning U. 1996. A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol. Microbiol. 19:1287-94 (Pubitemid 26112812)
    • (1996) Molecular Microbiology , vol.19 , Issue.6 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 20
    • 0028326431 scopus 로고
    • Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin
    • Clubb RT, Ferguson SB,WalshCT, Wagner G. 1994. Three-dimensional solution structure of Escherichia coli periplasmic cyclophilin. Biochemistry 33:2761-72 (Pubitemid 24103333)
    • (1994) Biochemistry , vol.33 , Issue.10 , pp. 2761-2772
    • Clubb, R.T.1    Ferguson, S.B.2    Walsh, C.T.3    Wagner, G.4
  • 21
    • 0030611303 scopus 로고    scopus 로고
    • The σ(E)-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of σ(E)
    • De Las Penas A, Connolly L, Gross CA. 1997. The sigmaE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of sigmaE. Mol. Microbiol. 24:373-85 (Pubitemid 27223867)
    • (1997) Molecular Microbiology , vol.24 , Issue.2 , pp. 373-385
    • De Las Penas, A.1    Connolly, L.2    Gross, C.A.3
  • 22
    • 50049088184 scopus 로고    scopus 로고
    • Washington, DC: Am. Soc. Microbiol.
    • Ehrmann M, ed. 2006. The Periplasm.Washington, DC: Am. Soc. Microbiol.
    • (2006) The Periplasm
    • Ehrmann, M.1
  • 23
    • 0034695425 scopus 로고    scopus 로고
    • HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria
    • Gajiwala KS, Burley SK. 2000. HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria. J. Mol. Biol. 295:605-12
    • (2000) J. Mol. Biol. , vol.295 , pp. 605-12
    • Gajiwala, K.S.1    Burley, S.K.2
  • 24
    • 0025832094 scopus 로고
    • Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3
    • Hara H, Yamamoto Y, Higashitani A, Suzuki H, Nishimura Y. 1991. Cloning, mapping, and characterization of the Escherichia coli prc gene, which is involved in C-terminal processing of penicillin-binding protein 3. J. Bacteriol. 173:4799-813
    • (1991) J. Bacteriol. , vol.173 , pp. 4799-813
    • Hara, H.1    Yamamoto, Y.2    Higashitani, A.3    Suzuki, H.4    Nishimura, Y.5
  • 27
    • 21244447713 scopus 로고    scopus 로고
    • The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
    • DOI 10.1074/jbc.M413742200
    • 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. 280:23540-48 (Pubitemid 40884832)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23540-23548
    • Hennecke, G.1    Nolte, J.2    Volkmer-Engert, R.3    Schneider-Mergener, J.4    Behrens, S.5
  • 28
    • 0014208282 scopus 로고
    • Selective release of enzymes from bacteria
    • Heppel LA. 1967. Selective release of enzymes from bacteria. Science 156:1451-55
    • (1967) Science , vol.156 , pp. 1451-55
    • Heppel, L.A.1
  • 30
    • 67149144225 scopus 로고    scopus 로고
    • CpxRA influences Xenorhabdus nematophila colonization initiation and outgrowth in Steinernema carpocapsae nematodes through regulation of the nil locus
    • Herbert Tran EE, Andersen AW, Goodrich-Blair H. 2009. CpxRA influences Xenorhabdus nematophila colonization initiation and outgrowth in Steinernema carpocapsae nematodes through regulation of the nil locus. Appl. Environ. Microbiol. 75:4007-14
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 4007-14
    • Herbert Tran, E.E.1    Andersen, A.W.2    Goodrich-Blair, H.3
  • 31
    • 77957232471 scopus 로고    scopus 로고
    • Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion
    • Hoy B, LowerM,Weydig C, Carra G, Tegtmeyer N, et al. 2010. Helicobacter pylori HtrA is a new secreted virulence factor that cleaves E-cadherin to disrupt intercellular adhesion. EMBO Rep. 10:798-804
    • (2010) EMBO Rep. , vol.10 , pp. 798-804
    • Hoy, B.1    Lower, M.2    Weydig, C.3    Carra, G.4    Tegtmeyer, N.5
  • 32
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R, Bode W. 1978. Structural basis of the activation and action of trypsin. Acc. Chem. Res. 11:114-22
    • (1978) Acc. Chem. Res. , vol.11 , pp. 114-22
    • Huber, R.1    Bode, W.2
  • 33
    • 0348147593 scopus 로고    scopus 로고
    • Temperature effect on inclusion body formation and stress response in the periplasm of Escherichia coli
    • DOI 10.1046/j.1365-2958.2003.03785.x
    • Hunke S, Betton JM. 2003. Temperature effect on inclusion body formation and stress response in the periplasm of Escherichia coli. Mol. Microbiol. 50:1579-89 (Pubitemid 38010454)
    • (2003) Molecular Microbiology , vol.50 , Issue.5 , pp. 1579-1589
    • Hunke, S.1    Betton, J.-M.2
  • 34
    • 58049199407 scopus 로고    scopus 로고
    • A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli
    • Inaba K, Suzuki M, Maegawa K, Akiyama S, Ito K, Akiyama Y. 2008. A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli. J. Biol. Chem. 283:35042-52
    • (2008) J. Biol. Chem. , vol.283 , pp. 35042-52
    • Inaba, K.1    Suzuki, M.2    Maegawa, K.3    Akiyama, S.4    Ito, K.5    Akiyama, Y.6
  • 36
    • 33750297745 scopus 로고    scopus 로고
    • E Regulon: Role in Down-regulation of Outer Membrane Proteins
    • DOI 10.1016/j.jmb.2006.09.004, PII S0022283606011727
    • Johansen J, Rasmussen A, Overgaard M, Valentin-Hansen P. 2006. Conserved small non-coding RNAs that belong to the sigma(E) regulon: role in down-regulation of outer membrane proteins. J. Mol. Biol. 364:1-8 (Pubitemid 44634530)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.1 , pp. 1-8
    • Johansen, J.1    Rasmussen, A.A.2    Overgaard, M.3    Valentin-Hansen, P.4
  • 37
    • 77955127606 scopus 로고    scopus 로고
    • Managing membrane stress: The phage shock protein (Psp) response, from molecular mechanisms to physiology
    • Joly N, Engl C, Jovanovic G, Huvet M, Toni T, et al. 2010. Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology. FEMS Microbiol. Rev. 34:797-827
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 797-827
    • Joly, N.1    Engl, C.2    Jovanovic, G.3    Huvet, M.4    Toni, T.5
  • 38
    • 77956318615 scopus 로고    scopus 로고
    • Mechanisms of oxidative protein folding in the bacterial cell envelope
    • Kadokura H, Beckwith J. 2010. Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid. Redox Signal 13:1231-46
    • (2010) Antioxid. Redox Signal , vol.13 , pp. 1231-46
    • Kadokura, H.1    Beckwith, J.2
  • 39
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • DOI 10.1146/annurev.biochem.72.121801.161459
    • Kadokura H, Katzen F, Beckwith J. 2003. Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 72:111-35 (Pubitemid 36930443)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 40
    • 77952694508 scopus 로고    scopus 로고
    • Structural basis for the negative regulation of bacterial stress response by RseB
    • Kim DY, Kwon E, Choi J, Hwang HY, Kim KK. 2010. Structural basis for the negative regulation of bacterial stress response by RseB. Protein Sci. 19:1258-63
    • (2010) Protein Sci. , vol.19 , pp. 1258-63
    • Kim, D.Y.1    Kwon, E.2    Choi, J.3    Hwang, H.Y.4    Kim, K.K.5
  • 41
    • 44349189894 scopus 로고    scopus 로고
    • Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease
    • KoideK, Ito K, Akiyama Y. 2008. Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease. J. Biol. Chem. 283:9562-70
