메뉴 건너뛰기




Volumn 1, Issue 2, 1998, Pages 223-231

The chaperone/usher pathway: A major terminal branch of the general secretory pathway

Author keywords

[No Author keywords available]

Indexed keywords

NEGIBACTERIA;

EID: 0032035356     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(98)80015-5     Document Type: Article
Times cited : (162)

References (68)
  • 3
    • 0030948568 scopus 로고    scopus 로고
    • Prevention of mucosal Escherichia coli infection by FimH-adhesin-based systemic vaccination
    • Langermann S, Palaszynski S, Barnhart M, Auguste G, Pinkner JS, Burlein J, Barren P, Koenig S, Leath S, Jones CH, Hultgren SJ: Prevention of mucosal Escherichia coli infection by FimH-adhesin-based systemic vaccination. Science 1997, 276:607-611. The first demonstration that adhesin-based vaccines can provide protection against infections by pathogenic bacteria. Shows that the adhesin FimH mediates binding to the bladder epithelium and that FimH- strains are greatly reduced for piliation.
    • (1997) Science , vol.276 , pp. 607-611
    • Langermann, S.1    Palaszynski, S.2    Barnhart, M.3    Auguste, G.4    Pinkner, J.S.5    Burlein, J.6    Barren, P.7    Koenig, S.8    Leath, S.9    Jones, C.H.10    Hultgren, S.J.11
  • 4
    • 0028794484 scopus 로고
    • Structural polymorphism of bacterial adhesion pili
    • Bullitt E, Makowski L: Structural polymorphism of bacterial adhesion pili. Nature 1995, 373:164-167.
    • (1995) Nature , vol.373 , pp. 164-167
    • Bullitt, E.1    Makowski, L.2
  • 5
    • 0026509588 scopus 로고
    • P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips
    • Kuehn MJ, Heuser J, Normark S, Hultgren SJ: P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips. Nature 1992, 356:252-255.
    • (1992) Nature , vol.356 , pp. 252-255
    • Kuehn, M.J.1    Heuser, J.2    Normark, S.3    Hultgren, S.J.4
  • 7
    • 0027528505 scopus 로고
    • Initiation of assembly and association of the structural elements of a bacterial pilus depend on two specialized tip proteins
    • Jacob-Dubuisson F, Heuser J, Dodson K, Normark S, Hultgren SJ: Initiation of assembly and association of the structural elements of a bacterial pilus depend on two specialized tip proteins. EMBO J 1993, 12:837-847.
    • (1993) EMBO J , vol.12 , pp. 837-847
    • Jacob-Dubuisson, F.1    Heuser, J.2    Dodson, K.3    Normark, S.4    Hultgren, S.J.5
  • 8
    • 0023663381 scopus 로고
    • Biogenesis of E. coli Pap pili: PapH, a minor pilin subunit involved in cell anchoring and length modulation
    • Baga M, Norgren M, Normark S: Biogenesis of E. coli Pap pili: PapH, a minor pilin subunit involved in cell anchoring and length modulation. Cell 1987, 49:241-251.
    • (1987) Cell , vol.49 , pp. 241-251
    • Baga, M.1    Norgren, M.2    Normark, S.3
  • 9
    • 0026076419 scopus 로고
    • Chaperone-assisted assembly and molecular architecture of adhesive pili
    • Hultgren SJ, Normark S, Abraham SN: Chaperone-assisted assembly and molecular architecture of adhesive pili. Annu Rev Microbiol 1991, 45:383-415.
