Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease.
Nat Commun
; 14(1): 8072, 2023 Dec 06.
Article
en En
| MEDLINE
| ID: mdl-38057323
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.
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1
Banco de datos:
MEDLINE
Asunto principal:
Ribonucleasas
/
Helicobacter pylori
Idioma:
En
Año:
2023
Tipo del documento:
Article