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

Alejandro Tejada-Arranz, Aleksei Lulla, Maxime Bouilloux-Lafont, Evelyne Turlin, Xue-Yuan Pei, Thibaut Douché, Mariette Matondo, Allison H. Williams, Bertrand Raynal, Ben F. Luisi and Hilde Reuse ()
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Alejandro Tejada-Arranz: Institut Pasteur
Aleksei Lulla: University of Cambridge
Maxime Bouilloux-Lafont: Institut Pasteur
Evelyne Turlin: Institut Pasteur
Xue-Yuan Pei: University of Cambridge
Thibaut Douché: Unité de Spectrométrie de Masse pour la Biologie, C2RT, USR CNRS 2000, Institut Pasteur
Mariette Matondo: Unité de Spectrométrie de Masse pour la Biologie, C2RT, USR CNRS 2000, Institut Pasteur
Allison H. Williams: University of California San Francisco, Cellular Molecular Pharmacology
Bertrand Raynal: Institut Pasteur
Ben F. Luisi: University of Cambridge
Hilde Reuse: Institut Pasteur

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-43825-8

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