RNase J2 is a specificity factor that governs global mRNA stability in Bacillus subtilis
Abstract
Ribonucleases (RNases) play a key role in modulating gene expression at the post-transcriptional level, enabling bacteria to rapidly adapt to their environment. The B. subtilis genome encodes more than 20 RNases and understanding the role of each of these enzymes is crucial for a comprehensive knowledge of bacterial post-transcriptional adaptation mechanisms. Among these, RNase J1 and J2, belonging to the ß-lactamase enzyme family, form a heterodimer. While the primary function of RNase J1 as a 5’-exoribonuclease in B. subtilis has been known for some time, the role of RNase J2, encoded by the rnjB gene, has remained unclear. Indeed, it has been considered a minor degradation factor due its very weak 5’-exoribonuclease in vitro , the lack of a growth phenotype and the limited number of mRNAs with altered equilibrium levels in rnjB mutants. In this study, we demonstrate that the absence of RNase J2 influences pellicle and macro-colony biofilm formation, as well as swarming in B. subtilis . We show that RNase J2 plays a far more global role in governing mRNA half-lives than originally thought, by stimulating RNase J1-mediated degradation of a subset of RNase J1’s mRNA substrates. An inter-subunit salt-bridge between RNase J1 and J2 is crucial for RNase J2 action. Altogether, our results suggest that RNase J2 acts primarily as a specificity co-factor for RNase J1 rather than as a ribonuclease per se. Significance This study elucidates the role of RNase J2 in RNA degradation in B. subtilis . Through a combination of phenotypic analyses and Rif-seq data, we demonstrate that RNase J2 plays a far more important role than previously appreciated. We provide evidence that physical interactions between RNase J1 and J2 (via salt-bridge) are critical for the degradation of RNase J2 targets, suggesting that RNase J2 acts more as a co-factor of RNase J1 than as a standalone RNase.
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BibTeX
@misc{christol2026rnase,
title = {{RNase J2 is a specificity factor that governs global mRNA stability in Bacillus subtilis}},
author = {Ninon Christol and Michelle Goujout and Alexandre Maes and Tania Kamwouo and Hannah Leblanc and Marie-Françoise Noirot-Gros and Romain Briandet and Ciarán Condon and Sylvain Durand},
howpublished = {HAL},
year = {2026},
month = may,
doi = {10.64898/2026.05.27.728192},
url = {https://hal.science/hal-05750012v1},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - UNPB
TI - RNase J2 is a specificity factor that governs global mRNA stability in Bacillus subtilis
AU - Ninon Christol
AU - Michelle Goujout
AU - Alexandre Maes
AU - Tania Kamwouo
AU - Hannah Leblanc
AU - Marie-Françoise Noirot-Gros
AU - Romain Briandet
AU - Ciarán Condon
AU - Sylvain Durand
PY - 2026
DA - 2026/05/27
PB - HAL
DO - 10.64898/2026.05.27.728192
UR - https://hal.science/hal-05750012v1
AB - Ribonucleases (RNases) play a key role in modulating gene expression at the post-transcriptional level, enabling bacteria to rapidly adapt to their environment. The B. subtilis genome encodes more than 20 RNases and understanding the role of each of these enzymes is crucial for a comprehensive knowledge of bacterial post-transcriptional adaptation mechanisms. Among these, RNase J1 and J2, belonging to the ß-lactamase enzyme family, form a heterodimer. While the primary function of RNase J1 as a 5’-exoribonuclease in B. subtilis has been known for some time, the role of RNase J2, encoded by the rnjB gene, has remained unclear. Indeed, it has been considered a minor degradation factor due its very weak 5’-exoribonuclease in vitro , the lack of a growth phenotype and the limited number of mRNAs with altered equilibrium levels in rnjB mutants. In this study, we demonstrate that the absence of RNase J2 influences pellicle and macro-colony biofilm formation, as well as swarming in B. subtilis . We show that RNase J2 plays a far more global role in governing mRNA half-lives than originally thought, by stimulating RNase J1-mediated degradation of a subset of RNase J1’s mRNA substrates. An inter-subunit salt-bridge between RNase J1 and J2 is crucial for RNase J2 action. Altogether, our results suggest that RNase J2 acts primarily as a specificity co-factor for RNase J1 rather than as a ribonuclease per se. Significance This study elucidates the role of RNase J2 in RNA degradation in B. subtilis . Through a combination of phenotypic analyses and Rif-seq data, we demonstrate that RNase J2 plays a far more important role than previously appreciated. We provide evidence that physical interactions between RNase J1 and J2 (via salt-bridge) are critical for the degradation of RNase J2 targets, suggesting that RNase J2 acts more as a co-factor of RNase J1 than as a standalone RNase.
ER -