메뉴 건너뛰기




Volumn 185, Issue 8, 2003, Pages 2611-2617

Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy

Author keywords

[No Author keywords available]

Indexed keywords

OUTER MEMBRANE PROTEIN; PROTEIN PILQ; SECRETIN; UNCLASSIFIED DRUG;

EID: 0037389450     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.8.2611-2617.2003     Document Type: Article
Times cited : (72)

References (53)
  • 1
    • 0030907570 scopus 로고    scopus 로고
    • Identification of a gene PilV required for type 4 fimbrial biogenesis in P. aeruginosa whose product possesses a prepilin-like leader sequence
    • Alm, R. A., and J. S. Mattick. 1997. Identification of a gene PilV required for type 4 fimbrial biogenesis in P. aeruginosa whose product possesses a prepilin-like leader sequence. Gene 192:89-98.
    • (1997) Gene , vol.192 , pp. 89-98
    • Alm, R.A.1    Mattick, J.S.2
  • 2
    • 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
    • Bitter, W., M. Koster, M. Latjinhouwers, H. de Cock, and J. Tommassen. 1998. Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa. Mol. Microbiol. 27:209-219.
    • (1998) Mol. Microbiol. , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latjinhouwers, M.3    De Cock, H.4    Tommassen, J.5
  • 4
    • 0034973703 scopus 로고    scopus 로고
    • Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure
    • Collins, R. F., L. Davidsen, J. P. Derrick, R. C. Ford, and T. Tønjum. 2001. Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure. J. Bacteriol. 183:3825-3832.
    • (2001) J. Bacteriol. , vol.183 , pp. 3825-3832
    • Collins, R.F.1    Davidsen, L.2    Derrick, J.P.3    Ford, R.C.4    Tønjum, T.5
  • 5
    • 0031026828 scopus 로고    scopus 로고
    • The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex
    • Cornelis, G. R., and H. Wolf-Watz. 1997. The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol. Microbiol. 23:861-867.
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, G.R.1    Wolf-Watz, H.2
  • 6
    • 0031665154 scopus 로고    scopus 로고
    • Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization
    • Crago, A. M., and V. Koronakis. 1998. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol. Microbiol. 30:47-56.
    • (1998) Mol. Microbiol. , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 7
    • 0031025472 scopus 로고    scopus 로고
    • PilP: A pilus biogenesis lipoprotein in Neisseria gonorrhoeae affects expression of PilQ as a high molecular mass multimer
    • Drake, S., S. A. Sandstedt, and M. Koomey. 1997. PilP: a pilus biogenesis lipoprotein in Neisseria gonorrhoeae affects expression of PilQ as a high molecular mass multimer. Mol. Microbiol. 23:657-668.
    • (1997) Mol. Microbiol. , vol.23 , pp. 657-668
    • Drake, S.1    Sandstedt, S.A.2    Koomey, M.3
  • 8
    • 0029560821 scopus 로고
    • The product of the PilQ gene is essential for the biogenesis of type IV pilus in N. gonorrhoeae
    • Drake, S. L., and M. Koomey. 1995. The product of the PilQ gene is essential for the biogenesis of type IV pilus in N. gonorrhoeae. Mol. Microbiol. 18: 975-986.
    • (1995) Mol. Microbiol. , vol.18 , pp. 975-986
    • Drake, S.L.1    Koomey, M.2
  • 9
    • 0034602835 scopus 로고    scopus 로고
    • Translocation of group 1 capsular polysaccharide to the surface of Escherichia coli requires a multimeric complex in the outer membrane
    • Drummelsmith, J., and C. Whitfield. 2000. Translocation of group 1 capsular polysaccharide to the surface of Escherichia coli requires a multimeric complex in the outer membrane. EMBO J. 19:57-66.
    • (2000) EMBO J. , vol.19 , pp. 57-66
    • Drummelsmith, J.1    Whitfield, C.2
  • 11
    • 0036089703 scopus 로고    scopus 로고
    • Single-particle imaging of macromolecules by cryo-electron microscopy
    • Frank, J. 2002. Single-particle imaging of macromolecules by cryo-electron microscopy. Annu. Rev. Biophys. Biomol. Struct. 31:303-319.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 303-319
    • Frank, J.1
  • 13
    • 0026045381 scopus 로고
    • 3-D reconstruction of the 70S ribosome in ice: The distribution of ribosomal RNA
    • Frank, J., P. Penczek, R. Grassucci, and S. Srivastav. 1991. 3-D reconstruction of the 70S ribosome in ice: the distribution of ribosomal RNA. J. Cell Biol. 115:597-605.
    • (1991) J. Cell Biol. , vol.115 , pp. 597-605