    • (1991) Annu Rev Microbiol , vol.45 , pp. 383-415
    • Hultgren, S.J.1    Normark, S.2    Abraham, S.N.3
  • 10
    • 0025885694 scopus 로고
    • Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits
    • Kuehn MJ, Normark S, Hultgren SJ: Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits. Proc Natl Acad Sci USA 1991, 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
  • 11
    • 0027483426 scopus 로고
    • Outer membrane PapC usher discriminately recognizes periplasmic chaperone-pilus subunit complexes
    • Dodson KW, Jacob-Dubuisson F, Striker RT, Hultgren SJ: Outer membrane PapC usher discriminately recognizes periplasmic chaperone-pilus subunit complexes. Proc Natl Acad Sci USA 1993, 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
  • 12
    • 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, Baga M, Tennent JM, Normark S: Nucleotide sequence, regulation and functional analysis of the papC gene required for cell surface localization of Pap pili of uropathogenic Escherichia coli. Mol Microbiol 1987, 1:169-178.
    • (1987) Mol Microbiol , vol.1 , pp. 169-178
    • Norgren, M.1    Baga, M.2    Tennent, J.M.3    Normark, S.4
  • 14
    • 0024215464 scopus 로고
    • Conservation of the D-mannose-adhesion protein among type 1 fimbriated members of the family Enterobactericeae
    • Abraham SN, Sun D, Dale JB, Beachey EH: Conservation of the D-mannose-adhesion protein among type 1 fimbriated members of the family Enterobactericeae. Nature 1988, 336:682-684.
    • (1988) Nature , vol.336 , pp. 682-684
    • Abraham, S.N.1    Sun, D.2    Dale, J.B.3    Beachey, E.H.4
  • 15
    • 0022392964 scopus 로고
    • A new locus, pilE required for the binding of type 1 piliated Escherichia coli to erythrocytes
    • Maurer L, Orndorff PE: A new locus, pilE required for the binding of type 1 piliated Escherichia coli to erythrocytes. FEMS Microbiol Lett 1985, 30:59-66.
    • (1985) FEMS Microbiol Lett , vol.30 , pp. 59-66
    • Maurer, L.1    Orndorff, P.E.2
  • 18
    • 0028153922 scopus 로고
    • FimH family of type 1 fimbrial adhesins: Functional heterogeneity due to minor sequence variations among fimH genes
    • Sokurenko EV, Courtney HS, Ohman DE, Klemm P, Hasty DL: FimH family of type 1 fimbrial adhesins: functional heterogeneity due to minor sequence variations among fimH genes. J Bacteriol 1994, 176:748-755.
    • (1994) J Bacteriol , vol.176 , pp. 748-755
    • Sokurenko, E.V.1    Courtney, H.S.2    Ohman, D.E.3    Klemm, P.4    Hasty, D.L.5
  • 19
    • 0030924003 scopus 로고    scopus 로고
    • Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection
    • Thankavel K, Madison B, Ikeda T, Malaviya R, Shah AH, Arumugam PM, Abraham SN: Localization of a domain in the FimH adhesin of Escherichia coli type 1 fimbriae capable of receptor recognition and use of a domain-specific antibody to confer protection against experimental urinary tract infection. J Clin Invest 1997, 100:1123-1136.
    • (1997) J Clin Invest , vol.100 , pp. 1123-1136
    • Thankavel, K.1    Madison, B.2    Ikeda, T.3    Malaviya, R.4    Shah, A.H.5    Arumugam, P.M.6    Abraham, S.N.7
  • 20
    • 0026779815 scopus 로고
    • Lesions in two Escherichia coli type 1 pilus genes alter pilus number and length without affecting receptor binding
    • Russell PW, Orndorff PE: Lesions in two Escherichia coli type 1 pilus genes alter pilus number and length without affecting receptor binding. J Bacteriol 1992, 174:5923-5935.
    • (1992) J Bacteriol , vol.174 , pp. 5923-5935
    • Russell, P.W.1    Orndorff, P.E.2
  • 22
    • 0025069863 scopus 로고
    • The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae
    • Klemm P, Christiansen G: The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae. Mol Gen Genet 1990, 220:334-336.
    • (1990) Mol Gen Genet , vol.220 , pp. 334-336
    • Klemm, P.1    Christiansen, G.2
  • 23
    • 0024468229 scopus 로고
    • Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
    • Holmgren A, Brändėn C: Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature 1989, 342:246-251.
