Structural Model of an mRNA in Complex with the Bacterial Chaperone Hfq

Published

October 20, 2014

Author(s)

Yi Peng, Joseph E. Curtis, Xianyang Fang, Sarah A. Woodson

Abstract

Small non-coding (s)RNAs and their chaperone protein Hfq regulate bacterial gene expression in response to stress and other environmental signals. Hfq binds specific RNA sequence motifs and facilitates base pairing between complementary sRNA-mRNA pairs. Here, we present a low-resolution model of Hfq bound to the rpoS mRNA 5'UTR, a bacterial stress response regulator. Small angle X-ray scattering and SHAPE footprinting show that the sital face and lateral rim of Hfq interact with three sites in the rpoS 5'UTR, folding the RNA into a compact tertiary structure. These interactions position the sRNA also binds. Our model suggest how Hfq distorts the structure of the rpoS 5'UTR for SRNA entry and translational control.

Citation

Proceedings of the National Academy of Sciences of the United States of America

Volume

111

Issue

48

Pub Type

Journals

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Keywords

Small-angle scattering, RNA, Monte Carlo, Molecular Dynamics

Citation

Peng, Y. , Curtis, J. , Fang, X. and Woodson, S. (2014), Structural Model of an mRNA in Complex with the Bacterial Chaperone Hfq, Proceedings of the National Academy of Sciences of the United States of America, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=915814 (Accessed October 9, 2025)