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Volumn 184, Issue 22, 2002, Pages 6260-6269

Bacterial outer membrane ushers contain distinct targeting and assembly domains for pilus biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE;

EID: 0036842083     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.22.6260-6269.2002     Document Type: Article
Times cited : (70)

References (42)
  • 2
    • 0025057970 scopus 로고
    • In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT
    • Baneyx, F., and G. Georgiou. 1990. In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT. J. Bacteriol. 172:491-494.
    • (1990) J. Bacteriol. , vol.172 , pp. 491-494
    • Baneyx, F.1    Georgiou, G.2
  • 3
    • 0020645046 scopus 로고
    • Kilo-sequencing: Creation of an ordered nest of asymmetric deletions across a large target sequence carried on phage M13
    • Barnes, W. M., M. Bevan, and P. H. Son. 1983. Kilo-sequencing: Creation of an ordered nest of asymmetric deletions across a large target sequence carried on phage M13. Methods Enzymol. 101:98-122.
    • (1983) Methods Enzymol. , vol.101 , pp. 98-122
    • Barnes, W.M.1    Bevan, M.2    Son, P.H.3
  • 5
    • 0025740667 scopus 로고
    • Type 1 fimbriae mutants of Escherichia coli K12: Characterization of recognized afimbriate strains and construction of new fim deletion mutants
    • Blomfield, I. C., M. S. McClain, and B. I. Eisenstein. 1991. Type 1 fimbriae mutants of Escherichia coli K12: Characterization of recognized afimbriate strains and construction of new fim deletion mutants. Mol. Microbiol. 5:1439-1445.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1439-1445
    • Blomfield, I.C.1    McClain, M.S.2    Eisenstein, B.I.3
  • 7
    • 0028794484 scopus 로고
    • Structural polymorphism of bacterial adhesion pili
    • Bullitt, E., and L. Makowski. 1995. Structural polymorphism of bacterial adhesion pili. Nature 373:164-167.
    • (1995) Nature , vol.373 , pp. 164-167
    • Bullitt, E.1    Makowski, L.2
  • 9
    • 0027190626 scopus 로고
    • An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum
    • Deléage, G., and C. Geourjon. 1993. An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput. Appl. Biosci. 9:197-199.
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 197-199
    • Deléage, G.1    Geourjon, C.2
  • 10
    • 0027483426 scopus 로고
    • Outer membrane PapC usher discriminately recognizes periplasmic chaperone-pilus subunit complexes
    • Dodson, K. W., F. Jacob-Dubuisson, R. T. Striker, and S. J. Hultgren. 1993. Outer membrane PapC 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
  • 11
    • 0035875099 scopus 로고    scopus 로고
    • Structural basis of the Interaction of the pyelonephritic E. coli adhesin to Its human kidney receptor
    • Dodson, K. W., J. S. Pinkner, T. Rose, G. Magnusson, S. J. Hultgren, and G. J. Waksman. 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.J.6
  • 12
    • 0033223439 scopus 로고    scopus 로고
    • Epitope tagging analysis of the outer membrane folding of the molecular usher FaeD involved in K88 fimbriae biosynthesis in Escherichia coli
    • Harms, N., W. C. Oudhuis, E. A. Eppens, Q. A. Valent, M. Koster, J. Luirink, and B. Oudega. 1999. Epitope tagging analysis of the outer membrane folding of the molecular usher FaeD involved in K88 fimbriae biosynthesis in Escherichia coli. J. Mol. Microbiol. Biotechnol. 1:319-325.
    • (1999) J. Mol. Microbiol. Biotechnol. , vol.1 , pp. 319-325
    • Harms, N.1    Oudhuis, W.C.2    Eppens, E.A.3    Valent, Q.A.4    Koster, M.5    Luirink, J.6    Oudega, B.7
  • 13
    • 0024468229 scopus 로고
    • Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
    • Holmgren, A., and C. Brändén. 1989. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature 342:248-251.
    • (1989) Nature , vol.342 , pp. 248-251
    • Holmgren, A.1    Brändén, C.2
  • 14
    • 0028302264 scopus 로고
    • Chaperone-assisted self-assembly of pili independent of cellular energy
    • Jacob-Dubuisson, F., R. Striker, and S. J. Hultgren. 1994. Chaperone-assisted self-assembly of pili independent of cellular energy. J. Biol. Chem. 269:12447-12455.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12447-12455
    • Jacob-Dubuisson, F.1    Striker, R.2    Hultgren, S.J.3
  • 15
    • 0030775342 scopus 로고    scopus 로고
    • The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
    • Jones, C. H., P. N. Danese, J. S. Pinkner, T. J. Silhavy, and S. J. Hultgren. 1997. The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems. EMBO J. 16:6394-6406.