    • Frank, J.1    Penczek, P.2    Grassucci, R.3    Srivastav, S.4
  • 14
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3-D electron microscopy and related fields
    • Frank, J., M. Radermacher, P. Penczek, J. Zhu, M. Ladjadj, and A. Leith. 1996. SPIDER and WEB: processing and visualization of images in 3-D electron microscopy and related fields. J. Struct. Biol. 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Ladjadj, M.5    Leith, A.6
  • 15
    • 0015868318 scopus 로고
    • Electron microscopical and cultural features of Neisseria meningitidis competence variants
    • Frøholm, L. O., K. Jyssum, and M. Bøvre. 1973. Electron microscopical and cultural features of Neisseria meningitidis competence variants. Acta Pathol. Microbiol. Scand. 81:525-537.
    • (1973) Acta Pathol. Microbiol. Scand. , vol.81 , pp. 525-537
    • Frøholm, L.O.1    Jyssum, K.2    Bøvre, M.3
  • 16
    • 0025179801 scopus 로고
    • Generation of capsule-deficient Neisseria meningitidis strains by homologous recombination
    • Frosch, M., E. Schultz, E. Glenncalvo, and T. F. Meyer. 1990. Generation of capsule-deficient Neisseria meningitidis strains by homologous recombination. Mol. Microbiol. 4:1215-1218.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1215-1218
    • Frosch, M.1    Schultz, E.2    Glenncalvo, E.3    Meyer, T.F.4
  • 17
    • 0026330896 scopus 로고
    • An inducible bundle-forming pilus of enteropathogenic E. coli
    • Giron, J. A., A. S. Y. Ho, and G. K. Schoolnik. 1991. An inducible bundle-forming pilus of enteropathogenic E. coli. Science 254:710-713.
    • (1991) Science , vol.254 , pp. 710-713
    • Giron, J.A.1    Ho, A.S.Y.2    Schoolnik, G.K.3
  • 18
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: Are there distinct domains for multimerization and secretion specificity?
    • Guilvout, I., K. R. Hardie, N. Sauvonnet, and A. P. Pugsley. 1999. Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity? J. Bacteriol. 181:7212-7220.
    • (1999) J. Bacteriol. , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 19
    • 0028028685 scopus 로고
    • Negative staining: A brief assessment of current technical benefits, limitations and future possibilities
    • Harris, J. R., and R. Horne. 1994. Negative staining: a brief assessment of current technical benefits, limitations and future possibilities. Micron 25:5-13.
    • (1994) Micron , vol.25 , pp. 5-13
    • Harris, J.R.1    Horne, R.2
  • 20
    • 2042481016 scopus 로고
    • Structure and function of pili of pathogenic Neisseria species
    • Heckels, J. E. 1989. Structure and function of pili of pathogenic Neisseria species. Clin. Microbiol. Rev. 2:S66-S73.
    • (1989) Clin. Microbiol. Rev. , vol.2
    • Heckels, J.E.1
  • 21
    • 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 assembly of surface associated protein complexes
    • Hobbs, M., and J. S. Mattick. 1993. Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein secretion apparatus: a general system for the assembly of surface associated protein complexes. Mol. Microbiol. 10:233-243.
    • (1993) Mol. Microbiol. , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 22
    • 0027983703 scopus 로고
    • Sequence changes in the pilus subunit lead to tropism variation of Neisseria gonorrhoeae to human tissue
    • Jönsson, A. B., D. Ilver, P. Falk, and S. Normark. 1994. Sequence changes in the pilus subunit lead to tropism variation of Neisseria gonorrhoeae to human tissue. Mol. Microbiol. 13:403-416.
    • (1994) Mol. Microbiol. , vol.13 , pp. 403-416
    • Jönsson, A.B.1    Ilver, D.2    Falk, P.3    Normark, S.4
  • 23
    • 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., W. Bitter, H. De Cock, A. Allaoui, G. R. Cornelis, and J. Tommassen. 1997. The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol. Microbiol. 26:789-797.
    • (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
  • 26
    • 1842293999 scopus 로고    scopus 로고
    • The filamentous phage pIV multimer visualized by scanning transmission electron microscopy
    • Linderoth, N. A., M. N. Simon, and M. Russel. 1997. The filamentous phage pIV multimer visualized by scanning transmission electron microscopy. Science 278:1635-1638.
    • (1997) Science , vol.278 , pp. 1635-1638
    • Linderoth, N.A.1    Simon, M.N.2    Russel, M.3
  • 27
