메뉴 건너뛰기




Volumn 27, Issue 20, 2008, Pages 2669-2680

The 'P-usher', a novel protein transporter involved in fimbrial assembly and TpsA secretion

Author keywords

Chaperone usher pathway; Fimbriae; POTRA; Pseudomonas; Type Vb secretion

Indexed keywords

BACTERIAL PROTEIN; CELL SURFACE PROTEIN; PROTEIN CUPB1; PROTEIN CUPB3; PROTEIN CUPB5; PROTEIN POTRA; UNCLASSIFIED DRUG;

EID: 54349103449     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2008.197     Document Type: Article
Times cited : (26)

References (47)
  • 1
    • 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
  • 2
    • 18844400863 scopus 로고    scopus 로고
    • Structural and dynamic properties of bacterial type IV secretion systems
    • Christie PJ, Cascales E (2005) Structural and dynamic properties of bacterial type IV secretion systems. Mol Membr Biol 22: 51-61
    • (2005) Mol Membr Biol , vol.22 , pp. 51-61
    • Christie, P.J.1    Cascales, E.2
  • 4
    • 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
  • 5
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis GR (2006) The type III secretion injectisome. Nat Rev Microbiol 4: 811-825
    • (2006) Nat Rev Microbiol , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 8
    • 0027483426 scopus 로고
    • Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes
    • Dodson KW, Jacob-Dubuisson F, Striker RT, Hultgren SJ (1993) Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes. Proc Natl Acad Sci USA 90: 3670-3674
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3670-3674
    • Dodson, K.W.1    Jacob-Dubuisson, F.2    Striker, R.T.3    Hultgren, S.J.4
  • 9
    • 0035875099 scopus 로고    scopus 로고
    • Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor
    • Dodson KW, Pinkner JS, Rose T, Magnusson G, Hultgren SJ, Waksman G (2001) Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor. Cell 105: 733-743
    • (2001) Cell , vol.105 , pp. 733-743
    • Dodson, K.W.1    Pinkner, J.S.2    Rose, T.3    Magnusson, G.4    Hultgren, S.J.5    Waksman, G.6
  • 10
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux A (2004) The underlying mechanisms of type II protein secretion. Biochim Biophys Acta 1964: 163-179
    • (2004) Biochim Biophys Acta , vol.1964 , pp. 163-179
    • Filloux, A.1
  • 13
    • 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
  • 14
    • 0034034907 scopus 로고    scopus 로고
    • Maturation and secretion of the non-typable Haemophilus influenzae HMW1 adhesin: Roles of the N-terminal and C-terminal domains
    • Grass S, St Geme III JW (2000) Maturation and secretion of the non-typable Haemophilus influenzae HMW1 adhesin: roles of the N-terminal and C-terminal domains. Mol Microbiol 36: 55-67
    • (2000) Mol Microbiol , vol.36 , pp. 55-67
    • Grass, S.1    St Geme III, J.W.2
  • 16
  • 17
    • 0026076419 scopus 로고
    • Chaperone-assisted assembly and molecular architecture of adhesive pili
    • Hultgren SJ, Normark S, Abraham SN (1991) Chaperone-assisted assembly and molecular architecture of adhesive pili. Annu Rev Microbiol 45: 383-415
    • (1991) Annu Rev Microbiol , vol.45 , pp. 383-415
    • Hultgren, S.J.1    Normark, S.2    Abraham, S.N.3
  • 18
    • 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
  • 20
    • 0025837193 scopus 로고
    • A wide-host-range suicide vector for improving reverse genetics in Gram negative bacteria: Inactivation of the bla gene of Yersinia enterocolitica
    • Kaniga K, Delor L, Cornelis GR (1991) A wide-host-range suicide vector for improving reverse genetics in Gram negative bacteria: inactivation of the bla gene of Yersinia enterocolitica. Gene 109: 137-141
    • (1991) Gene , vol.109 , pp. 137-141
    • Kaniga, K.1    Delor, L.2    Cornelis, G.R.3
  • 21
    • 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, Kahne D (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    Kahne, D.6
  • 23
    • 13144257722 scopus 로고    scopus 로고