    • (2008) J. Biol. Chem. , vol.283 , pp. 9562-70
    • Koide, K.1    Ito, K.2    Akiyama, Y.3
  • 42
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • DOI 10.1038/416455a
    • Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T. 2002. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416:455-59 (Pubitemid 34272883)
    • (2002) Nature , vol.416 , Issue.6879 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 44
    • 77954384306 scopus 로고    scopus 로고
    • HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
    • Krojer T, Sawa J, Huber R, Clausen T. 2010. HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Nat. Struct. Mol. Biol. 17:844-52
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 844-52
    • Krojer, T.1    Sawa, J.2    Huber, R.3    Clausen, T.4
  • 45
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • DOI 10.1038/nature07004, PII NATURE07004
    • 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 453:885-90 (Pubitemid 351832567)
    • (2008) Nature , vol.453 , Issue.7197 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 47
    • 34548570108 scopus 로고    scopus 로고
    • Chlamydial CT441 Is a PDZ domain-containing tail-specific protease that interferes with the NF-κB pathway of immune response
    • DOI 10.1128/JB.00429-07
    • Lad SP, Yang G, Scott DA, Wang G, Nair P, et al. 2007. Chlamydial CT441 is a PDZ domaincontaining tail-specific protease that interferes with the NF-kappaB pathway of immune response. J. Bacteriol. 189:6619-25 (Pubitemid 47397368)
    • (2007) Journal of Bacteriology , vol.189 , Issue.18 , pp. 6619-6625
    • Lad, S.P.1    Yang, G.2    Scott, D.A.3    Wang, G.4    Nair, P.5    Mathison, J.6    Reddy, V.S.7    Li, E.8
  • 49
    • 70349299921 scopus 로고    scopus 로고
    • Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage
    • Li X, Wang B, Feng L, Kang H, Qi Y, et al. 2009. Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage. Proc. Natl. Acad. Sci. USA 106:14837-42
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14837-42
    • Li, X.1    Wang, B.2    Feng, L.3    Kang, H.4    Qi, Y.5
  • 50
    • 0025755354 scopus 로고
    • Human and Escherichia coli cyclophilins: Sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue
    • Liu J, Chen CM, Walsh CT. 1991. Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue. Biochemistry 30:2306-10
    • (1991) Biochemistry , vol.30 , pp. 2306-10
    • Liu, J.1    Chen, C.M.2    Walsh, C.T.3
  • 51
    • 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 CT. 1990. 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 87:4028-32
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4028-32
    • Liu, J.1    Walsh, C.T.2
  • 52
  • 53
    • 33947486602 scopus 로고
    • Release of alkaline phosphatase from cells of Escherichia coli upon lysozyme spheroplast formation
    • Malamy MH, Horecker BL. 1964. Release of alkaline phosphatase from cells of Escherichia coli upon lysozyme spheroplast formation. Biochemistry 3:1889-93
    • (1964) Biochemistry , vol.3 , pp. 1889-93
    • Malamy, M.H.1    Horecker, B.L.2
  • 54
    • 34548484888 scopus 로고    scopus 로고
    • Pitrilysins/inverzincins
    • ed. A Messerschmidt, M Cygler, WBode Chichester, UK: Wiley
    • Maskos K. 2004. Pitrilysins/inverzincins. In Handbook of Metalloproteins, ed. A Messerschmidt, M Cygler, WBode, 3:190-98. Chichester, UK:Wiley
    • (2004) Handbook of Metalloproteins , vol.3 , pp. 190-98
    • Maskos, K.1
  • 55
    • 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
    • (2010) BMC Microbiol. , vol.10 , pp. 251
