9QH3

Pseudomonas aeruginosa polynucleotide phosphorylase in complex with recognition site of RNase E

9QH3 の概要

• エントリーDOI: 10.2210/pdb9qh3/pdb
• EMDBエントリー: 53153
• 分子名称: Polyribonucleotide nucleotidyltransferase, Ribonuclease E, ADENOSINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: polynucleotide phosphorylase, ribonuclease e, rna degradosome, rna binding protein
• 由来する生物種: Pseudomonas aeruginosa PAO1; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 183136.53

構造登録者

Paris, G.,Luisi, B.F. (登録日: 2025-03-14, 公開日: 2025-05-14, 最終更新日: 2025-11-26)

主引用文献

Paris, G.,Katsuya-Gaviria, K.,Clarke, H.,Johncock, M.,Dendooven, T.,Lulla, A.,Luisi, B.F.
A multi-dentate, cooperative interaction between endo- and exo-ribonucleases within the bacterial RNA degradosome.
Nucleic Acids Res., 53:-, 2025

PubMed Abstract: In Escherichia coli and numerous other bacteria, two of the principal enzymes mediating messenger RNA decay and RNA processing-RNase E, an endoribonuclease, and polynucleotide phosphorylase (PNPase), an exoribonuclease-assemble into a multi-enzyme complex known as the RNA degradosome. While RNase E forms a homotetramer and PNPase a homotrimer, it remains unclear how these two enzymes interact within the RNA degradosome to potentially satisfy all mutual recognition sites. In this study, we used cryo-EM, biochemistry, and biophysical studies to discover and characterize a new binding mode for PNPase encompassing two or more motifs that are necessary and sufficient for strong interaction with RNase E. While a similar interaction is seen in Salmonella enterica, a different recognition mode arose for Pseudomonas aeruginosa, illustrating the evolutionary drive to maintain physical association of the two ribonucleases. The data presented here suggest a model for the quaternary organization of the RNA degradosome of E. coli, where one PNPase trimer interacts with one RNase E protomer. Conformational transitions are predicted to facilitate substrate capture and transfer to catalytic centres. The model suggests how the endo- and exo-ribonucleases might cooperate in cellular RNA turnover and recruitment of regulatory RNA by the degradosome assembly.

PubMed: 41036625
DOI: 10.1093/nar/gkaf960

実験手法

ELECTRON MICROSCOPY (2.4 Å)