7C79

Cryo-EM structure of yeast Ribonuclease MRP

7C79 の概要

• エントリーDOI: 10.2210/pdb7c79/pdb
• EMDBエントリー: 30296
• 分子名称: Ribonuclease MRP RNA subunit NME1, Ribonuclease MRP protein subunit SNM1, Ribonuclease MRP protein subunit RMP1, ... (13 entities in total)
• 機能のキーワード: ribonuclease mrp, rna-protein complex, rna binding protein
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 445021.19

構造登録者

Lan, P.,Wu, J.,Lei, M. (登録日: 2020-05-24, 公開日: 2020-07-08, 最終更新日: 2024-03-27)

主引用文献

Lan, P.,Zhou, B.,Tan, M.,Li, S.,Cao, M.,Wu, J.,Lei, M.
Structural insight into precursor ribosomal RNA processing by ribonuclease MRP.
Science, 369:656-663, 2020

PubMed Abstract: Ribonuclease (RNase) MRP is a conserved eukaryotic ribonucleoprotein complex that plays essential roles in precursor ribosomal RNA (pre-rRNA) processing and cell cycle regulation. In contrast to RNase P, which selectively cleaves transfer RNA-like substrates, it has remained a mystery how RNase MRP recognizes its diverse substrates. To address this question, we determined cryo-electron microscopy structures of RNase MRP alone and in complex with a fragment of pre-rRNA. These structures and the results of biochemical studies reveal that coevolution of both protein and RNA subunits has transformed RNase MRP into a distinct ribonuclease that processes single-stranded RNAs by recognizing a short, loosely defined consensus sequence. This broad substrate specificity suggests that RNase MRP may have myriad yet unrecognized substrates that could play important roles in various cellular contexts.

PubMed: 32586950
DOI: 10.1126/science.abc0149

実験手法

ELECTRON MICROSCOPY (2.5 Å)