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Title | Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 8072, Year 2023 |
Publish date | Dec 6, 2023 |
Authors | 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 De Reuse / |
PubMed 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 ...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. |
External links | Nat Commun / PubMed:38057323 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.75 - 4.1 Å |
Structure data | EMDB-16647, PDB-8cgl: PDB-7pcr: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | HYDROLASE / RNase J / Helicobacter pylori / RNA metabolism / RNA BINDING PROTEIN / ribonuclease / degradosome |