Fiber assembly by the chaperone-usher pathway.

TitleFiber assembly by the chaperone-usher pathway.
Publication TypeJournal Article
Year of Publication2004
AuthorsSauer, F. G., H. Remaut, S. J. Hultgren, and G. Waksman
JournalBiochim Biophys Acta
Volume1694
Issue1-3
Pagination259-67
Date Published2004 Nov 11
ISSN0006-3002
KeywordsBacterial Proteins, Fimbriae Proteins, Fimbriae, Bacterial, Gram-Negative Bacteria, Molecular Chaperones, Protein Conformation
Abstract

Bacterial pathogens utilize the chaperone-usher pathway to assemble extracellular multi-subunit fibers essential for virulence. The periplasmic chaperone facilitates the initial folding of fiber subunits but then traps them in activated folding transition states. Chaperone dissociation releases the folding energy that drives subunit incorporation into the fiber, which grows through a pore formed by the outer-membrane usher.

DOI10.1016/j.bbamcr.2004.02.010
Alternate JournalBiochim. Biophys. Acta
PubMed ID15546670
Grant ListAI29549 / AI / NIAID NIH HHS / United States
AI48689 / AI / NIAID NIH HHS / United States
DK51406 / DK / NIDDK NIH HHS / United States
DK64540 / DK / NIDDK NIH HHS / United States