    • (1989) Nature , vol.342 , pp. 246-251
    • Holmgren, A.1    Bränden, C.2
  • 25
    • 0029738256 scopus 로고    scopus 로고
    • Molecular basis of two subfamilies of immunoglobulin-like chaperones
    • Hung DL, Knight SD, Woods RM, Pinkner JS, Hultgren SJ: Molecular basis of two subfamilies of immunoglobulin-like chaperones. EMBO J 1996, 15:3792-3805. The PapD chaperone family can e divided into two subfamilies based on conserved structural differences. These two subfamilies assembly pili of distinct architecture: rod-like pili or atypical, non-pilus organelles.
    • (1996) EMBO J , vol.15 , pp. 3792-3805
    • Hung, D.L.1    Knight, S.D.2    Woods, R.M.3    Pinkner, J.S.4    Hultgren, S.J.5
  • 26
    • 0030775342 scopus 로고    scopus 로고
    • The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
    • Jones CH, Danese PN, Pinkner JS, Silhavy TJ, Hultgren SJ: The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems. EMBO J 1997, 16:6394-6406. PapD is needed for the release of subunits from the cytoplasmic membrane and their proper folding in the periplasm. Off-pathway aggregates of pilus subunits are sensed by the Cpx and sE signal transduction pathways which regulate a number of periplasmic proteases and chaperones.
    • (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
  • 28
    • 0029843213 scopus 로고    scopus 로고
    • The DegP and DegQ periplasmic endoproteases of Escherichia coli: Specificity for cleavage sites and substrate conformation
    • Kolmar H, Waller PRH, Sauer RT: The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation. J Bacieriol 1996, 178:5925-5929.
    • (1996) J Bacieriol , vol.178 , pp. 5925-5929
    • Kolmar, H.1    Waller, P.R.H.2    Sauer, R.T.3
  • 29
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • Pogliano J, Lynch AS, Belin D, Lln ECC, Beckwith J: Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system. Genes Dev 1997, 11:1169-1162. Demonstrates that the Cpx pathway activates a number of proteins involved in protein-folding and degradation in the periplasm. Identifies the consensus binding site of the CpxR response regulator.
    • (1997) Genes Dev , vol.11 , pp. 1169-11162
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lln, E.C.C.4    Beckwith, J.5
  • 30
    • 0030998321 scopus 로고    scopus 로고
    • The sE and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding systems in Escherichia coli
    • ••] shows that extracytoplasmic stress is controlled not only through protein turn over, but also protein folding.
    • (1997) Genes Dev , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 31
    • 0030611303 scopus 로고    scopus 로고
    • The σE-mediated response to extra cytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of σE
    • De Las Penas A, Connolly L, Gross CA: The σE-mediated response to extra cytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of σE. Mol Microbiol 1997, 24:373-385. Identification of cytoplasmic membrane and periplasmic components responsible for transmitting stress signals from outside the cytoplasm to the σE regulatory sigma factor. σE regulates the activity of a number of proteins, including the DegP periplasmic protease.
    • (1997) Mol Microbiol , vol.24 , pp. 373-385
    • De Las Penas, A.1    Connolly, L.2    Gross, C.A.3
  • 32
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakis D, Betton J-M, Raina S: New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol Microbiol 1996, 21:871-884.
    • (1996) Mol Microbiol , vol.21 , pp. 871-884
    • Missiakis, D.1    Betton, J.-M.2    Raina, S.3
  • 33
    • 0028302264 scopus 로고
    • Chaperone-assisted self-assembly of pili independent of cellular energy
    • Jacob Dubuisson F, Striker R, Hultgren SJ: Chaperone-assisted self-assembly of pili independent of cellular energy. J Biol Chem 1994, 269:12447-12455.