    • 0033612142 scopus 로고    scopus 로고
    • An aqueous channel for filamentous phage export
    • Marciano, D. K., M. Russel, and S. M. Simon. 1999. An aqueous channel for filamentous phage export. Science 284:1516-1519.
    • (1999) Science , vol.284 , pp. 1516-1519
    • Marciano, D.K.1    Russel, M.2    Simon, S.M.3
  • 28
    • 0034769801 scopus 로고    scopus 로고
    • Bacterial gliding motility: Multiple mechanisms for cell movement over surfaces
    • McBride, M. J. 2001. Bacterial gliding motility: multiple mechanisms for cell movement over surfaces. Annu. Rev. Microbiol. 55:49-75.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 49-75
    • McBride, M.J.1
  • 29
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. 1999. XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 30
    • 0034618643 scopus 로고    scopus 로고
    • Pilus retraction powers bacterial twitching motility
    • Merz, A. J., M. So, and M. P. Sheetz. 2000. Pilus retraction powers bacterial twitching motility. Nature 407:98-102.
    • (2000) Nature , vol.407 , pp. 98-102
    • Merz, A.J.1    So, M.2    Sheetz, M.P.3
  • 32
    • 0034657105 scopus 로고    scopus 로고
    • Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy
    • Nouwen, N., H. Stahleberg, A. P. Pugsley, and A. Engel. 2000. Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy. EMBO J. 19:2229-2236.
    • (2000) EMBO J. , vol.19 , pp. 2229-2236
    • Nouwen, N.1    Stahleberg, H.2    Pugsley, A.P.3    Engel, A.4
  • 33
    • 0033214349 scopus 로고    scopus 로고
    • Bacterial type II protein export and pilus biogenesis: More than just homologies?
    • Nunn, D. 1999. Bacterial type II protein export and pilus biogenesis: more than just homologies? Trends Cell Biol. 9:402-408.
    • (1999) Trends Cell Biol. , vol.9 , pp. 402-408
    • Nunn, D.1
  • 35
    • 0031583477 scopus 로고    scopus 로고
    • Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution
    • Orlova, E. V., P. Dube, J. R. Harris, E. Beckman, F. Zemlin, J. Markl, and M. van Heel. 1997. Structure of keyhole limpet hemocyanin type 1 (KLH1) at 15 Å resolution by electron cryomicroscopy and angular reconstitution. J. Mol. Biol. 271:417-437.
    • (1997) J. Mol. Biol. , vol.271 , pp. 417-437
    • Orlova, E.V.1    Dube, P.2    Harris, J.R.3    Beckman, E.4    Zemlin, F.5    Markl, J.6    Van Heel, M.7
  • 37
    • 0026521233 scopus 로고
    • 3-D reconstruction of single particles embedded in ice
    • Penczek, P., M. Radermacher, and J. Frank. 1992. 3-D reconstruction of single particles embedded in ice. Ultramicroscopy 40:33-53.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 38
    • 0024082194 scopus 로고
    • Nucleotide-sequence of the structural gene for class-1 pilin from Neisseria meningitidis: Homologies with the pilE locus of Neisseria gonorrhoeae
    • Potts, W. J., and J. R. Saunders. 1988. Nucleotide-sequence of the structural gene for class-1 pilin from Neisseria meningitidis: homologies with the pilE locus of Neisseria gonorrhoeae. Mol. Microbiol. 2:647-653.
    • (1988) Mol. Microbiol. , vol.2 , pp. 647-653
    • Potts, W.J.1    Saunders, J.R.2
  • 39
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A. P. 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.P.1
  • 40
    • 0034986184 scopus 로고    scopus 로고
    • Determining the structure of biological macromolecules by transmission electron microscopy, single particle analysis and 3D reconstruction
    • Ruprecht, J., and J. Nield. 2001. Determining the structure of biological macromolecules by transmission electron microscopy, single particle analysis and 3D reconstruction. Prog. Biophys. Mol. Biol. 75:121-164.
    • (2001) Prog. Biophys. Mol. Biol. , vol.75 , pp. 121-164
    • Ruprecht, J.1    Nield, J.2
  • 41
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali, A., and T. A. Blundell. 1993. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.A.2
  • 42
    • 0034255260 scopus 로고    scopus 로고
    • Snapshots of usher-mediated protein secretion and ordered pilus assembly
    • Saulino, E. T., E. Bullitt, and S. J. Hultgren. 2000. Snapshots of usher-mediated 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
  • 43
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • Saxton, W. O., and W. Baumeister. 1982. The correlation averaging of a regularly arranged bacterial cell envelope protein. J. Microsc. 127(Pt. 2): 127-138.