    • A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes
    • Kulasekara HD, Ventre I, Kulasekara BR, Lazdunski A, Filloux A, Lory S (2005) A novel two-component system controls the expression of Pseudomonas aeruginosa fimbrial cup genes. Mol Microbiol 55: 368-380
    • (2005) Mol Microbiol , vol.55 , pp. 368-380
    • Kulasekara, H.D.1    Ventre, I.2    Kulasekara, B.R.3    Lazdunski, A.4    Filloux, A.5    Lory, S.6
  • 24
    • 0031798664 scopus 로고    scopus 로고
    • N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin
    • Lambert-Buisine C, Willery E, Locht C, Jacob-Dubuisson F (1998) N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin. Mol Microbiol 28: 1283-1293
    • (1998) Mol Microbiol , vol.28 , pp. 1283-1293
    • Lambert-Buisine, C.1    Willery, E.2    Locht, C.3    Jacob-Dubuisson, F.4
  • 26
    • 33644871665 scopus 로고    scopus 로고
    • Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore
    • Méli 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
    • Méli, A.C.1    Hodak, H.2    Clantin, B.3    Locht, C.4    Molle, G.5    Jacob-Dubuisson, F.6    Saint, N.7
  • 27
    • 34247372309 scopus 로고    scopus 로고
    • Recognition of the N-terminal lectin domain of FimH adhesin by the usher FimD is required for type 1 pilus biogenesis
    • Munera D, Hultgren S, Fernández LA (2007) Recognition of the N-terminal lectin domain of FimH adhesin by the usher FimD is required for type 1 pilus biogenesis. Mol Microbiol 64: 333-346
    • (2007) Mol Microbiol , vol.64 , pp. 333-346
    • Munera, D.1    Hultgren, S.2    Fernández, L.A.3
  • 28
    • 3843050179 scopus 로고    scopus 로고
    • The usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events
    • Ng TW, Akman L, Osisami M, Thanassi DG (2004) The usher N terminus is the initial targeting site for chaperone-subunit complexes and participates in subsequent pilus biogenesis events. J Bacteriol 186: 5321-5331
    • (2004) J Bacteriol , vol.186 , pp. 5321-5331
    • Ng, T.W.1    Akman, L.2    Osisami, M.3    Thanassi, D.G.4
  • 29
    • 37349093031 scopus 로고    scopus 로고
    • Evolution of the chaperone/usher assembly pathway: Fimbrial classification goes Greek
    • Nuccio SP, Baümler AJ (2007) Evolution of the chaperone/usher assembly pathway: fimbrial classification goes Greek. Microbiol Mol Biol Rev 71: 551-575
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 551-575
    • Nuccio, S.P.1    Baümler, A.J.2
  • 30
    • 0029794015 scopus 로고    scopus 로고
    • Characterization of the Streptococcus pneumoniae immunoglobulin A1 protease gene (iga) and its translation product
    • Poulsen K, Reinholdt J, Kilian M (1996) Characterization of the Streptococcus pneumoniae immunoglobulin A1 protease gene (iga) and its translation product. Infect Immun 64: 3957-3966
    • (1996) Infect Immun , vol.64 , pp. 3957-3966
    • Poulsen, K.1    Reinholdt, J.2    Kilian, M.3
  • 33
    • 0033582158 scopus 로고    scopus 로고
    • The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: Identification of a cyanobacterial homolog
    • Reumann S, Davila-Aponte J, Keegstra K (1999) The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: identification of a cyanobacterial homolog. Proc Natl Acad Sci USA 96: 784-789
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 784-789
    • Reumann, S.1    Davila-Aponte, J.2    Keegstra, K.3
  • 34
    • 34247593045 scopus 로고    scopus 로고
    • Assembly of fimbrial structures in Pseudomonas aeruginosa: Functionality and specificity of chaperone-usher machineries
    • Ruer S, Stender S, Filloux A, de Bentzmann S (2007) Assembly of fimbrial structures in Pseudomonas aeruginosa: functionality and specificity of chaperone-usher machineries. J Bacteriol 189: 3547-3555
    • (2007) J Bacteriol , vol.189 , pp. 3547-3555
    • Ruer, S.1    Stender, S.2    Filloux, A.3    de Bentzmann, S.4
  • 35
    • 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
  • 37
    • 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