    • Matern, Y.1    Barion, B.2    Behrens-Kneip, S.3
  • 56
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • Mayer MP. 2010. Gymnastics of molecular chaperones. Mol. Cell 39:321-31
    • (2010) Mol. Cell , vol.39 , pp. 321-31
    • Mayer, M.P.1
  • 57
    • 41249087703 scopus 로고    scopus 로고
    • Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control
    • Meltzer M, Hasenbein S, Hauske P, Kucz N, Merdanovic M, et al. 2008. Allosteric activation of HtrA protease DegP by stress signals during bacterial protein quality control. Angew. Chem. Int. Ed. Engl. 47:1332-34
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 1332-34
    • Meltzer, M.1    Hasenbein, S.2    Hauske, P.3    Kucz, N.4    Merdanovic, M.5
  • 58
    • 77954384789 scopus 로고    scopus 로고
    • Determinants of structural and functional plasticity of a widely conserved protease chaperone complex
    • Merdanovic M, Mamant N, MeltzerM, Poepsel S, Auckenthaler A, et al. 2010. Determinants of structural and functional plasticity of a widely conserved protease chaperone complex. Nat. Struct. Mol. Biol. 17:837-43
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 837-43
    • Merdanovic, M.1    Mamant, N.2    Meltzerm Poepsel, S.3    Auckenthaler, A.4
  • 59
    • 0001353602 scopus 로고
    • Approaches to the analysis of specific membrane transport
    • ed. TW Goodwin, O Lindberg New York: Academic
    • Mitchell P. 1961. Approaches to the analysis of specific membrane transport. In Biological Structure and Function, ed. TW Goodwin, O Lindberg, pp. 581-603. New York: Academic
    • (1961) Biological Structure and Function , pp. 581-603
    • Mitchell, P.1
  • 61
    • 70350520053 scopus 로고    scopus 로고
    • The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential
    • Patel GJ, Behrens-Kneip S, Holst O, Kleinschmidt JH. 2009. The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential. Biochemistry 48:10235-45
    • (2009) Biochemistry , vol.48 , pp. 10235-45
    • Patel, G.J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 62
    • 63049096052 scopus 로고    scopus 로고
    • Characterization of the Cpx regulon in Escherichia coli strain MC4100
    • Price NL, Raivio TL. 2009. Characterization of the Cpx regulon in Escherichia coli strain MC4100. J. Bacteriol. 191:1798-815
    • (2009) J. Bacteriol. , vol.191 , pp. 1798-815
    • Price, N.L.1    Raivio, T.L.2
  • 63
    • 34547643207 scopus 로고    scopus 로고
    • IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA
    • DOI 10.1128/JB.00483-07
    • PurdyGE, Fisher CR, Payne SM. 2007. IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA. J. Bacteriol. 189:5566-73 (Pubitemid 47206402)
    • (2007) Journal of Bacteriology , vol.189 , Issue.15 , pp. 5566-5573
    • Purdy, G.E.1    Fisher, C.R.2    Payne, S.M.3
  • 64
    • 66649116274 scopus 로고    scopus 로고
    • Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study
    • Qu J, Behrens-Kneip S,Holst O, Kleinschmidt JH. 2009. Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study. Biochemistry 48:4926-36
    • (2009) Biochemistry , vol.48 , pp. 4926-36
    • Qu, J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 65
    • 79952363991 scopus 로고    scopus 로고
    • Genetic selection designed to stabilize proteins uncovers a chaperone called Spy
    • Quan S, Koldewey P, Tapley TL, Kirsch N, Ruane K, et al. 2011. Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat. Struct. Mol. Biol. 18:262-69
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 262-69
    • Quan, S.1    Koldewey, P.2    Tapley, T.L.3    Kirsch, N.4    Ruane, K.5
