Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins

Thoma, Johannes and Burmann, Björn M. and Hiller, Sebastian and Müller, Daniel J.. (2015) Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins. Nature structural & molecular biology, 22 (10). pp. 795-802.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/41193/

Downloads: Statistics Overview


Chaperones increase the folding yields of soluble proteins by suppressing misfolding and aggregation, but how they modulate the folding of integral membrane proteins is not well understood. Here we use single-molecule force spectroscopy and NMR spectroscopy to observe the periplasmic holdase chaperones SurA and Skp shaping the folding trajectory of the large β-barrel outer-membrane receptor FhuA from Escherichia coli. Either chaperone prevents FhuA from misfolding by stabilizing a dynamic, unfolded state, thus allowing the substrate to search for structural intermediates. During this search, the SurA-chaperoned FhuA polypeptide inserts β-hairpins into the membrane in a stepwise manner until the β-barrel is folded. The membrane acts as a free-energy sink for β-hairpin insertion and physically separates transient folds from chaperones. This stabilization of dynamic unfolded states and the trapping of folding intermediates funnel the FhuA polypeptide toward the native conformation.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publ. Group
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:19 Dec 2017 13:20
Deposited On:23 Aug 2016 08:00

Repository Staff Only: item control page