  • 38
    • 0027449198 scopus 로고
    • Amino acid replacements in the Serratia marcescens haemolysin ShlA define sites involved in activation and secretion
    • Schönherr R, Tsolis R, Focareta T, Braun V (1993) Amino acid replacements in the Serratia marcescens haemolysin ShlA define sites involved in activation and secretion. Mol Microbiol 9: 1229-1237
    • (1993) Mol Microbiol , vol.9 , pp. 1229-1237
    • Schönherr, R.1    Tsolis, R.2    Focareta, T.3    Braun, V.4
  • 39
    • 33645300368 scopus 로고    scopus 로고
    • Analysis of the requirements for pilus biogenesis at the outer membrane usher and the function of the usher C-terminus
    • So SS, Thanassi DG (2006) Analysis of the requirements for pilus biogenesis at the outer membrane usher and the function of the usher C-terminus. Mol Microbiol 60: 364-375
    • (2006) Mol Microbiol , vol.60 , pp. 364-375
    • So, S.S.1    Thanassi, D.G.2
  • 40
    • 0036842083 scopus 로고    scopus 로고
    • Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis
    • Thanassi DG, Stathopoulos C, Dodson K, Geiger D, Hultgren SJ (2002) Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis. J Bacteriol 184: 6260-6269
    • (2002) J Bacteriol , vol.184 , pp. 6260-6269
    • Thanassi, D.G.1    Stathopoulos, C.2    Dodson, K.3    Geiger, D.4    Hultgren, S.J.5
  • 41
    • 34548142297 scopus 로고    scopus 로고
    • Getting into and through the outer membrane
    • Tommassen J (2007) Getting into and through the outer membrane. Science 317: 903-904
    • (2007) Science , vol.317 , pp. 903-904
    • Tommassen, J.1
  • 42
    • 0035811059 scopus 로고    scopus 로고
    • The chaperone/usher pathway of Pseudomonas aeruginosa: Identification of fimbrial gene clusters (cup) and their involvement in biofilm formation
    • Vallet I, Olson JW, Lory S, Lazdunski A, Filloux A (2001) The chaperone/usher pathway of Pseudomonas aeruginosa: identification of fimbrial gene clusters (cup) and their involvement in biofilm formation. Proc Natl Acad Sci USA 98: 6911-6916
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6911-6916
    • Vallet, I.1    Olson, J.W.2    Lory, S.3    Lazdunski, A.4    Filloux, A.5
  • 43
    • 33644946448 scopus 로고    scopus 로고
    • Protein secretion and secreted proteins in pathogenic Neisseriaceae
    • van Ulsen P, Tommassen J (2006) Protein secretion and secreted proteins in pathogenic Neisseriaceae. FEMS Microbiol Rev 30: 292-319
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 292-319
    • van Ulsen, P.1    Tommassen, J.2
  • 44
    • 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
  • 45
    • 0028335286 scopus 로고
    • Mutational analysis of the Bordetella pertussis fim/fha gene cluster: Identification of a gene with sequence similarities to haemolysin accessory genes involved in export of FHA
    • Willems RJ, Geuijen C, van der Heide HG, Renauld G, Bertin P, van den Akker WM, Locht C, Mooi FR (1994) Mutational analysis of the Bordetella pertussis fim/fha gene cluster: identification of a gene with sequence similarities to haemolysin accessory genes involved in export of FHA. Mol Microbiol 11: 337-347
    • (1994) Mol Microbiol , vol.11 , pp. 337-347
    • Willems, R.J.1    Geuijen, C.2    van der Heide, H.G.3    Renauld, G.4    Bertin, P.5    van den Akker, W.M.6    Locht, C.7    Mooi, F.R.8
  • 46
    • 0033777399 scopus 로고    scopus 로고
    • ShlB mutants of Serratia marcescens allow uncoupling of activation and secretion of the ShlA hemolysin
    • Yang FL, Braun V (2000) ShlB mutants of Serratia marcescens allow uncoupling of activation and secretion of the ShlA hemolysin. Int J Med Microbiol 290: 529-538
    • (2000) Int J Med Microbiol , vol.290 , pp. 529-538
    • Yang, F.L.1    Braun, V.2
  • 47
    • 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, St Geme III JW (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    St Geme III, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.