Pilus chaperones represent a new type of protein-folding catalyst (original) (raw)

References

1. Sauer, F. G. et al. Chaperone-assisted pilus assembly and bacterial attachment. Curr. Opin. Struct. Biol. 10, 548–556 (2000)
   Article CAS PubMed Google Scholar
2. Lindberg, F., Tennent, J. M., Hultgren, S. J., Lund, B. & Normark, S. PapD, a periplasmic transport protein in P-pilus biogenesis. J. Bacteriol. 171, 6052–6058 (1989)
   Article CAS PubMed PubMed Central Google Scholar
3. Kuehn, M. J., Normark, S. & Hultgren, S. J. Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits. Proc. Natl Acad. Sci. USA 88, 10586–10590 (1991)
   Article ADS CAS PubMed PubMed Central Google Scholar
4. Jones, C. H. et al. FimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteria. Proc. Natl Acad. Sci. USA 90, 8397–8401 (1993)
   Article ADS CAS PubMed PubMed Central Google Scholar
5. Klemm, P. & Christiansen, G. The fimD gene required for cell surface localization of Escherichia coli type 1 fimbriae. Mol. Gen. Genet. 220, 334–338 (1990)
   Article CAS PubMed Google Scholar
6. Dodson, K. W., Jacob-Dubuisson, F., Striker, R. T. & Hultgren, S. J. Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes. Proc. Natl Acad. Sci. USA 90, 3670–3674 (1993)
   Article ADS CAS PubMed PubMed Central Google Scholar
7. Thanassi, D. G. et al. The PapC usher forms an oligomeric channel: implications for pilus biogenesis across the outer membrane. Proc. Natl Acad. Sci. USA 95, 3146–3151 (1998)
   Article ADS CAS PubMed PubMed Central Google Scholar
8. Saulino, E. T., Bullitt, E. & Hultgren, S. J. Snapshots of usher-mediated protein secretion and ordered pilus assembly. Proc. Natl Acad. Sci. USA 97, 9240–9245 (2000)
   Article ADS CAS PubMed PubMed Central Google Scholar
9. Hahn, E. et al. Exploring the 3D molecular architecture of Escherichia coli type 1 pili. J. Mol. Biol. 323, 845–857 (2002)
   Article CAS PubMed Google Scholar
10. Choudhury, D. et al. X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science 285, 1061–1066 (1999)
    Article CAS PubMed Google Scholar
11. Sauer, F. G. et al. Structural basis of chaperone function and pilus biogenesis. Science 285, 1058–1061 (1999)
    Article CAS PubMed Google Scholar
12. Sauer, F. G., Pinkner, J. S., Waksman, G. & Hultgren, S. J. Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell 111, 543–551 (2002)
    Article CAS PubMed Google Scholar
13. Zavialov, A. V. et al. Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation. Cell 113, 587–596 (2003)
    Article CAS PubMed Google Scholar
14. Zavialov, A. V. et al. Donor strand complementation mechanism in the biogenesis of non-pilus systems. Mol. Microbiol. 45, 983–995 (2002)
    Article CAS PubMed Google Scholar
15. Jacob-Dubuisson, F., Striker, R. T. & Hultgren, S. J. Chaperone-assisted self-assembly of pili independent of cellular energy. J. Biol. Chem. 269, 12447–12455 (1994)
    CAS PubMed Google Scholar
16. Schmid, F. X. Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. Biochemistry 22, 4690–4696 (1983)
    Article CAS PubMed Google Scholar
17. Balbach, J. & Schmid, F. X. in Protein Folding: Frontiers in Molecular Biology (ed. Pain, R.) (Oxford Univ. Press, Oxford, 2000)
    Google Scholar
18. Pugsley, A. P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57, 50–108 (1993)
    CAS PubMed PubMed Central Google Scholar
19. Vetsch, M., Sebbel, P. & Glockshuber, R. Chaperone-independent folding of type 1 pilus domains. J. Mol. Biol. 322, 827–840 (2002)
    Article CAS PubMed Google Scholar
20. Hartl, F. U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852–1858 (2002)
    Article ADS CAS PubMed Google Scholar
21. Brinker, A. et al. Dual function of protein confinement in chaperonin-assisted protein folding. Cell 107, 223–233 (2001)
    Article CAS PubMed Google Scholar
22. Jones, C. H., Danese, P. N., Pinkner, J. S., Silhavy, T. J. & Hultgren, S. J. The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems. EMBO J. 16, 6394–6406 (1997)
    Article CAS PubMed PubMed Central Google Scholar
23. Eder, J. & Fersht, A. R. Pro-sequence-assisted protein folding. Mol. Microbiol. 16, 609–614 (1995)
    Article CAS PubMed Google Scholar
24. Baker, D., Sohl, J. L. & Agard, D. A. A protein-folding reaction under kinetic control. Nature 356, 263–265 (1992)
    Article ADS CAS PubMed Google Scholar
25. Frand, A. R., Cuozzo, J. W. & Kaiser, C. A. Pathways for protein disulphide bond formation. Trends Cell Biol. 10, 203–210 (2000)
    Article CAS PubMed Google Scholar
26. Schiene-Fischer, C., Habazettl, J., Schmid, F. X. & Fischer, G. The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase. Nature Struct. Biol. 9, 419–424 (2002)
    Article CAS PubMed Google Scholar
27. Hermanns, U., Sebbel, P., Eggli, V. & Glockshuber, R. Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli. Biochemistry 39, 11564–11570 (2000)
    Article CAS PubMed Google Scholar
28. Nishiyama, M., Vetsch, M., Puorger, C., Jelesarov, I. & Glockshuber, R. Identification and characterization of the chaperone-subunit complex-binding domain from the type 1 pilus assembly platform FimD. J. Mol. Biol. 330, 513–525 (2003)
    Article CAS PubMed Google Scholar

Download references