    • (1997) EMBO J. , vol.16 , pp. 6394-6406
    • Jones, C.H.1    Danese, P.N.2    Pinkner, J.S.3    Silhavy, T.J.4    Hultgren, S.J.5
  • 18
    • 0025069863 scopus 로고
    • The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae
    • Klemm, P., and G. Christiansen. 1990. The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae. Mol. Gen. Genet. 220:334-338.
    • (1990) Mol. Gen. Genet. , vol.220 , pp. 334-338
    • Klemm, P.1    Christiansen, G.2
  • 19
    • 0028919373 scopus 로고
    • The export systems of type 1 and F1C fimbriae are interchangeable but work in parental pairs
    • Klemm, P., B. J. Jorgensen, B. Kreft, and G. Christiansen. 1995. The export systems of type 1 and F1C fimbriae are interchangeable but work in parental pairs. J. Bacteriol. 177:621-627.
    • (1995) J. Bacteriol. , vol.177 , pp. 621-627
    • Klemm, P.1    Jorgensen, B.J.2    Kreft, B.3    Christiansen, G.4
  • 20
    • 0026509588 scopus 로고
    • P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips
    • Kuehn, M. J., J. Heuser, S. Normark, and S. J. Hultgren. 1992. P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips. Nature 356:252-255.
    • (1992) Nature , vol.356 , pp. 252-255
    • Kuehn, M.J.1    Heuser, J.2    Normark, S.3    Hultgren, S.J.4
  • 21
    • 0025885694 scopus 로고
    • Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits
    • Kuehn, M. J., S. Normark., and S. J. Hultgren. 1991. Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits. Proc. Natl. Acad. Sci. USA 88:10586-10590.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10586-10590
    • Kuehn, M.J.1    Normark, S.2    Hultgren, S.J.3
  • 22
    • 0025991209 scopus 로고
    • Mapping and topographic localization of epitopes of the Yersinia pseudotuberculosis invasin protein
    • Leong, J. M., R. S. Fournier, and R. R. Isberg. 1991. Mapping and topographic localization of epitopes of the Yersinia pseudotuberculosis invasin protein. Infect. Immun. 59:3424-3433.
    • (1991) Infect. Immun. , vol.59 , pp. 3424-3433
    • Leong, J.M.1    Fournier, R.S.2    Isberg, R.R.3
  • 23
    • 0022392964 scopus 로고
    • A new locus, pilE, required for the binding of type 1 piliated Escherichia coli to erythrocytes
    • Maurer, L., and P. E. Orndorff. 1985. A new locus, pilE, required for the binding of type 1 piliated Escherichia coli to erythrocytes. FEMS Microbiol. Lett. 30:59-66.
    • (1985) FEMS Microbiol. Lett. , vol.30 , pp. 59-66
    • Maurer, L.1    Orndorff, P.E.2
  • 24
    • 0035148522 scopus 로고    scopus 로고
    • Biosynthesis of K88 fimbriae in Escherichia coli: Interaction of tip-subunit FaeC with the periplasmic chaperone FaeE and the outer membrane usher FaeD
    • Mol, O., W. C. Oudhuis, R. Oud, R. Sijbrandi, J. Luirink, N. Harms, and B. Oudega. 2001. Biosynthesis of K88 fimbriae in Escherichia coli: Interaction of tip-subunit FaeC with the periplasmic chaperone FaeE and the outer membrane usher FaeD. J. Mol. Microbiol. Biotechnol. 3:135-142.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 135-142
    • Mol, O.1    Oudhuis, W.C.2    Oud, R.3    Sijbrandi, R.4    Luirink, J.5    Harms, N.6    Oudega, B.7
  • 25
    • 0028298380 scopus 로고
    • Isolation of outer membranes
    • Nikaido, H. 1994. Isolation of outer membranes. Methods Enzymol. 235:225-234.
    • (1994) Methods Enzymol. , vol.235 , pp. 225-234
    • Nikaido, H.1
  • 26
    • 0023412066 scopus 로고
    • Nucleotide sequence, regulation and functional analysis of the papC gene required for cell surface localization of Pap pili of uropathogenic Escherichia coli
    • Norgren, M., M. Baga, J. M. Tennent, and S. Normark. 1987. Nucleotide sequence, regulation and functional analysis of the papC gene required for cell surface localization of Pap pili of uropathogenic Escherichia coli. Mol. Microbiol. 1:169-178.
    • (1987) Mol. Microbiol. , vol.1 , pp. 169-178
    • Norgren, M.1    Baga, M.2    Tennent, J.M.3    Normark, S.4
  • 27
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.1
  • 28
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., and C. Sander. 1993. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 30
    • 0034255260 scopus 로고    scopus 로고
    • Snapshots of ushermediated protein secretion and ordered pilus assembly
    • Saulino, E. T., E. Bullitt, and S. J. Hultgren. 2000. Snapshots of ushermediated protein secretion and ordered pilus assembly. Proc. Natl. Acad. Sci. USA 97:9240-9245.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9240-9245
    • Saulino, E.T.1    Bullitt, E.2    Hultgren, S.J.3
  • 31
    • 0032522714 scopus 로고    scopus 로고
    • Ramifications of kinetic partitioning on usher-mediated pilus biogenesis
    • Saulino, E. T., D. G. Thanassi, J. S. Pinkner, and S. J. Hultgren. 1998. Ramifications of kinetic partitioning on usher-mediated pilus biogenesis. EMBO J. 17:2177-2185.
    • (1998) EMBO J. , vol.17 , pp. 2177-2185
    • Saulino, E.T.1    Thanassi, D.G.2    Pinkner, J.S.3    Hultgren, S.J.4
  • 32
    • 0028121757 scopus 로고
    • Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli
    • Schifferli, D. M., and M. A. Alrutz. 1994. Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli. J. Bacteriol. 176:1099-1110.
    • (1994) J. Bacteriol. , vol.176 , pp. 1099-1110
    • Schifferli, D.M.1    Alrutz, M.A.2
  • 33
    • 0027161268 scopus 로고
    • Prediction of membrane-spanning β-strands and its application to maltoporin
    • Schirmer, T., and S. W. Cowan. 1993. Prediction of membrane-spanning β-strands and its application to maltoporin. Protein Sci. 2:1361-1363.
    • (1993) Protein Sci. , vol.2 , pp. 1361-1363
    • Schirmer, T.1    Cowan, S.W.2
  • 34
    • 0015651967 scopus 로고
    • Outer membrane proteins of Escherichia coli. I. Effect of preparative conditions on the migration of protein in polyacrylamide gels
    • Schnaitman, C. A. 1973. Outer membrane proteins of Escherichia coli. I. Effect of preparative conditions on the migration of protein in polyacrylamide gels. Arch. Biochem. Biophys. 157:541-552.
    • (1973) Arch. Biochem. Biophys. , vol.157 , pp. 541-552
    • Schnaitman, C.A.1
  • 35
    • 0033932639 scopus 로고    scopus 로고
    • β-barrel membrane proteins
    • Schulz, G. E. 2000. β-barrel membrane proteins. Curr. Opin. Struct. Biol. 10:443-447.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 443-447
    • Schulz, G.E.1
  • 36
    • 0027085578 scopus 로고
    • Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly
    • Slonim, L. N., J. S. Pinkner, C. I. Branden, and S. J. Hultgren. 1992. Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly. EMBO J. 11:4747-4756.
    • (1992) EMBO J. , vol.11 , pp. 4747-4756
    • Slonim, L.N.1    Pinkner, J.S.2    Branden, C.I.3    Hultgren, S.J.4
  • 38
    • 0029823940 scopus 로고    scopus 로고
    • Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa
    • Sugawara, E., M. Steiert, S. Rouhani, and H. Nikaido. 1996. Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa. J. Bacteriol. 178:6067-6069.
    • (1996) J. Bacteriol. , vol.178 , pp. 6067-6069
    • Sugawara, E.1    Steiert, M.2    Rouhani, S.3    Nikaido, H.4
  • 39
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi, D. G., and S. J. Hultgren. 2000. Multiple pathways allow protein secretion across the bacterial outer membrane. Curr. Opin. Cell Biol. 12:420-430.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 40
    • 0032035356 scopus 로고    scopus 로고
    • The chaperone/usher pathway: A major terminal branch of the general secretory pathway
    • Thanassi, D. G., E. T. Saulino, and S. J. Hultgren. 1998. The chaperone/ usher pathway: A major terminal branch of the general secretory pathway. Curr. Opin. Microbiol. 1:223-231.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 223-231
    • Thanassi, D.G.1    Saulino, E.T.2    Hultgren, S.J.3
  • 42
    • 0029165969 scopus 로고
    • Subcellular localization and topology of the K88 usher FaeD in Escherichia coli
    • Valent, Q. A., J. Zaal, F. K. de Graaf, and B. Oudega. 1995. Subcellular localization and topology of the K88 usher FaeD in Escherichia coli. Mol. Microbiol. 16:1243-1257.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1243-1257
    • Valent, Q.A.1    Zaal, J.2    De Graaf, F.K.3    Oudega, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.