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Publication Abstract from PubMed

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.

Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease.,Tejada-Arranz A, Lulla A, Bouilloux-Lafont M, Turlin E, Pei XY, Douche T, Matondo M, Williams AH, Raynal B, Luisi BF, De Reuse H Nat Commun. 2023 Dec 6;14(1):8072. doi: 10.1038/s41467-023-43825-8. PMID:38057323^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.