NDLI: Snapshots of usher-mediated protein secretion and ordered pilus assembly.

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Snapshots of usher-mediated protein secretion and ordered pilus assembly.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Saulino, E. T. Hultgren, S. J. Bullitt, E.
Description	Author Affiliation: Saulino ET ( Department of Molecular Microbiology and Microbial Pathogenesis, Washington University School of Medicine, St. Louis, MO 63110-1010, USA.);
Abstract	Type 1 pilus biogenesis was used as a paradigm to investigate ordered macromolecular assembly at the outer cell membrane. The ability of Gram-negative bacteria to secrete proteins across their outer membrane and to assemble adhesive macromolecular structures on their surface is a defining event in pathogenesis. We elucidated genetic, biochemical, and biophysical requirements for assembly of functional type 1 pili. We discovered that the minor pilus protein FimG plays a critical role in nucleating the formation of the adhesive tip fibrillum. Genetic methods were used to trap pilus subunits during their translocation through the outer membrane usher protein, providing data on the structural interactions that occur between subunit components during type 1 pilus formation. Electron microscopic and biochemical analyses of these stepwise assembly intermediates demonstrated that translocation of pilus subunits occurs linearly through the usher's central channel, with formation of the pilus helix occurring extracellularly. Specialized pilin subunits play unique roles both in this multimerization and in the final ultrastructure of the adhesive pilus.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	16
Volume Number	97
Language	English
Publisher	National Academy of Sciences
Publisher Date	2000-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Secretion Fimbriae, Bacterial Animals Guinea Pigs Microscopy, Electron Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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