7PCR

Helicobacter pylori RNase J

7PCR の概要

• エントリーDOI: 10.2210/pdb7pcr/pdb
• 分子名称: Ribonuclease J (2 entities in total)
• 機能のキーワード: rnase j, helicobacter pylori, rna metabolism, hydrolase
• 由来する生物種: Helicobacter pylori 26695
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61502.62

構造登録者

Luisi, B.F.,Pei, X.Y. (登録日: 2021-08-03, 公開日: 2022-05-25, 最終更新日: 2024-01-31)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.75 Å)