8cgl | pdb_00008cgl
Cryo-EM structure of RNase J from Helicobacter pylori
Structural highlights
FunctionRNJ_HELP8 An RNase that has 5'-3' exonuclease and possibly endoonuclease activity. Degrades 5'-monophosphorylated ssRNA and dsRNA, considerably more active on ssRNA. Association with RhpA significantly increases the dsRNase activity. Stimulates ATPase activity of RNA helicase RhpA. Involved in stabilization of mRNA but apparently not rRNA.[1] Publication Abstract from PubMedIn 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. References
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