7PCR

Helicobacter pylori RNase J

Summary for 7PCR

• Entry DOI: 10.2210/pdb7pcr/pdb
• Descriptor: Ribonuclease J (2 entities in total)
• Functional Keywords: rnase j, helicobacter pylori, rna metabolism, hydrolase
• Biological source: Helicobacter pylori 26695
• Total number of polymer chains: 1
• Total formula weight: 61502.62

Authors

Luisi, B.F.,Pei, X.Y. (deposition date: 2021-08-03, release date: 2022-05-25, Last modification date: 2024-01-31)

Primary citation

Tejada-Arranz, A.,Lulla, A.,Bouilloux-Lafont, M.,Turlin, E.,Pei, X.Y.,Douche, T.,Matondo, M.,Williams, A.H.,Raynal, B.,Luisi, B.F.,De Reuse, H.
Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease.
Nat Commun, 14:8072-8072, 2023

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 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.

PubMed: 38057323
DOI: 10.1038/s41467-023-43825-8

Experimental method

X-RAY DIFFRACTION (2.75 Å)