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- Title
Escherichia coli Hfq has distinct interaction surfaces for DsrA, rpoS and poly(A) RNAs.
- Authors
Mikulecky, Peter J.; Kaw, Meenakshi K.; Brescia, Cristin C.; Takach, Jennifer C.; Sledjeski, Darren D.; Feig, Andrew L.
- Abstract
The bacterial Sm-like protein Hfq facilitates RNA-RNA interactions involved in post-transcriptional regulation of the stress response. Specifically, Hfq helps pair noncoding RNAs (ncRNAs) with complementary regions of target mRNAs. To probe the mechanism of this pairing, we generated a series of Hfq mutants and measured their affinity for RNAs like those with which Hfq must associate in vivo. We tested the mutants' DsrA-dependent activation of rpoS, and their ability to stabilize DsrA ncRNA against degradation in vivo. Our results suggest that Hfq has two independent RNA-binding surfaces. In addition to a well-known site around the core of the Hfq hexamer, we observe interactions with the distal face of Hfq, a new locus with which mRNAs and poly(A) sequences associate. Our model explains how Hfq can simultaneously bind a ncRNA and its mRNA target to facilitate the strand displacement reaction required for Hfq-dependent translational regulation.
- Subjects
BACTERIAL genetics; ESCHERICHIA coli; RNA; GENETICS; PROTEOMICS; MOLECULAR biology
- Publication
Nature Structural & Molecular Biology, 2004, Vol 11, Issue 12, p1206
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb858