Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-05107-6
Keywords
-
Categories
Funding
- Ministry of Economy and Competitiveness (MINECO) [BIO2016-77390-R, BFU2015-71964, CTQ2015-65320-R]
- European Commission
- Basque Government
- CIC nanoGUNE
- Ikerbasque Foundation for Science
- MINECO [RYC-2016-19590, FIS2012-37549-C05, FIS2015-64886-C5-1-P]
- Programa Red Guipuzcoana de Ciencia, Tecnologia e Innovacion, Diputacion Foral de Gipuzkoa [Exp. 97/14]
- ERDF
- ESF
Ask authors/readers for more resources
Uropathogenic Escherichia coil attach to tissues using pili type 1. Each pilus is composed by thousands of coiled FimA domains followed by the domains of the tip fibrillum, FimF-FimG-FimH. The domains are linked by non-covalent beta-strands that must resist mechanical forces during attachment. Here, we use single-molecule force spectroscopy to measure the mechanical contribution of each domain to the stability of the pilus and monitor the oxidative folding mechanism of a single Fim domain assisted by periplasmic FimC and the oxidor-eductase DsbA. We demonstrate that pilus domains bear high mechanical stability following a hierarchy by which domains close to the tip are weaker than those close to or at the pilus rod. During folding, this remarkable stability is achieved by the intervention of DsbA that not only forms strategic disulfide bonds but also serves as a chaperone assisting the folding of the domains.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available