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

    Sauer, F.G. and Pinkner, J. and Waksman, Gabriel and Hultgren, S.J. (2002) Chaperone priming of pilus subunit facilitates a topological transition that drives fiber formation. Cell 111 (4), pp. 543-551. ISSN 0092-8674.

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    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.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 29 Apr 2019 14:06
    Last Modified: 29 Apr 2019 15:12
    URI: http://eprints.bbk.ac.uk/id/eprint/27344

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