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Journal of Bacteriology, July 2007, p. 5276-5283, Vol. 189, No. 14
0021-9193/07/$08.00+0     doi:10.1128/JB.01648-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Adaptor Function of PapF Depends on Donor Strand Exchange in P-Pilus Biogenesis of Escherichia coli{triangledown}

Yvonne M. Lee,{dagger} Karen W. Dodson, and Scott J. Hultgren*

Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Ave., Campus Box 8230, St. Louis, Missouri 63110

Received 24 October 2006/ Accepted 2 May 2007

P-pilus biogenesis occurs via the highly conserved chaperone-usher pathway and involves the strict coordination of multiple subunit proteins. All nonadhesin structural P-pilus subunits possess the same topology, consisting of two domains: an incomplete immunoglobulin-like fold (pilin body) and an N-terminal extension. Pilus subunits form interactions with one another through donor strand exchange, occurring at the usher, in which the N-terminal extension of an incoming subunit completes the pilin body of the preceding subunit, allowing the incorporation of the subunit into the pilus fiber. In this study, pilus subunits in which the N-terminal extension was either deleted or swapped with that of another subunit were used to examine the role of each domain of PapF in functions involving donor strand exchange and hierarchical assembly. We found that the N-terminal extension of PapF is required to adapt the PapG adhesin to the tip of the fiber. The pilin body of PapF is required to efficiently initiate assembly of the remainder of the pilus, with the assistance of the N-terminal extension. Thus, distinct functions were assigned to each region of the PapF subunit. In conclusion, all pilin subunits possess the same overall architectural topology; however, each N-terminal extension and pilin body has specific functions in pilus biogenesis.

* Corresponding author. Mailing address: Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Ave., Campus Box 8230, St. Louis, MO 63110. Phone: (314) 362-6772. Fax: (314) 362-1998. E-mail: hultgren{at}borcim.wustl.edu

{triangledown} Published ahead of print on 11 May 2007.

{dagger} Present address: Department of Pharmacology, University of California, San Diego, 9500 Gilman Drive, Mail Code 0721, San Diego, CA 92093-0721.

Journal of Bacteriology, July 2007, p. 5276-5283, Vol. 189, No. 14
0021-9193/07/$08.00+0     doi:10.1128/JB.01648-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rose, R. J., Verger, D., Daviter, T., Remaut, H., Paci, E., Waksman, G., Ashcroft, A. E., Radford, S. E. (2008). Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry. Proc. Natl. Acad. Sci. USA 105: 12873-12878 [Abstract] [Full Text]  


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