  • 66
    • 0036033555 scopus 로고    scopus 로고
    • A third envelope stress signal transduction pathway in Escherichia coli
    • DOI 10.1046/j.1365-2958.2002.03112.x
    • Raffa RG, Raivio TL. 2002. A third envelope stress signal transduction pathway in Escherichia coli. Mol. Microbiol. 45:1599-611 (Pubitemid 35231977)
    • (2002) Molecular Microbiology , vol.45 , Issue.6 , pp. 1599-1611
    • Raffa, R.G.1    Raivio, T.L.2
  • 67
    • 0038831330 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA: II. Isomerase-independent chaperone activity in vitro
    • DOI 10.1074/jbc.M910234199
    • Ramm K, Pluckthun A. 2000. The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro. J. Biol. Chem. 275:17106-13 (Pubitemid 30398955)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.22 , pp. 17106-17113
    • Ramm, K.1    Pluckthun, A.2
  • 68
    • 0035816225 scopus 로고    scopus 로고
    • High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA
    • DOI 10.1006/jmbi.2001.4747
    • Ramm K, Pluckthun A. 2001. High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. J. Mol. Biol. 310:485-98 (Pubitemid 32664881)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.2 , pp. 485-498
    • Ramm, K.1    Pluckthun, A.2
  • 69
    • 33745588575 scopus 로고    scopus 로고
    • Role of sigma E-regulated genes in Escherichia coli uropathogenesis
    • DOI 10.1128/IAI.01984-05
    • Redford P, Welch R. 2006. Role of sigma E-regulated genes in Escherichia coli uropathogenesis. Infect. Immun. 74:4030-38 (Pubitemid 43993335)
    • (2006) Infection and Immunity , vol.74 , Issue.7 , pp. 4030-4038
    • Redford, P.1    Welch, R.A.2
  • 70
    • 31144454629 scopus 로고    scopus 로고
    • Conserved and variable functions of the sigmaE stress response in related genomes
    • Rhodius V, SuhW, Nonaka G,West J, Gross C. 2006. Conserved and variable functions of the sigmaE stress response in related genomes. PLoS Biol. 4:e2
    • (2006) PLoS Biol. , vol.4
    • Rhodius, V.1    Suh, W.2    Nonaka, G.3    West, J.4    Gross, C.5
  • 71
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • Richter K, Haslbeck M, Buchner J. 2010. The heat shock response: life on the verge of death. Mol. Cell 40:253-66
    • (2010) Mol. Cell , vol.40 , pp. 253-66
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 72
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • DOI 10.1128/JB.183.23.6794-6800.2001
    • Rizzitello AE, Harper JR, Silhavy TJ. 2001. Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J. Bacteriol. 183:6794-800 (Pubitemid 33064192)
    • (2001) Journal of Bacteriology , vol.183 , Issue.23 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 73
    • 33947281521 scopus 로고    scopus 로고
    • E regulatory pathway are involved in adhesion and invasion of the Crohn's disease-associated Escherichia coli strain LF82
    • DOI 10.1111/j.1365-2958.2007.05638.x
    • Rolhion N, Carvalho FA, Darfeuille-Michaud A. 2007. OmpC and the sigma(E) regulatory pathway are involved in adhesion and invasion of the Crohn's disease-associated Escherichia coli strain LF82. Mol. Microbiol. 63:1684-700 (Pubitemid 46426710)
    • (2007) Molecular Microbiology , vol.63 , Issue.6 , pp. 1684-1700
    • Rolhion, N.1    Carvalho, F.A.2    Darfeuille-Michaud, A.3
  • 74
    • 33646851752 scopus 로고    scopus 로고
    • Pushing the envelope: Extracytoplasmic stress responses in bacterial pathogens
    • DOI 10.1038/nrmicro1394, PII N1394
    • Rowley G, Spector M, Kormanec J, Roberts M. 2006. Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens. Nat. Rev. Microbiol. 4:383-94 (Pubitemid 43771856)
