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  • center
  • program_project
  • nrc
  • whocc
  • project
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  • tool
  • patent
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  • Assistant Professor
  • Associate Professor
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  • Clinical Research Nurse
  • Clinician Researcher
  • Department Manager
  • Dual-education Student
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  • Lab assistant
  • Master Student
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  • Nursing Staff
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Prize
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
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Scientific Fields
Diseases
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Published in Nature communications - 06 Dec 2023

Tejada-Arranz A, Lulla A, Bouilloux-Lafont M, Turlin E, Pei XY, Douché T, Matondo M, Williams AH, Raynal B, Luisi BF, De Reuse H

Link to Pubmed [PMID] – 38057323

Link to DOI – 10.1038/s41467-023-43825-8

Nat Commun 2023 Dec; 14(1): 8072

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.