Email RIS file
Bookmark
Report an Issue

Structural model of an mRNA in complex with the bacterial chaperone Hfq [electronic resource].

Published
Washington, D.C. : United States. Dept. of Energy, 2014.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
Physical Description
pages 17,134-17,139 : digital, PDF file
Additional Creators
Johns Hopkins University, United States. Department of Energy, National Institutes of Health (U.S.), National Science Foundation (U.S.), Engineering and Physical Sciences Research Council, and United States. Department of Energy. Office of Scientific and Technical Information
Access Online

Availability

I Want It
I Want It

Finding items...

Restrictions on Access
Free-to-read Unrestricted online access
Summary
The Sm-like protein Hfq (host factor Q-beta phage) facilitates regulation by bacterial small noncoding RNAs (sRNAs) in response to stress and other environmental signals. In this paper, we present a low-resolution model of Escherichia coli Hfq bound to the rpoS mRNA, a bacterial stress response gene that is targeted by three different sRNAs. Selective 2'-hydroxyl acylation and primer extension, small-angle X-ray scattering, and Monte Carlo molecular dynamics simulations show that the distal face and lateral rim of Hfq interact with three sites in the rpoS leader, folding the RNA into a compact tertiary structure. These interactions are needed for sRNA regulation of rpoS translation and position the sRNA target adjacent to an sRNA binding region on the proximal face of Hfq. Finally, our results show how Hfq specifically distorts the structure of the rpoS mRNA to enable sRNA base pairing and translational control.
Report Numbers
E 1.99:1168867
Subject(s)
Other Subject(s)
Note
Published through SciTech Connect.
11/17/2014.
Proceedings of the National Academy of Sciences of the United States of America 111 48 ISSN 0027-8424 AM
Yi Peng; Joseph E. Curtis; Xianyang Fang; Sarah A. Woodson.
Funding Information
AC02-06CH11357
R01 GM46686
CHE-1265821
EP/K039121/1
View MARC record | catkey: 23500653