    • (2006) Nature Reviews Microbiology , vol.4 , Issue.5 , pp. 383-394
    • Rowley, G.1    Spector, M.2    Kormanec, J.3    Roberts, M.4
  • 75
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality: A genetic strategy to probe organelle assembly
    • DOI 10.1016/j.cell.2005.02.014
    • Ruiz N, Falcone B, Kahne D, Silhavy TJ. 2005. Chemical conditionality: a genetic strategy to probe organelle assembly. Cell 121:307-17 (Pubitemid 40546397)
    • (2005) Cell , vol.121 , Issue.2 , pp. 307-317
    • Ruiz, N.1    Falcone, B.2    Kahne, D.3    Silhavy, T.J.4
  • 76
    • 70350470007 scopus 로고    scopus 로고
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae
    • Ruiz-Perez F, Henderson IR, Leyton DL, Rossiter AE, Zhang Y, Nataro JP. 2009. Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae. J. Bacteriol. 191:6571-83
    • (2009) J. Bacteriol. , vol.191 , pp. 6571-83
    • Ruiz-Perez, F.1    Henderson, I.R.2    Leyton, D.L.3    Rossiter, A.E.4    Zhang, Y.5    Nataro, J.P.6
  • 77
    • 0346366809 scopus 로고    scopus 로고
    • Structural and Functional Studies of FkpA from Escherichia coli, a cis/trans Peptidyl-prolyl Isomerase with Chaperone Activity
    • DOI 10.1016/j.jmb.2003.10.056
    • Saul FA, Arie JP, Vulliez-le Normand B, Kahn R, Betton JM, 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 (Pubitemid 37532659)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.2 , pp. 595-608
    • Saul, F.A.1    Arie, J.-P.2    Vulliez-le Normand, B.3    Kahn, R.4    Betton, J.-M.5    Bentley, G.A.6
  • 78
    • 0038105593 scopus 로고    scopus 로고
    • Skp, amolecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • SchaferU, Beck K,MullerM. 1999. Skp, amolecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 274:24567-74
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-74
    • Schafer, U.1    Beck, K.2    Muller, M.3
  • 79
    • 0026457932 scopus 로고
    • Multiple antibiotic susceptibility associated with inactivation of the prc gene
    • Seoane A, Sabbaj A, McMurry LM, Levy SB. 1992. Multiple antibiotic susceptibility associated with inactivation of the prc gene. J. Bacteriol. 174:7844-47
    • (1992) J. Bacteriol. , vol.174 , pp. 7844-47
    • Seoane, A.1    Sabbaj, A.2    McMurry, L.M.3    Levy, S.B.4
  • 80
    • 0026513218 scopus 로고
    • Tsp: A tail-specific protease that selectively degrades proteins with nonpolar C termini
    • Silber KR, Keiler KC, Sauer RT. 1992. Tsp: a tail-specific protease that selectively degrades proteins with nonpolar C termini. Proc. Natl. Acad. Sci. USA 89:295-99
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 295-99
    • Silber, K.R.1    Keiler, K.C.2    Sauer, R.T.3
  • 81
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • DOI 10.1016/S0092-8674(00)80743-6
    • Spiess C, Beil A, Ehrmann M. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-47 (Pubitemid 29214590)
    • (1999) Cell , vol.97 , Issue.3 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 82
    • 11144298973 scopus 로고    scopus 로고
    • Exploring biology with small organic molecules
    • DOI 10.1038/nature03196
    • Stockwell BR. 2004. Exploring biology with small organic molecules. Nature 432:846-54 (Pubitemid 40037140)
    • (2004) Nature , vol.432 , Issue.7019 , pp. 846-854
    • Stockwell, B.R.1
  • 84
    • 34249807616 scopus 로고    scopus 로고
    • E regulates and is regulated by a small RNA in Escherichia coli
    • DOI 10.1128/JB.00020-07
    • Thompson KM, Rhodius VA, Gottesman S. 2007. SigmaE regulates and is regulated by a small RNA in Escherichia coli. J. Bacteriol. 189:4243-56 (Pubitemid 46847373)
