RNase III Participates in the Adaptation to Temperature Shock and Oxidative Stress in Escherichia coli

Abstract

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.

RNase III participates in control of quorum sensing, pigmentation and oxidative stress resistance in Rhodobacter sphaeroides

“…A functional role of RNases in the stress response of numerous microorganisms has been reported already in the past. Often a reduction or lack of the native RNase activity leads to enhanced susceptibility towards various cellular stresses, like oxidative, osmotic or temperature stress (Duggal et al, 2020; Förstner et al, 2018; Lejars & Hajnsdorf, 2022; Möller et al, 2019; Spanka et al, 2021). In contrast, our data (Figure 9) document a higher resistance of R. sphaeroides against oxidative stress when RNase III activity is lacking.…”