메뉴 건너뛰기




Volumn 3, Issue 10, 2008, Pages

Components of SurA required for outer membrane biogenesis in uropathogenic Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; CHAPERONE; NOVOBIOCIN; OUTER MEMBRANE PROTEIN; PEPTIDYLPROLYL ISOMERASE; PROTEIN FIMD; PROTEIN SURA; UNCLASSIFIED DRUG; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; FIMBRIA PROTEIN; FIMD PROTEIN, E COLI; PORIN; SURA PROTEIN, E COLI;

EID: 53749086601     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0003359     Document Type: Article
Times cited : (29)

References (31)
  • 1
    • 34548139422 scopus 로고    scopus 로고
    • Structure and function of an essential component of the outer membrane protein assembly machine
    • Kim S, Malinverni JC, Sliz P, Silhavy TJ, Harrison SC, et al. (2007) Structure and function of an essential component of the outer membrane protein assembly machine. Science 317: 961-964.
    • (2007) Science , vol.317 , pp. 961-964
    • Kim, S.1    Malinverni, J.C.2    Sliz, P.3    Silhavy, T.J.4    Harrison, S.C.5
  • 2
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, et al. (2006) YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol 61: 151-164.
    • (2006) Mol Microbiol , vol.61 , pp. 151-164
    • Malinverni, J.C.1    Werner, J.2    Kim, S.3    Sklar, J.G.4    Kahne, D.5
  • 3
    • 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, et al. (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
  • 4
    • 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 U S A 87: 4028-4032.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4028-4032
    • Liu, J.1    Walsh, C.T.2
  • 5
    • 0029064061 scopus 로고
    • Escherichia coli and other species of the Enterobacteriaceae encode a protein similair to the family of Mip-like FK506-binding proteins
    • Horne SM, Young KD (1995) Escherichia coli and other species of the Enterobacteriaceae encode a protein similair to the family of Mip-like FK506-binding proteins. Arch Microbiol 163: 357-365.
    • (1995) Arch Microbiol , vol.163 , pp. 357-365
    • Horne, S.M.1    Young, K.D.2
  • 6
    • 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
  • 7
    • 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.
    • (1998) EMBO J , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 8
    • 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.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 121-134
    • Duguay, A.R.1    Silhavy, T.J.2
  • 9
    • 0036302064 scopus 로고    scopus 로고
    • Peptidyl-prolyl isomerases: A new twist to transcription
    • Shaw PE (2002) Peptidyl-prolyl isomerases: a new twist to transcription. EMBO Rep 3: 521-526.
    • (2002) EMBO Rep , vol.3 , pp. 521-526
    • Shaw, P.E.1
  • 10
    • 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.
    • (2001) Mol Microbiol , vol.39 , pp. 199-210
    • Arié, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 11
    • 0038831330 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro
    • Ramm K, Plückthun A (2000) The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro. J Biol Chem 275: 17106-17113.
    • (2000) J Biol Chem , vol.275 , pp. 17106-17113
    • Ramm, K.1    Plückthun, A.2
  • 12
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouvière PE, Gross CA (1996) SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev 10: 3170-3182.
    • (1996) Genes Dev , vol.10 , pp. 3170-3182
    • Rouvière, P.E.1    Gross, C.A.2
  • 13
    • 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, et al. (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.
    • (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
  • 14
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vitro 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 vitro and has chaperone activity. EMBO J 20: 285-294.
    • (2001) EMBO J , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    de Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TI, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.I.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5
  • 18
    • 33645827531 scopus 로고    scopus 로고
    • Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: A comparative gerromics approach
