期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 105, 期 35, 页码 12873-12878出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0802177105
关键词
donor strand exchange; electrospray ionization; noncovalent protein complexes; uropathogenic bacteria
资金
- BBSRC
- Medical Research Council
- Wellcome Trust
- MRC [G0800002] Funding Source: UKRI
- Medical Research Council [G0800002] Funding Source: researchfish
P pili are multisubunit fibers essential for the attachment of uropathogenic Escherichia coli to the kidney. These fibers are formed by the noncovalent assembly of six different homologous subunit types in an array that is strictly defined in terms of both the number and order of each subunit type. Assembly occurs through a mechanism termed donor-strand exchange (DSE) in which an N-terminal extension (Nte) of one subunit donates a beta-strand to an adjacent subunit, completing its Ig fold. Despite structural determination of the different subunits, the mechanism determining specificity of subunit ordering in pilus assembly remained unclear. Here, we have used noncovalent mass spectrometry to monitor DSE between all 30 possible pairs of P pilus subunits and their Ntes. We demonstrate a striking correlation between the natural order of subunits in pili and their ability to undergo DSE in vitro. The results reveal insights into the molecular mechanism by which subunit ordering during the assembly of this complex is achieved.
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