Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst |
| |
Authors: | Nishiyama Mireille Ishikawa Takashi Rechsteiner Helene Glockshuber Rudi |
| |
Affiliation: | Institute of Molecular Biology and Biophysics, Eidgen?ssische Technische Hochschule (ETH) Zurich, 8093 Zurich, Switzerland. |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|