Dissection of pilus tip assembly by the FimD usher monomer.
Dissection of pilus tip assembly by the FimD usher monomer.
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DOI:
10.1016/j.jmb.2012.12.024
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发表时间:
2013-03-11
影响因子:
5.6
通讯作者:
Waksman, Gabriel
中科院分区:
文献类型:
--
作者:
Allen, William J.;Phan, Gilles;Hultgren, Scott J.;Waksman, Gabriel
Type 1 pili are representative of a class of bacterial surface structures assembled by the conserved chaperone/usher pathway and used by uropathogenic Escherichia coli to attach to bladder cells during infection. The outer membrane assembly platform—the usher—is critical for the formation of pili, catalysing the polymerisation of pilus subunits and enabling the secretion of the nascent pilus. Despite extensive structural characterisation of the usher, a number of questions about its mechanism remain, notably its oligomerisation state, and how it orchestrates the ordered assembly of pilus subunits. We demonstrate here that the FimD usher is able to catalyse in vitro pilus assembly effectively in its monomeric form. Furthermore, by establishing the kinetics of usher-catalysed reactions between various pilus subunits, we establish a complete kinetic model of tip fibrillum assembly, able to account for the order of subunits in native type 1 pili. ► The mechanism of pilus tip assembly by FimD is investigated. ► The FimD usher can catalyse donor strand exchange in its monomeric form. ► A novel model for the kinetics of donor strand exchange is proposed. ► A complete kinetic characterisation of pilus biogenesis is achieved.
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5.6
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通讯作者:
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