메뉴 건너뛰기




Volumn 277, Issue 22, 2010, Pages 4755-4765

Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily

Author keywords

Bordetella; Outer membrane protein; Protein structure; Protein transport; Two partner secretion

Indexed keywords

BACTERIAL PROTEIN; FILAMENTOUS HAEMAGGLUTININ ADHESIN C; TPSA PROTEIN; TPSB PROTEIN; UNCLASSIFIED DRUG;

EID: 78049291824     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07881.x     Document Type: Article
Times cited : (36)

References (36)
  • 1
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67, 593-656.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 2
    • 8844235655 scopus 로고    scopus 로고
    • Protein secretion through autotransporter and two-partner pathways
    • Jacob-Dubuisson F, Fernandez R & Coutte L (2004) Protein secretion through autotransporter and two-partner pathways. Biochim Biophys Acta 1694, 235-257.
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 235-257
    • Jacob-Dubuisson, F.1    Fernandez, R.2    Coutte, L.3
  • 4
    • 28244436432 scopus 로고    scopus 로고
    • Molecular architecture and function of the Omp85 family of proteins
    • Gentle IE, Burri L & Lithgow T (2005) Molecular architecture and function of the Omp85 family of proteins. Mol Microbiol 58, 1216-1225.
    • (2005) Mol Microbiol , vol.58 , pp. 1216-1225
    • Gentle, I.E.1    Burri, L.2    Lithgow, T.3
  • 5
    • 77952946054 scopus 로고    scopus 로고
    • Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85
    • Koenig P, Mirus O, Haarmann R, Sommer MS, Sinning I, Schleiff E & Tews I (2010) Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85. J Biol Chem 285, 18016-18024.
    • (2010) J Biol Chem , vol.285 , pp. 18016-18024
    • Koenig, P.1    Mirus, O.2    Haarmann, R.3    Sommer, M.S.4    Sinning, I.5    Schleiff, E.6    Tews, I.7
  • 6
    • 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.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 7
    • 36749048640 scopus 로고    scopus 로고
    • Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain
    • Bos MP, Robert V & Tommassen J (2007) Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain. EMBO Rep 8, 1149-1154.
    • (2007) EMBO Rep , vol.8 , pp. 1149-1154
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 8
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: the role of the BAM complex in outer membrane protein assembly
    • Knowles TJ, Scott-Tucker A, Overduin M & Henderson IR (2009) Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat Rev Microbiol 7, 206-214.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 11
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle I, Gabriel K, Beech P, Waller R & Lithgow T (2004) The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J Cell Biol 164, 19-24.
    • (2004) J Cell Biol , vol.164 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 12
    • 27844456862 scopus 로고    scopus 로고
    • Membrane protein insertion: mixing eukaryotic and prokaryotic concepts
    • Schleiff E & Soll J (2005) Membrane protein insertion: mixing eukaryotic and prokaryotic concepts. EMBO Rep 6, 1023-1027.
    • (2005) EMBO Rep , vol.6 , pp. 1023-1027
    • Schleiff, E.1    Soll, J.2
  • 13
    • 33748496461 scopus 로고    scopus 로고
    • Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate
    • Hodak H, Clantin B, Willery E, Villeret V, Locht C & Jacob-Dubuisson F (2006) Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate. Mol Microbiol 61, 368-382.
    • (2006) Mol Microbiol , vol.61 , pp. 368-382
    • Hodak, H.1    Clantin, B.2    Willery, E.3    Villeret, V.4    Locht, C.5    Jacob-Dubuisson, F.6
  • 14
    • 33644871665 scopus 로고    scopus 로고
    • Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore
    • Meli AC, Hodak H, Clantin B, Locht C, Molle G, Jacob-Dubuisson F & Saint N (2006) Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore. J Biol Chem 281, 158-166.
    • (2006) J Biol Chem , vol.281 , pp. 158-166
    • Meli, A.C.1    Hodak, H.2    Clantin, B.3    Locht, C.4    Molle, G.5    Jacob-Dubuisson, F.6    Saint, N.7
  • 15
    • 1942437434 scopus 로고    scopus 로고
    • The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway
    • Clantin B, Hodak H, Willery E, Locht C, Jacob-Dubuisson F & Villeret V (2004) The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway. Proc Natl Acad Sci USA 101, 6194-6199.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6194-6199
    • Clantin, B.1    Hodak, H.2    Willery, E.3    Locht, C.4    Jacob-Dubuisson, F.5    Villeret, V.6
  • 16
    • 35649021756 scopus 로고    scopus 로고
    • The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion
