RNase Y mediates posttranscriptional control of the virulence-associated CncR1 small-RNA in Helicobacter pylori

Ribonucleases are involved in several biological processes, including the turnover of structural and messenger RNAs and the specific processing of the cellular transcriptome. Here, we characterized the RNase Y from <i>Helicobacter pylori</i>. We found that RNase Y is membrane-associated and its expression is controlled during bacterial growth and by Fur in response to iron. We observed that RNase Y deletion has a limited impact on <i>H. pylori</i> transcriptome and on bacterial growth. Interestingly, we found that RNase Y is involved in the metabolism of CncR1, a virulence-associated sRNA oppositely modulating bacterial motility and adhesion to host cells. Indeed, RNase Y inactivation led to the accumulation of a 3'-extended CncR1 isoform, which appeared unable to interact <i>in vitro</i> with a known target mRNA. The observation that the RNAse Y-mutant strain showed deregulation of several members of the CncR1 regulon suggests this ribonuclease has an important role in <i>H. pylori</i> posttranscriptional regulation.