    • (1994) J Biol Chem , vol.269 , pp. 12447-12455
    • Jacob Dubuisson, F.1    Striker, R.2    Hultgren, S.J.3
  • 34
    • 0032539855 scopus 로고    scopus 로고
    • The PapC usher forms an oligomeric channel: Implications for pilus biogenesis across the outer membrane
    • in press
    • Thanassi DG, Saulino ET, Lombarde M-J, Roth R, Heuser J, Hultgren SJ: The PapC usher forms an oligomeric channel: implications for pilus biogenesis across the outer membrane. Pro Natl Acad USA 1998, 95:in press. Shows that the PapC usher protein assembles into ring-shaped oligomeric complexes with central pores of 2-3 nm in diameter. Provides evidence that pili translocate through the usher in a linear form and only adopt their final structure upon reaching the cell surface.
    • (1998) Pro Natl Acad USA , vol.95
    • Thanassi, D.G.1    Saulino, E.T.2    Lombarde, M.-J.3    Roth, R.4    Heuser, J.5    Hultgren, S.J.6
  • 35
    • 0028121757 scopus 로고
    • Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli
    • Schifferli DM, Alrutz MA: Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli. J Bacteriol 1994, 176:1099-1110.
    • (1994) J Bacteriol , vol.176 , pp. 1099-1110
    • Schifferli, D.M.1    Alrutz, M.A.2
  • 36
    • 0029165969 scopus 로고
    • Subcellular localization and topology of the K88 usher FaeD in Escherichia coli
    • Valent QA, Zaal J, de Graaf FK, Oudega B: Subcellular localization and topology of the K88 usher FaeD in Escherichia coli. Mol Microbiol 1995, 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
  • 37
    • 0026704322 scopus 로고
    • Glycerol-induced unraveling of the tight helical conformation of Escherichia coli type 1 fimbriae
    • Abraham SN, Land M, Ponniah S, Endres R, Hasty DL, Babu JP: Glycerol-induced unraveling of the tight helical conformation of Escherichia coli type 1 fimbriae. J Bacteriol 1992, 174:5145-5148.
    • (1992) J Bacteriol , vol.174 , pp. 5145-5148
    • Abraham, S.N.1    Land, M.2    Ponniah, S.3    Endres, R.4    Hasty, D.L.5    Babu, J.P.6
  • 38
    • 0029840463 scopus 로고    scopus 로고
    • Type 1 fimbrial expression enhances Escherichia coli virulence for the urinary tract
    • Cornell H, Agace W, Klemm P, Schembri M, Marild S, Svanborg C: Type 1 fimbrial expression enhances Escherichia coli virulence for the urinary tract Proc Natl Acad Sci USA 1996, 93:9827-9832. Supports the role of type 1 pili, in addition to P pili, in the pathogenesis of E. coli in the urinary tract Demonstrates the need for the adhesin FimH for assembly of type 1 pili on the cell surface.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9827-9832
    • Cornell, H.1    Agace, W.2    Klemm, P.3    Schembri, M.4    Marild, S.5    Svanborg, C.6
  • 40
    • 0027385590 scopus 로고
    • Structure-function and biogenesis of type IV pili
    • Strom MS, Lory S: Structure-function and biogenesis of type IV pili. Annu Rev Microbiol 1993, 47:565-596.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 565-596
    • Strom, M.S.1    Lory, S.2
  • 42
    • 0029879021 scopus 로고    scopus 로고
    • A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilus
    • Stone KD, Zhang H-Z, Carlson LK, Donnenberg MS: A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for the biogenesis of a type IV pilus. Mol Microbiol 1996, 20:325-337. Identifies genes coding for type 4 pilus assembly in enteropalhogenic E. coli. The first reconstitution of type 4 pilus assembly in a laboratory strain of E. coli from a defined set of genes.
    • (1996) Mol Microbiol , vol.20 , pp. 325-337
    • Stone, K.D.1    Zhang, H.-Z.2    Carlson, L.K.3    Donnenberg, M.S.4
  • 43
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram negative bacteria
    • Pugsley A: The complete general secretory pathway in Gram negative bacteria. Microbiol Rev 1993, 57:50-108.
    • (1993) Microbiol Rev , vol.57 , pp. 50-108
    • Pugsley, A.1
  • 44
    • 0027489247 scopus 로고
    • Common components in the assembly of type 4 fimbriae, DNa transfer systems, filamentous phage and protein-secretion apparatus: A general system for the formation of surf a ce-associated protein complexes
    • Hobbs M, Mattick JS: Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surf a ce-associated protein complexes. Mol Microbiol 1993, 10:233-243.
    • (1993) Mol Microbiol , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 45
    • 0026505643 scopus 로고
    • Protein secretion in Pseudomonas aeruginosa: Characterization of seven xcp genes and processing of secretory apparatus by prepilin peptidase
    • Bally M, Filloux A, Akrim M, Ball G, Lazdunski A, Tommassen J: Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus by prepilin peptidase. Mol Microbiol 1992, 6:1121-1131.
    • (1992) Mol Microbiol , vol.6 , pp. 1121-1131
    • Bally, M.1    Filloux, A.2    Akrim, M.3    Ball, G.4    Lazdunski, A.5    Tommassen, J.6
  • 46
    • 0026502111 scopus 로고
    • Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase
    • Nunn DN, Lory S: Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase. Proc Natl Acad Sci USA 1992, 89:47-51.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 47-51
    • Nunn, D.N.1    Lory, S.2
  • 47
    • 0030478233 scopus 로고    scopus 로고
    • Pili, peptidases and protein secretion: Curious connections
    • Salmond GP: Pili, peptidases and protein secretion: curious connections. Trends Microbiol 1996, 4:474-476.
    • (1996) Trends Microbiol , vol.4 , pp. 474-476
    • Salmond, G.P.1
  • 48
    • 0029899207 scopus 로고    scopus 로고
    • Multimers of the precursor of a type IV pilin-like component of the general secretory pathway are unrelated to pili
    • Pugsley AP: Multimers of the precursor of a type IV pilin-like component of the general secretory pathway are unrelated to pili. Mol Microbiol 1996, 20:1235-1245.
    • (1996) Mol Microbiol , vol.20 , pp. 1235-1245
    • Pugsley, A.P.1
  • 49
    • 0027358573 scopus 로고
    • The general secretory pathway of Klebsiella oxytoca: No evidence for relocalization or assembly of pilin-like PulG protein into a multiprotein complex
    • Pugsley AP, Possot O: The general secretory pathway of Klebsiella oxytoca: no evidence for relocalization or assembly of pilin-like PulG protein into a multiprotein complex. Mol Microbiol 1993, 10:665-674.
    • (1993) Mol Microbiol , vol.10 , pp. 665-674
    • Pugsley, A.P.1    Possot, O.2
  • 50
    • 0030992350 scopus 로고    scopus 로고
    • Translocation failure in a type-4 pilin operon: rfb and tcpT mutants in Vibrio cholerae
    • Iredell JR, Manning PA: Translocation failure in a type-4 pilin operon: rfb and tcpT mutants in Vibrio cholerae. Gene 1997, 192:71-77.
    • (1997) Gene , vol.192 , pp. 71-77
    • Iredell, J.R.1    Manning, P.A.2
  • 51
    • 0025968869 scopus 로고
    • Mutagenesis and isolation of Aeromonas hydrophila genes which are required for extracellular secretion
    • Jiang B, Howard SP: Mutagenesis and isolation of Aeromonas hydrophila genes which are required for extracellular secretion. J Bacteriol 1991, 173:1241-1249.
    • (1991) J Bacteriol , vol.173 , pp. 1241-1249
    • Jiang, B.1    Howard, S.P.2
  • 52
    • 0029063497 scopus 로고
    • Identification of a gene, pilV, required for type 4 fimbrial biogenesis in Pseudomonas aeruginosa, whose product possesses a pre-pilin-like leader sequence
    • Aim RA, Mattick JS: Identification of a gene, pilV, required for type 4 fimbrial biogenesis in Pseudomonas aeruginosa, whose product possesses a pre-pilin-like leader sequence. Mol Microbiol 1995, 16:485-496.