    • (2007) Journal of Bacteriology , vol.189 , Issue.11 , pp. 4243-4256
    • Thompson, K.M.1    Rhodius, V.A.2    Gottesman, S.3
  • 85
    • 67549146965 scopus 로고    scopus 로고
    • Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073
    • Totsika M, Heras B, Wurpel DJ, Schembri MA. 2009. Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073. J. Bacteriol. 191:3901-8
    • (2009) J. Bacteriol. , vol.191 , pp. 3901-8
    • Totsika, M.1    Heras, B.2    Wurpel, D.J.3    Schembri, M.A.4
  • 86
    • 0034604528 scopus 로고    scopus 로고
    • Determinants of translocation and folding of TreF, a trehalase of Escherichia coli
    • DOI 10.1074/jbc.M002793200
    • Uhland K, Mondigler M, Spiess C, Prinz W, Ehrmann M. 2000. Determinants of translocation and folding of TreF, a trehalase of Escherichia coli. J. Biol. Chem. 275:23439-45 (Pubitemid 30624623)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.31 , pp. 23439-23445
    • Uhland, K.1    Mondigler, M.2    Spiess, C.3    Prinz, W.4    Ehrmann, M.5
  • 87
    • 34247098804 scopus 로고    scopus 로고
    • Small RNAs controlling outer membrane porins
    • DOI 10.1016/j.mib.2007.03.001, PII S1369527407000185, Cell Regulation (RNA Special Issue)
    • Valentin-Hansen P, Johansen J, Rasmussen AA. 2007. Small RNAs controlling outer membrane porins. Curr. Opin. Microbiol. 10:152-55 (Pubitemid 46590041)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.2 , pp. 152-155
    • Valentin-Hansen, P.1    Johansen, J.2    Rasmussen, A.A.3
  • 88
    • 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 9:2432-43
    • (2009) Proteomics , vol.9 , pp. 2432-43
    • Vertommen, D.1    Ruiz, N.2    Leverrier, P.3    Silhavy, T.J.4    Collet, J.F.5
  • 89
    • 0344953579 scopus 로고    scopus 로고
    • OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • DOI 10.1016/S0092-8674(03)00203-4
    • Walsh NP, Alba BM, Bose B, Gross CA, Sauer RT. 2003. OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113:61-71 (Pubitemid 36411960)
    • (2003) Cell , vol.113 , Issue.1 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 90
    • 75149136165 scopus 로고    scopus 로고
    • The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity
    • Weininger U, Jakob RP, Kovermann M, Balbach J, Schmid FX. 2010. The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity. Protein Sci. 19:6-18
    • (2010) Protein Sci. , vol.19 , pp. 6-18
    • Weininger, U.1    Jakob, R.P.2    Kovermann, M.3    Balbach, J.4    Schmid, F.X.5
  • 91
    • 2342659637 scopus 로고    scopus 로고
    • Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease
    • DOI 10.1016/S0092-8674(04)00454-4, PII S0092867404004544
    • Wilken C, Kitzing K, Kurzbauer R, Ehrmann M, Clausen T. 2004. Crystal structure of the DegS stress sensor: how a PDZ domain recognizesmisfolded protein and activates a protease domain. Cell 117:483-94 (Pubitemid 38610233)
    • (2004) Cell , vol.117 , Issue.4 , pp. 483-494
    • Wilken, C.1    Kitzing, K.2    Kurzbauer, R.3    Ehrmann, M.4    Clausen, T.5
  • 93
    • 77950604350 scopus 로고    scopus 로고
    • Acid stress response in enteropathogenic gammaproteobacteria: An aptitude for survival
    • 168 Merdanovic
    • Zhao B, Houry WA. 2010. Acid stress response in enteropathogenic gammaproteobacteria: an aptitude for survival. Biochem. Cell Biol. 88:301-14 168 Merdanovic
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 301-14
    • Zhao, B.1    Houry, W.A.2


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