Your browser version may not work well with NCBI's Web applications. More information
here...
Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst.
Nishiyama M, Ishikawa T, Rechsteiner H, Glockshuber R.
Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland.
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.
Publication Types:
PMID: 18369105 [PubMed - indexed for MEDLINE]