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Small  RNA s post‐transcriptionally regulate many processes in bacteria. Base‐pairing of  sRNA s near ribosome‐binding sites in  mRNA s inhibits translation, often requiring the  RNA  chaperone Hfq. In the canonical model, Hfq simultaneously binds  sRNA s and  mRNA  targets to accelerate pairing. Here, we show that the  Escherichia coli   sRNA s OmrA and OmrB inhibit translation of the diguanylate cyclase DgcM (previously: YdaM), a player in biofilm regulation. In OmrA/B repression of  dgcM , Hfq is not required as an  RNA  interaction platform, but rather unfolds an inhibitory  RNA  structure that impedes OmrA/B binding. This restructuring involves distal face binding of Hfq and is supported by  RNA  structure mapping. A corresponding mutant protein cannot support inhibition  in vitro  and  in vivo ; proximal and rim mutations have negligible effects. Strikingly, OmrA/B‐dependent translational inhibition  in vitro  is restored, in complete absence of Hfq, by a deoxyoligoribonucleotide that base‐pairs to the biochemically mapped Hfq site in  dgcM   mRNA . We suggest that Hfq‐dependent  RNA  structure remodeling can promote  sRNA  access, which represents a mechanism distinct from an interaction platform model.

Hfq‐dependent mRNA unfolding promotes sRNA ‐based inhibition of translation