    • (1995) Mol Microbiol , vol.16 , pp. 485-496
    • Aim, R.A.1    Mattick, J.S.2
  • 53
    • 0028875938 scopus 로고
    • Prepilin-like molecules in type 4 pilus biogenesis: Minor subunits, chaperones or mediators of organelle translocation?
    • Koomey M: Prepilin-like molecules in type 4 pilus biogenesis: minor subunits, chaperones or mediators of organelle translocation? Trends Microbiol 1995, 3:406-411.
    • (1995) Trends Microbiol , vol.3 , pp. 406-411
    • Koomey, M.1
  • 54
    • 0030930294 scopus 로고    scopus 로고
    • The type III (Hrp) secretion pathway of plant pathogenic bacteria: Trafficking harpins, Avr proteins, and death
    • Alfano JR, Collmer A: The type III (Hrp) secretion pathway of plant pathogenic bacteria: trafficking harpins, Avr proteins, and death. J Bacteriol 1997, 179:5655-5662. Reviews the recent discoveries of contact-dependent (type III) secretion systems in plant pathogenic bacteria. These Hrp secretion systems directly inject Avr proteins into the interior of plant cells, triggering cell death, and are related to the Yersinia Yop and other contact-dependent secretion systems of animal pathogenic bacteria.
    • (1997) J Bacteriol , vol.179 , pp. 5655-5662
    • Alfano, J.R.1    Collmer, A.2
  • 55
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis GR, Wolf-Watz H; The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol Microbiol 1997, 23:861-867. Details the current understanding of the Yop contact-dependent secretion system of Yersinia. The Yop secretion system is the archetype for the contact-dependent (type III) secretion system family.
    • (1997) Mol Microbiol , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 56
    • 0029879556 scopus 로고    scopus 로고
    • Molecular genetic basis of Salmonella entry into host cells
    • Galán JE: Molecular genetic basis of Salmonella entry into host cells. Mol Microbiol 1996, 20:263-271. Reviews the contact-dependent (type III) secretion system of Salmonella, its role in pathogenesis, and its remarkable homology to the contact-dependent secretion system of Shigella.
    • (1996) Mol Microbiol , vol.20 , pp. 263-271
    • Galán, J.E.1
  • 57
    • 0029886432 scopus 로고    scopus 로고
    • Customized secretion chaperones in pathogenic bacteria
    • Wattiau P, Woestyn S, Cornelis GR: Customized secretion chaperones in pathogenic bacteria. Mol Microbiol 1996, 20:255-262.
    • (1996) Mol Microbiol , vol.20 , pp. 255-262
    • Wattiau, P.1    Woestyn, S.2    Cornelis, G.R.3
  • 58
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie KR, Lory S, Pugsley AP: Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J 1996, 15:978-988. Demonstrates that the Klebsielle oxytoca PulD protein forms stable oligomers in the OM, as found for the plV filamentous phage protein. Presents evidence that the PulS protein functions as a chaperone for the insertion of PulD in the OM, and suggests that PulS homotogs may function similarly in other MTB (type II) secretion systems.
    • (1996) EMBO J , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 59
    • 0028353854 scopus 로고
    • A super-family of proteins involved in different secretion pathways in Gram-negative bacteria: Modular structure and specificity of the N-terminal domain
    • Genin S, Boucher CA: A super-family of proteins involved in different secretion pathways in Gram-negative bacteria: modular structure and specificity of the N-terminal domain. Mol Gen Genet 1994, 243:112-118.
    • (1994) Mol Gen Genet , vol.243 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 60
    • 0028999019 scopus 로고
    • Moving through the membrane with filamentous phages
    • Russel M: Moving through the membrane with filamentous phages. Trends Microbiol 1995, 3:223-228.
