Publication Date:
2008-03-29
Description:
Type 1 pili from uropathogenic Escherichia coli are a prototype of adhesive surface organelles assembled and secreted by the conserved chaperone/usher pathway. We reconstituted type 1 pilus biogenesis from purified pilus proteins. The usher FimD acted as a catalyst to accelerate the ordered assembly of protein subunits independently of cellular energy. Its activity was highly dependent on the adhesin subunit FimH, which triggered the conversion of FimD into a high-efficiency assembly catalyst. Furthermore, a simple kinetic model adequately rationalized usher-catalyzed pilus assembly in vivo. Our results contribute to a mechanistic understanding of protein-catalyzed biogenesis of supramolecular protein complexes at the bacterial outer cell membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishiyama, Mireille -- Ishikawa, Takashi -- Rechsteiner, Helene -- Glockshuber, Rudi -- New York, N.Y. -- Science. 2008 Apr 18;320(5874):376-9. doi: 10.1126/science.1154994. Epub 2008 Mar 27.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biophysics, Eidgenossische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18369105" target="_blank"〉PubMed〈/a〉
Keywords:
Adhesins, Escherichia coli/metabolism
;
Bacterial Outer Membrane Proteins/*metabolism
;
Catalysis
;
Escherichia coli/*metabolism/ultrastructure
;
Escherichia coli Proteins/genetics/*metabolism
;
Fimbriae Proteins/genetics/*metabolism
;
Fimbriae, Bacterial/*metabolism/ultrastructure
;
Kinetics
;
Models, Biological
;
Temperature
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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