    • (1982) J. Microsc. , vol.127 , Issue.PART 2 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 44
    • 0034906825 scopus 로고    scopus 로고
    • Structure-function analysis of BfpB, a secretin-like protein encoded by the bundle-forming-pilus operon of enteropathogenic Escherichia coli
    • Schmidt, S. A., D. Bieber, S. W. Ramer, J. Hwang, C. Y. Wu, and G. Schoolnik. 2001. Structure-function analysis of BfpB, a secretin-like protein encoded by the bundle-forming-pilus operon of enteropathogenic Escherichia coli. J. Bacteriol. 183:4848-4859.
    • (2001) J. Bacteriol. , vol.183 , pp. 4848-4859
    • Schmidt, S.A.1    Bieber, D.2    Ramer, S.W.3    Hwang, J.4    Wu, C.Y.5    Schoolnik, G.6
  • 45
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi OMP of the general secretory pathway and secreted proteins
    • Shevchick, V. E., J. Robert-Baudouy, and G. Condemine. 1997. Specific interaction between OutD, an Erwinia chrysanthemi OMP of the general secretory pathway and secreted proteins. EMBO J. 16:3007-3016.
    • (1997) EMBO J. , vol.16 , pp. 3007-3016
    • Shevchick, V.E.1    Robert-Baudouy, J.2    Condemine, G.3
  • 46
    • 0029879021 scopus 로고    scopus 로고
    • A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for biogenesis of a type IV pilus
    • Stone, K. D., H. Z. Zhang, L. K. Carlson, and M. S. Donnenberg. 1996. A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for biogenesis of a type IV pilus. Mol. Microbiol. 20:325-337.
    • (1996) Mol. Microbiol. , vol.20 , pp. 325-337
    • Stone, K.D.1    Zhang, H.Z.2    Carlson, L.K.3    Donnenberg, M.S.4
  • 47
    • 0027385590 scopus 로고
    • Structure, function, and biogenesis of the type IV pili
    • Strom, M. S., and S. Lory. 1993. Structure, function, and biogenesis of the type IV pili. Annu. Rev. Microbiol. 47:565-596.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 565-596
    • Strom, M.S.1    Lory, S.2
  • 48
    • 0015140023 scopus 로고
    • Studies on gonococcus infection. IV. Pili: Their role in attachment of gonococci to tissue culture cells
    • Swanson, J., S. J. Kraus, and E. C. Gotschlich. 1971. Studies on gonococcus infection. IV. Pili: their role in attachment of gonococci to tissue culture cells. J. Exp. Med. 134:886-906.
    • (1971) J. Exp. Med. , vol.134 , pp. 886-906
    • Swanson, J.1    Kraus, S.J.2    Gotschlich, E.C.3
  • 50
    • 0031871011 scopus 로고    scopus 로고
    • Structure and function of repetitive sequence elements associated with a polymorphic domain of the N. meningitidis PilQ complex
    • Tønjum, T., D. A. Caugant, S. A. Dunham, and M. Koomey. 1998. Structure and function of repetitive sequence elements associated with a polymorphic domain of the N. meningitidis PilQ complex. Mol. Microbiol. 29:975-986.
    • (1998) Mol. Microbiol. , vol.29 , pp. 975-986
    • Tønjum, T.1    Caugant, D.A.2    Dunham, S.A.3    Koomey, M.4
  • 51
    • 0029030966 scopus 로고
    • Identification and characterization of PilG, a highly conserved pilus assembly gene in pathogenic Neisseria
    • Tønjum, T., N. E. Freitag, E. Namork, and M. Koomey. 1995. Identification and characterization of PilG, a highly conserved pilus assembly gene in pathogenic Neisseria. Mol. Microbiol. 16:451-464.
    • (1995) Mol. Microbiol. , vol.16 , pp. 451-464
    • Tønjum, T.1    Freitag, N.E.2    Namork, E.3    Koomey, M.4
  • 52
    • 0030913947 scopus 로고    scopus 로고
    • The pilus colonization factor of pathogenic neisserial species: Organelle biogenesis and structure/function relationships
    • Tønjum, T., and M. Koomey. 1997. The pilus colonization factor of pathogenic neisserial species: organelle biogenesis and structure/function relationships. Gene 192:155-163.
    • (1997) Gene , vol.192 , pp. 155-163
    • Tønjum, T.1    Koomey, M.2
  • 53
    • 0026647913 scopus 로고
    • Gene conversion in Neisseria gonorrhoeae: Evidence for its role in pilus antigenic variation
    • Zhang, Q. Y., D. Deryckere, P. Lauer, and M. Koomey. 1992. Gene conversion in Neisseria gonorrhoeae: evidence for its role in pilus antigenic variation. Proc. Natl. Acad. Sci. USA 89:5366-5370.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5366-5370
    • Zhang, Q.Y.1    Deryckere, D.2    Lauer, P.3    Koomey, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.