Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation

Frederic G. Sauer, Jerome S. Pinkner, Gabriel Waksman, Scott J. Hultgren

Research output: Contribution to journalArticle

204 Scopus citations

Abstract

Periplasmic chaperones direct the assembly of adhesive, multi-subunit pilus fibers that play critical roles in bacterial pathogenesis. Pilus assembly occurs via a donor strand exchange mechanism in which the N-terminal extension of one subunit replaces the chaperone G1 strand that transiently occupies a groove in the neighboring subunit. Here, we show that the chaperone primes the subunit for assembly by holding the groove in an open, activated conformation. During donor strand exchange, the subunit undergoes a topological transition that triggers the closure of the groove and seals the N-terminal extension in place. It is this topological transition, made possible only by the priming action of the chaperone that drives subunit assembly into the fiber.

Original languageEnglish
Pages (from-to)543-551
Number of pages9
JournalCell
Volume111
Issue number4
DOIs
StatePublished - Nov 15 2002

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