Bacteria thrive in ever-changing environments by quickly remodeling their transcriptome and
proteome via complex regulatory circuits. Regulation occurs at multiple steps, from the transcription of genes to the post-translational modification of
proteins, via both
protein and
RNA regulators. At the post-transcriptional level, the
RNA fate is balanced through the binding of ribosomes, chaperones and
ribonucleases. We aim to decipher the role of the
double-stranded-RNA-specific
endoribonuclease RNase III and to evaluate its
biological importance in the adaptation to modifications of the environment. The inactivation of
RNase III affects a large number of genes and leads to several phenotypical defects, such as reduced thermotolerance in Escherichia coli. In this study, we reveal that
RNase III inactivation leads to an increased sensitivity to temperature
shock and oxidative stress. We further show that
RNase III is important for the induction of the heat shock
sigma factor RpoH and for the expression of the
superoxide dismutase SodA.