Structural model of an mRNA in complex with the bacterial chaperone Hfq

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

Research output: Contribution to journalArticlepeer-review

46 Scopus citations


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. Here, 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. Our results show how Hfq specifically distorts the structure of the rpoS mRNA to enable sRNA base pairing and translational control.

Original languageEnglish (US)
Pages (from-to)17134-17139
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number48
StatePublished - Dec 2 2014


  • Bacterial posttranscriptional control
  • Lsm protein
  • RNA-protein interactions
  • SAXS
  • Small noncoding RNA

ASJC Scopus subject areas

  • General


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