Autoregulation allows Escherichia coli RNase E to adjust continuously its synthesis to that of its substrates

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In this Subject: <a title="Microbiology" href="/content/subcat;jsessionid=63isqosnqs8i4.alice?j_subject=161&j_availability=">Microbiology
By this author: Sousa S. ;&nbsp; Marchand I. ;&nbsp; Dreyfus M.

Authors: Sousa S.; Marchand I.; Dreyfus M.

Source: Molecular Microbiology, Volume 42, Number 3, November 2001 , pp. 867-878(12)

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Abstract:

The Escherichia coli endonuclease RNase E plays a key role in rRNA maturation and mRNA decay. In particular, it controls the decay of its own mRNA by cleaving it within the 5 prime -untranslated region (UTR), thereby autoregulating its synthesis. Here, we report that, when the synthesis of an RNase E substrate is artificially induced to high levels in vivo, both the rne mRNA concentration and RNase E synthesis increase abruptly and then decrease to a steady-state level that remains higher than in the absence of induction. Using rne–lacZ fusions that retain or lack the rne 5 prime UTR, we show that these variations reflect a transient mRNA stabilization mediated by the rne 5 prime UTR. Finally, by putting RNase E synthesis under the control of an IPTG-controlled promoter, we show that a similar, rne 5 prime UTR-mediated mRNA stabilization can result from a shortage of RNase E. We conclude that the burst in substrate synthesis has titrated RNase E, stabilizing the rne mRNA by protecting its 5 prime UTR. However, this stabilization is self-correcting, because it allows the RNase E pool to expand until its mRNA is destabilized again. Thus, autoregulation allows RNase E to adjust its synthesis to that of its substrates, a behaviour that may be common among autoregulated proteins. Incidentally, this adjustment cannot occur when translation is blocked, and we argue that the global mRNA stabilization observed under these conditions originates in part from this defect.