Mechanical architecture and folding of E. coli type 1 pilus domains

The pilus type 1 of uropathogenic E. coli must resist mechanical forces to remain attached to the epithelium. Here the authors use single-molecule force spectroscopy to demonstrate a hierarchy of mechanical stability among the pilus domains and show that the oxidoreductase DsbA also acts as a foldin...

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Autores principales:	Alvaro Alonso-Caballero, Jörg Schönfelder, Simon Poly, Fabiano Corsetti, David De Sancho, Emilio Artacho, Raul Perez-Jimenez
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/90d847fd94ed4db0be96ca5bbf74b922
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spelling	oai:doaj.org-article:90d847fd94ed4db0be96ca5bbf74b9222021-12-02T14:38:53ZMechanical architecture and folding of E. coli type 1 pilus domains10.1038/s41467-018-05107-62041-1723https://doaj.org/article/90d847fd94ed4db0be96ca5bbf74b9222018-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05107-6https://doaj.org/toc/2041-1723The pilus type 1 of uropathogenic E. coli must resist mechanical forces to remain attached to the epithelium. Here the authors use single-molecule force spectroscopy to demonstrate a hierarchy of mechanical stability among the pilus domains and show that the oxidoreductase DsbA also acts as a folding chaperone on the domains.Alvaro Alonso-CaballeroJörg SchönfelderSimon PolyFabiano CorsettiDavid De SanchoEmilio ArtachoRaul Perez-JimenezNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Alvaro Alonso-Caballero Jörg Schönfelder Simon Poly Fabiano Corsetti David De Sancho Emilio Artacho Raul Perez-Jimenez Mechanical architecture and folding of E. coli type 1 pilus domains
description	The pilus type 1 of uropathogenic E. coli must resist mechanical forces to remain attached to the epithelium. Here the authors use single-molecule force spectroscopy to demonstrate a hierarchy of mechanical stability among the pilus domains and show that the oxidoreductase DsbA also acts as a folding chaperone on the domains.
format	article
author	Alvaro Alonso-Caballero Jörg Schönfelder Simon Poly Fabiano Corsetti David De Sancho Emilio Artacho Raul Perez-Jimenez
author_facet	Alvaro Alonso-Caballero Jörg Schönfelder Simon Poly Fabiano Corsetti David De Sancho Emilio Artacho Raul Perez-Jimenez
author_sort	Alvaro Alonso-Caballero
title	Mechanical architecture and folding of E. coli type 1 pilus domains
title_short	Mechanical architecture and folding of E. coli type 1 pilus domains
title_full	Mechanical architecture and folding of E. coli type 1 pilus domains
title_fullStr	Mechanical architecture and folding of E. coli type 1 pilus domains
title_full_unstemmed	Mechanical architecture and folding of E. coli type 1 pilus domains
title_sort	mechanical architecture and folding of e. coli type 1 pilus domains
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/90d847fd94ed4db0be96ca5bbf74b922
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Mechanical architecture and folding of E. coli type 1 pilus domains

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