    • Yeo HJ, Yokoyama T, Walkiewicz K, Kim Y, Grass S & Geme JW III (2007) The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion. J Biol Chem 282, 31076-31084.
    • (2007) J Biol Chem , vol.282 , pp. 31076-31084
    • Yeo, H.J.1    Yokoyama, T.2    Walkiewicz, K.3    Kim, Y.4    Grass, S.5    Geme III, J.W.6
  • 19
    • 33747790227 scopus 로고    scopus 로고
    • The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of Type V secretory proteins
    • Kajava AV & Steven AC (2006) The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of Type V secretory proteins. J Struct Biol 155, 306-315.
    • (2006) J Struct Biol , vol.155 , pp. 306-315
    • Kajava, A.V.1    Steven, A.C.2
  • 20
    • 0035035580 scopus 로고    scopus 로고
    • Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins
    • Jacob-Dubuisson F, Locht C & Antoine R (2001) Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Mol Microbiol 40, 306-313.
    • (2001) Mol Microbiol , vol.40 , pp. 306-313
    • Jacob-Dubuisson, F.1    Locht, C.2    Antoine, R.3
  • 22
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins
    • Sanchez-Pulido L, Devos D, Genevrois S, Vicente M & Valencia A (2003) POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins. Trends Biochem Sci 28, 523-526.
    • (2003) Trends Biochem Sci , vol.28 , pp. 523-526
    • Sanchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 23
    • 0033621401 scopus 로고    scopus 로고
    • Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin
    • Jacob-Dubuisson F, El-Hamel C, Saint N, Guedin S, Willery E, Molle G & Locht C (1999) Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J Biol Chem 274, 37731-37735.
    • (1999) J Biol Chem , vol.274 , pp. 37731-37735
    • Jacob-Dubuisson, F.1    El-Hamel, C.2    Saint, N.3    Guedin, S.4    Willery, E.5    Molle, G.6    Locht, C.7
  • 24
    • 23344442676 scopus 로고    scopus 로고
    • The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains
    • Ertel F, Mirus O, Bredemeier R, Moslavac S, Becker T & Schleiff E (2005) The evolutionarily related beta-barrel polypeptide transporters from Pisum sativum and Nostoc PCC7120 contain two distinct functional domains. J Biol Chem 280, 28281-28289.
    • (2005) J Biol Chem , vol.280 , pp. 28281-28289
    • Ertel, F.1    Mirus, O.2    Bredemeier, R.3    Moslavac, S.4    Becker, T.5    Schleiff, E.6
  • 25
    • 33751056360 scopus 로고    scopus 로고
    • Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif
    • Robert V, Volokhina EB, Senf F, Bos MP, Van Gelder P & Tommassen J (2006) Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif. PLoS Biol 4, e377.
    • (2006) PLoS Biol , vol.4
    • Robert, V.1    Volokhina, E.B.2    Senf, F.3    Bos, M.P.4    Van Gelder, P.5    Tommassen, J.6
  • 26
    • 33750287565 scopus 로고    scopus 로고
    • Characterization of pores formed by YaeT (Omp85) from Escherichia coli
    • Stegmeier JF & Andersen C (2006) Characterization of pores formed by YaeT (Omp85) from Escherichia coli. J Biochem 140, 275-283.
    • (2006) J Biochem , vol.140 , pp. 275-283
    • Stegmeier, J.F.1    Andersen, C.2
  • 30
    • 77952894531 scopus 로고    scopus 로고
    • Omp85 from the thermophilic cyanobacterium Thermosynechococcus elongatus differs from proteobacterial Omp85 in structure and domain composition
    • Arnold T, Zeth K & Linke D (2010) Omp85 from the thermophilic cyanobacterium Thermosynechococcus elongatus differs from proteobacterial Omp85 in structure and domain composition. J Biol Chem 285, 18003-18015.
    • (2010) J Biol Chem , vol.285 , pp. 18003-18015
    • Arnold, T.1    Zeth, K.2    Linke, D.3
  • 32
    • 0034730655 scopus 로고    scopus 로고
    • Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin
    • Guedin S, Willery E, Tommassen J, Fort E, Drobecq H, Locht C & Jacob-Dubuisson F (2000) Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J Biol Chem 275, 30202-30210.
    • (2000) J Biol Chem , vol.275 , pp. 30202-30210
    • Guedin, S.1    Willery, E.2    Tommassen, J.3    Fort, E.4    Drobecq, H.5    Locht, C.6    Jacob-Dubuisson, F.7
  • 33
    • 0035903666 scopus 로고    scopus 로고
    • Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway
    • Coutte L, Antoine R, Drobecq H, Locht C & Jacob-Dubuisson F (2001) Subtilisin-like autotransporter serves as maturation protease in a bacterial secretion pathway. EMBO J 20, 5040-5048.
    • (2001) EMBO J , vol.20 , pp. 5040-5048
    • Coutte, L.1    Antoine, R.2    Drobecq, H.3    Locht, C.4    Jacob-Dubuisson, F.5
  • 34
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26, 795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 35
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2, 2728-2733.
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.