    • Chen SL, Hung CS, Xu J, Reigstad CS, Magrini V, et al. (2006) Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: A comparative gerromics approach. Proc Natl Acad Sci U S A 103: 5977-5982.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5977-5982
    • Chen, S.L.1    Hung, C.S.2    Xu, J.3    Reigstad, C.S.4    Magrini, V.5
  • 19
    • 0036849659 scopus 로고    scopus 로고
    • Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins
    • Bitto E, McKay DB (2002) Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure (Camb) 10: 1489-1498.
    • (2002) Structure (Camb) , vol.10 , pp. 1489-1498
    • Bitto, E.1    McKay, D.B.2
  • 20
    • 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.
    • (2003) J Biol Chem , vol.278 , pp. 49316-49322
    • Bitto, E.1    McKay, D.B.2
  • 21
    • 2942622465 scopus 로고    scopus 로고
    • Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins
    • Bitto E, McKay DB (2004) Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins. FEBS Lett 568: 94-98.
    • (2004) FEBS Lett , vol.568 , pp. 94-98
    • Bitto, E.1    McKay, D.B.2
  • 22
    • 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.
    • (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
  • 23
    • 0035824680 scopus 로고    scopus 로고
    • Interaction of the periplasmic peptidylprolyl cis-trans isomerase SmA with model peptides. The N-terminal region of SurA is essential and sufficient for peptide binding
    • Webb HM, Ruddock LW, Marchant RJ, Jonas K, Klappa P (2001) Interaction of the periplasmic peptidylprolyl cis-trans isomerase SmA with model peptides. The N-terminal region of SurA is essential and sufficient for peptide binding. J Biol Chem 276: 45622-45627.
    • (2001) J Biol Chem , vol.276 , pp. 45622-45627
    • Webb, H.M.1    Ruddock, L.W.2    Marchant, R.J.3    Jonas, K.4    Klappa, P.5
  • 24
    • 0034978222 scopus 로고    scopus 로고
    • Establishment of a persistent Escherichia coli reservoir during the acute phase of a bladder infection
    • Mulvey MA, Schilling JD, Hultgren SJ (2001) Establishment of a persistent Escherichia coli reservoir during the acute phase of a bladder infection. Infect Immun 69: 4572-4579.
    • (2001) Infect Immun , vol.69 , pp. 4572-4579
    • Mulvey, M.A.1    Schilling, J.D.2    Hultgren, S.J.3
  • 25
    • 21544483771 scopus 로고    scopus 로고
    • Suppression of bladder epithelial cytokine responses by uropathogenic Escherichia coli
    • Hunstad DA, Justice SS, Hung CS, Lauer SR, Hultgren SJ (2005) Suppression of bladder epithelial cytokine responses by uropathogenic Escherichia coli. Infect Immun 73: 3999-4006.
    • (2005) Infect Immun , vol.73 , pp. 3999-4006
    • Hunstad, D.A.1    Justice, S.S.2    Hung, C.S.3    Lauer, S.R.4    Hultgren, S.J.5
  • 28
    • 33746656682 scopus 로고    scopus 로고
    • Maturation of intracellular Escherichia coli communities requires SurA
    • Justice SS, Lauer SR, Hultgren SJ, Hunstad DA (2006) Maturation of intracellular Escherichia coli communities requires SurA. Infect Immun 74: 4793-4800.
    • (2006) Infect Immun , vol.74 , pp. 4793-4800
    • Justice, S.S.1    Lauer, S.R.2    Hultgren, S.J.3    Hunstad, D.A.4
  • 29
    • 0027992183 scopus 로고
    • Measurement of invasion by gentamicin resistance
    • Elsinghorst EA (1994) Measurement of invasion by gentamicin resistance. Methods Enzymol 236: 405-420.
    • (1994) Methods Enzymol , vol.236 , pp. 405-420
    • Elsinghorst, E.A.1
  • 30
    • 34548851967 scopus 로고    scopus 로고
    • The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues
    • Xu X, Wang S, Hu YX, McKay DB (2007) The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. J Mol Biol 373: 367-381.
    • (2007) J Mol Biol , vol.373 , pp. 367-381
    • Xu, X.1    Wang, S.2    Hu, Y.X.3    McKay, D.B.4
  • 31
    • 0033953691 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhiminum surA mutants are attenuated and effective live oral vaccines
    • Sydenham M, Douce G, Bowe F, Ahmed S, Chatfield S, et al. (2000) Salmonella enterica serovar Typhiminum surA mutants are attenuated and effective live oral vaccines. Infect Immun 68: 1109-1115.
    • (2000) Infect Immun , vol.68 , pp. 1109-1115
    • Sydenham, M.1    Douce, G.2    Bowe, F.3    Ahmed, S.4    Chatfield, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.