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Article Dans Une Revue Nature Communications Année : 2023

Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease

Xue-Yuan Pei
Ben Luisi

Résumé

Abstract In the gastric pathogen Helicobacter pylori , post-transcriptional regulation relies strongly on the activity of the essential ribonuclease RNase J. Here, we elucidated the crystal and cryo-EM structures of RNase J and determined that it assembles into dimers and tetramers in vitro. We found that RNase J extracted from H. pylori is acetylated on multiple lysine residues. Alanine substitution of several of these residues impacts on H. pylori morphology, and thus on RNase J function in vivo. Mutations of Lysine 649 modulates RNase J oligomerization in vitro, which in turn influences ribonuclease activity in vitro. Our structural analyses of RNase J reveal loops that gate access to the active site and rationalizes how acetylation state of K649 can influence activity. We propose acetylation as a regulatory level controlling the activity of RNase J and its potential cooperation with other enzymes of RNA metabolism in H. pylori .
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hal-04612500 , version 1 (17-06-2024)

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Alejandro Tejada-Arranz, Aleksei Lulla, Maxime Bouilloux-Lafont, Evelyne Turlin, Xue-Yuan Pei, et al.. Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease. Nature Communications, 2023, 14 (1), pp.8072. ⟨10.1038/s41467-023-43825-8⟩. ⟨hal-04612500⟩
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