메뉴 건너뛰기




Volumn 22, Issue 4, 2014, Pages 582-589

Independent domain assembly in a trapped folding intermediate of multimeric outer membrane secretins

Author keywords

[No Author keywords available]

Indexed keywords

OUTER MEMBRANE PROTEIN; PEPTIDE; PROTEIN PULD; PROTEIN XCPQ; SECRETIN; UNCLASSIFIED DRUG; LIPOSOME; PULD PROTEIN; BACTERIAL PROTEIN; MEMBRANE PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN; XCPQ PROTEIN, PSEUDOMONAS AERUGINOSA;

EID: 84898437564     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.02.009     Document Type: Article
Times cited : (10)

References (42)
  • 1
    • 33846901901 scopus 로고    scopus 로고
    • Intermediates: Ubiquitous species on folding energy landscapes?
    • D.J. Brockwell, and S.E. Radford Intermediates: ubiquitous species on folding energy landscapes? Curr. Opin. Struct. Biol. 17 2007 30 37
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 30-37
    • Brockwell, D.J.1    Radford, S.E.2
  • 3
    • 1642581491 scopus 로고    scopus 로고
    • A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compounds
    • C.J. Chen, D.M. Tobiason, C.E. Thomas, W.M. Shafer, H.S. Seifert, and P.F. Sparling A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compounds J. Bacteriol. 186 2004 730 739
    • (2004) J. Bacteriol. , vol.186 , pp. 730-739
    • Chen, C.J.1    Tobiason, D.M.2    Thomas, C.E.3    Shafer, W.M.4    Seifert, H.S.5    Sparling, P.F.6
  • 6
    • 84862605391 scopus 로고    scopus 로고
    • Packing a punch: The mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins
    • M.A. Dunstone, and R.K. Tweten Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins Curr. Opin. Struct. Biol. 22 2012 342 349
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 9
    • 16344376554 scopus 로고    scopus 로고
    • A simple statistical method for discriminating outer membrane proteins with better accuracy
    • M.M. Gromiha, and M. Suwa A simple statistical method for discriminating outer membrane proteins with better accuracy Bioinformatics 21 2005 961 968
    • (2005) Bioinformatics , vol.21 , pp. 961-968
    • Gromiha, M.M.1    Suwa, M.2
  • 11
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: Are there distinct domains for multimerization and secretion specificity?
    • I. Guilvout, K.R. Hardie, N. Sauvonnet, and A.P. Pugsley Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity? J. Bacteriol. 181 1999 7212 7220
    • (1999) J. Bacteriol. , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 12
    • 33751086145 scopus 로고    scopus 로고
    • Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin
    • I. Guilvout, M. Chami, A. Engel, A.P. Pugsley, and N. Bayan Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin EMBO J. 25 2006 5241 5249
    • (2006) EMBO J. , vol.25 , pp. 5241-5249
    • Guilvout, I.1    Chami, M.2    Engel, A.3    Pugsley, A.P.4    Bayan, N.5
  • 13
  • 14
    • 79952105841 scopus 로고    scopus 로고
    • Multimerization-defective variants of dodecameric secretin PulD
    • I. Guilvout, N.N. Nickerson, M. Chami, and A.P. Pugsley Multimerization-defective variants of dodecameric secretin PulD Res. Microbiol. 162 2011 180 190
    • (2011) Res. Microbiol. , vol.162 , pp. 180-190
    • Guilvout, I.1    Nickerson, N.N.2    Chami, M.3    Pugsley, A.P.4
  • 15
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • K.R. Hardie, S. Lory, and A.P. Pugsley Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein EMBO J. 15 1996 978 988
    • (1996) EMBO J. , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 16
    • 34247850883 scopus 로고    scopus 로고
    • PilQ Missense mutations have diverse effects on PilQ multimer formation, piliation, and pilus function in Neisseria gonorrhoeae
    • R.A. Helm, M.M. Barnhart, and H.S. Seifert pilQ Missense mutations have diverse effects on PilQ multimer formation, piliation, and pilus function in Neisseria gonorrhoeae J. Bacteriol. 189 2007 3198 3207
    • (2007) J. Bacteriol. , vol.189 , pp. 3198-3207
    • Helm, R.A.1    Barnhart, M.M.2    Seifert, H.S.3
  • 17
    • 84855218868 scopus 로고    scopus 로고
    • Outer membrane targeting of Pseudomonas aeruginosa proteins shows variable dependence on the components of Bam and Lol machineries
    • e00246-11
    • H.H. Hoang, N.N. Nickerson, V.T. Lee, A. Kazimirova, M. Chami, A.P. Pugsley, and S. Lory Outer membrane targeting of Pseudomonas aeruginosa proteins shows variable dependence on the components of Bam and Lol machineries MBio. 2 2011 e00246-11
    • (2011) MBio. , vol.2
    • Hoang, H.H.1    Nickerson, N.N.2    Lee, V.T.3    Kazimirova, A.4    Chami, M.5    Pugsley, A.P.6    Lory, S.7
  • 19
    • 84886912356 scopus 로고    scopus 로고
    • Sequential steps in the assembly of the multimeric outer membrane secretin PulD
    • G.H. Huysmans, I. Guilvout, and A.P. Pugsley Sequential steps in the assembly of the multimeric outer membrane secretin PulD J. Biol. Chem. 288 2013 30700 30707
    • (2013) J. Biol. Chem. , vol.288 , pp. 30700-30707
    • Huysmans, G.H.1    Guilvout, I.2    Pugsley, A.P.3
  • 21
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • S.E. Jackson How do small single-domain proteins fold? Fold. Des. 3 1998 R81 R91
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 22
    • 0029822373 scopus 로고    scopus 로고
    • Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism
