Rose, R.J., Verger, D., Daviter, T., Remaut, H., Paci, E., Waksman, G., Ashcroft, A.E. and Radford, S.E. (2008) Unraveling the molecular basis of subunit specificity in P pilus assembly by mass spectrometry. Proceedings of the National Academy of Sciences of The United States of America, 105 (35). pp. 12873-12878.Full text available as:
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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 β-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.
|Copyright, Publisher and Additional Information:||© 2008 National Academy of Sciences. This is an author produced version of a paper published in Proceedings of the National Academy of Sciences of The United States of America. Uploaded in accordance with the publisher's self archiving policy.|
|Academic Units:||The University of Leeds > Faculty of Biological Sciences (Leeds) > Institute of Molecular and Cellular Biology (Leeds)
The University of Leeds > University of Leeds Research Centres and Institutes > Astbury Centre for Structural Molecular Biology (Leeds)
|Depositing User:||Sherpa Assistant|
|Date Deposited:||13 Nov 2008 15:03|
|Last Modified:||08 Feb 2013 17:05|
|Publisher:||National Academy of Sciences|
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