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

Author

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  • Alejandro Tejada-Arranz

    (Institut Pasteur
    Université de Paris, Sorbonne Paris Cité
    University of Basel)

  • 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)

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.

Suggested Citation

  • 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 & Hilde Reu, 2023. "Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43825-8
    DOI: 10.1038/s41467-023-43825-8
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    References listed on IDEAS

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    1. Cynthia M. Sharma & Steve Hoffmann & Fabien Darfeuille & Jérémy Reignier & Sven Findeiß & Alexandra Sittka & Sandrine Chabas & Kristin Reiche & Jörg Hackermüller & Richard Reinhardt & Peter F. Stadler, 2010. "The primary transcriptome of the major human pathogen Helicobacter pylori," Nature, Nature, vol. 464(7286), pages 250-255, March.
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