    • J.H. Kleinschmidt, and L.K. Tamm Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism Biochemistry 35 1996 12993 13000
    • (1996) Biochemistry , vol.35 , pp. 12993-13000
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 23
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • K.V. Korotkov, E. Pardon, J. Steyaert, and W.G. Hol Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody Structure 17 2009 255 265
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 24
    • 84859885138 scopus 로고    scopus 로고
    • The type II secretion system: Biogenesis, molecular architecture and mechanism
    • K.V. Korotkov, M. Sandkvist, and W.G. Hol The type II secretion system: biogenesis, molecular architecture and mechanism Nat. Rev. Microbiol. 10 2012 336 351
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 336-351
    • Korotkov, K.V.1    Sandkvist, M.2    Hol, W.G.3
  • 25
    • 77956501272 scopus 로고    scopus 로고
    • A transient and low-populated protein-folding intermediate at atomic resolution
    • D.M. Korzhnev, T.L. Religa, W. Banachewicz, A.R. Fersht, and L.E. Kay A transient and low-populated protein-folding intermediate at atomic resolution Science 329 2010 1312 1316
    • (2010) Science , vol.329 , pp. 1312-1316
    • Korzhnev, D.M.1    Religa, T.L.2    Banachewicz, W.3    Fersht, A.R.4    Kay, L.E.5
  • 26
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • S.J. Ludtke, P.R. Baldwin, and W. Chiu EMAN: semiautomated software for high-resolution single-particle reconstructions J. Struct. Biol. 128 1999 82 97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 29
    • 79959326174 scopus 로고    scopus 로고
    • Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion
    • D.W. Meinhold, and P.E. Wright Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion Proc. Natl. Acad. Sci. USA 108 2011 9078 9083
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 9078-9083
    • Meinhold, D.W.1    Wright, P.E.2
  • 31
    • 0022365856 scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • S. Michaelis, C. Chapon, C. D'Enfert, A.P. Pugsley, and M. Schwartz Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae J. Bacteriol. 164 1985 633 638
    • (1985) J. Bacteriol. , vol.164 , pp. 633-638
    • Michaelis, S.1    Chapon, C.2    D'Enfert, C.3    Pugsley, A.P.4    Schwartz, M.5
  • 33
    • 84866370622 scopus 로고    scopus 로고
    • A single amino acid substitution changes the self-assembly status of a type IV piliation secretin
    • N.N. Nickerson, S.S. Abby, E.P. Rocha, M. Chami, and A.P. Pugsley A single amino acid substitution changes the self-assembly status of a type IV piliation secretin J. Bacteriol. 194 2012 4951 4958
    • (2012) J. Bacteriol. , vol.194 , pp. 4951-4958
    • Nickerson, N.N.1    Abby, S.S.2    Rocha, E.P.3    Chami, M.4    Pugsley, A.P.5
  • 34
    • 0034657105 scopus 로고    scopus 로고
    • Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy
    • N. Nouwen, H. Stahlberg, A.P. Pugsley, and A. Engel Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy EMBO J. 19 2000 2229 2236
    • (2000) EMBO J. , vol.19 , pp. 2229-2236
    • Nouwen, N.1    Stahlberg, H.2    Pugsley, A.P.3    Engel, A.4
  • 35
    • 77957813869 scopus 로고    scopus 로고
    • Structure of the cholera toxin secretion channel in its closed state
    • S.L. Reichow, K.V. Korotkov, W.G. Hol, and T. Gonen Structure of the cholera toxin secretion channel in its closed state Nat. Struct. Mol. Biol. 17 2010 1226 1232
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1226-1232
    • Reichow, S.L.1    Korotkov, K.V.2    Hol, W.G.3    Gonen, T.4
  • 36
    • 27144532135 scopus 로고    scopus 로고
    • Solution structure of a protein denatured state and folding intermediate
    • T.L. Religa, J.S. Markson, U. Mayor, S.M. Freund, and A.R. Fersht Solution structure of a protein denatured state and folding intermediate Nature 437 2005 1053 1056
    • (2005) Nature , vol.437 , pp. 1053-1056
    • Religa, T.L.1    Markson, J.S.2    Mayor, U.3    Freund, S.M.4    Fersht, A.R.5
  • 40
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • S.J. Tilley, and H.R. Saibil The mechanism of pore formation by bacterial toxins Curr. Opin. Struct. Biol. 16 2006 230 236
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 41
    • 84863724751 scopus 로고    scopus 로고
    • Visualizing transient protein-folding intermediates by tryptophan-scanning mutagenesis
    • A. Vallée-Bélisle, and S.W. Michnick Visualizing transient protein-folding intermediates by tryptophan-scanning mutagenesis Nat. Struct. Mol. Biol. 19 2012 731 736
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 731-736
    • Vallée-Bélisle, A.1    Michnick, S.W.2
  • 42
    • 84872358471 scopus 로고    scopus 로고
    • New insights into the assembly of bacterial secretins: Structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa
    • R. Van der Meeren, Y. Wen, P. Van Gelder, J. Tommassen, B. Devreese, and S.N. Savvides New insights into the assembly of bacterial secretins: structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa J. Biol. Chem. 288 2013 1214 1225
    • (2013) J. Biol. Chem. , vol.288 , pp. 1214-1225
    • Van Der Meeren, R.1    Wen, Y.2    Van Gelder, P.3    Tommassen, J.4    Devreese, B.5    Savvides, S.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.