RNase E autoregulates its synthesis in Escherichia coli by binding directly to a stem-loop in the rne 5' untranslated region.

RNase E autoregulates its production in Escherichia coli by governing the decay rate of rne (RNase E) mRNA. It does so by a mechanism that is dependent in part on hp2, a cis-acting stem-loop within the rne 5' untranslated region. In principle, hp2 could function either as a cleavage site for RNase E or as a binding site for that protein or an ancillary factor. Here we show that the effector region at the top of hp2 is cleaved poorly by RNase E yet binds the catalytic domain of that ribonuclease with a sequence specificity reflecting its efficacy in feedback regulation. These findings suggest that hp2 controls RNase E synthesis by binding to RNase E and expediting cleavage elsewhere within the rne transcript.