    • (1995) Trends Microbiol , vol.3 , pp. 223-228
    • Russel, M.1
  • 61
    • 0030716279 scopus 로고    scopus 로고
    • The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex
    • Koster M, Bitter W, de Cock H, Allaoui A, Cornelis GR, Tommassen J: The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol Microbiol 1997, 26:789-797. Demonstrates that the YscC protein of the Yop secretion system of Y. enterocolitica forms a stable oligomeric complex in the OM, and that the VirG protein appears to facilitate YscC insertion in the OM. Purified YscC complex is shown to assemble into a ring shaped complex with an apparent central pore.
    • (1997) Mol Microbiol , vol.26 , pp. 789-797
    • Koster, M.1    Bitter, W.2    De Cock, H.3    Allaoui, A.4    Cornelis, G.R.5    Tommassen, J.6
  • 62
    • 1842293999 scopus 로고    scopus 로고
    • The filamentous phage plV multimer visualized by scanning transmission electron microscopy
    • Linderoth NA, Simon MN, Russel M: The filamentous phage plV multimer visualized by scanning transmission electron microscopy. Science 1997, 278:1635-1638. Demonstrates that the plV outer membrane protein assembles into cylindrical complexes containing large central pores. The pores are large enough to accommodate an assembled filamentous phage.
    • (1997) Science , vol.278 , pp. 1635-1638
    • Linderoth, N.A.1    Simon, M.N.2    Russel, M.3
  • 63
    • 0031983616 scopus 로고    scopus 로고
    • Formation of oligomeric rings by XcpQ and PilQ which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa
    • ••]. This suggests that the usher and PulD/plV protein families may be structurally and functionally similar.
    • (1998) Mol Microbiol , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latijnhouwers, M.3    De Cook, H.4    Tommassen, J.5
  • 64
    • 0031005016 scopus 로고    scopus 로고
    • Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway
    • Possot OM, Letellier L, Pugsley AP: Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway. Mol Microbiol 1997, 24:457-464.
    • (1997) Mol Microbiol , vol.24 , pp. 457-464
    • Possot, O.M.1    Letellier, L.2    Pugsley, A.P.3
  • 65
    • 0029855069 scopus 로고    scopus 로고
    • Duplication of pilus gene complexes of Haemophilus influenzae biogroup aegyptius
    • Read TD, Dowdell M, Satola SW, Farley MM: Duplication of pilus gene complexes of Haemophilus influenzae biogroup aegyptius. J Bacteriol 1996, 176:6564-6570.
    • (1996) J Bacteriol , vol.176 , pp. 6564-6570
    • Read, T.D.1    Dowdell, M.2    Satola, S.W.3    Farley, M.M.4
  • 66
    • 0028913176 scopus 로고
    • Identification and sequence analysis of IpfABCDE, a putative fimbrial operon of Salmonella typhimurium
    • Büumler AJ, Heffron F: Identification and sequence analysis of IpfABCDE, a putative fimbrial operon of Salmonella typhimurium. J Bacteriol 1995, 177:2087-2097.
    • (1995) J Bacteriol , vol.177 , pp. 2087-2097
    • Büumler, A.J.1    Heffron, F.2
  • 67
    • 0029819462 scopus 로고    scopus 로고
    • Proteus mirabilis ambient-temperature fimbriae: Cloning and nucleotide sequence of the aft gene cluster
    • J. F.
    • Massad G, Fulkerson J, J. F. , Watson DC, Mobley HLT: Proteus mirabilis ambient-temperature fimbriae: cloning and nucleotide sequence of the aft gene cluster. Infect Immun 1996, 64:4390-4395.
    • (1996) Infect Immun , vol.64 , pp. 4390-4395
    • Massad, G.1    Fulkerson, J.2    Watson, D.C.3    Mobley, H.L.T.4
  • 68
    • 0029888256 scopus 로고    scopus 로고
    • Identification of major and minor chaperone proteins involved in the export of 987P fimbriae
    • Edwards RA, Cao J, Schifferli DM: Identification of major and minor chaperone proteins involved in the export of 987P fimbriae. J Bacteriol 1996, 178:3426-3433.
    • (1996) J Bacteriol , vol.178 , pp. 3426-3433
    • Edwards, R.A.1    Cao, J.2    Schifferli, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.