7C79

Cryo-EM structure of yeast Ribonuclease MRP

Summary for 7C79

• Entry DOI: 10.2210/pdb7c79/pdb
• EMDB information: 30296
• Descriptor: Ribonuclease MRP RNA subunit NME1, Ribonuclease MRP protein subunit SNM1, Ribonuclease MRP protein subunit RMP1, ... (13 entities in total)
• Functional Keywords: ribonuclease mrp, rna-protein complex, rna binding protein
• Biological source: Saccharomyces cerevisiae S288C; More
• Total number of polymer chains: 12
• Total formula weight: 445021.19

Authors

Lan, P.,Wu, J.,Lei, M. (deposition date: 2020-05-24, release date: 2020-07-08, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.5 Å)