6W6V

Structure of yeast RNase MRP holoenzyme

Summary for 6W6V

• Entry DOI: 10.2210/pdb6w6v/pdb
• EMDB information: 21564
• Descriptor: RNA component of RNase MRP NME1, Ribonuclease MRP protein subunit RMP1, Ribonucleases P/MRP protein subunit POP1, ... (10 entities in total)
• Functional Keywords: ribozyme, rnp, ribonucleoprotein, hydrolase
• Biological source: Saccharomyces cerevisiae S288C (Baker's yeast); More
• Total number of polymer chains: 11
• Total formula weight: 422248.72

Authors

Perederina, A.,Li, D.,Lee, H.,Bator, C.,Berezin, I.,Hafenstein, S.L.,Krasilnikov, A.S. (deposition date: 2020-03-17, release date: 2020-07-15, Last modification date: 2024-03-06)

Primary citation

Perederina, A.,Li, D.,Lee, H.,Bator, C.,Berezin, I.,Hafenstein, S.L.,Krasilnikov, A.S.
Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.
Nat Commun, 11:3474-3474, 2020

PubMed Abstract: RNase MRP is an essential eukaryotic ribonucleoprotein complex involved in the maturation of rRNA and the regulation of the cell cycle. RNase MRP is related to the ribozyme-based RNase P, but it has evolved to have distinct cellular roles. We report a cryo-EM structure of the S. cerevisiae RNase MRP holoenzyme solved to 3.0 Å. We describe the structure of this 450 kDa complex, interactions between its components, and the organization of its catalytic RNA. We show that some of the RNase MRP proteins shared with RNase P undergo an unexpected RNA-driven remodeling that allows them to bind to divergent RNAs. Further, we reveal how this RNA-driven protein remodeling, acting together with the introduction of new auxiliary elements, results in the functional diversification of RNase MRP and its progenitor, RNase P, and demonstrate structural underpinnings of the acquisition of new functions by catalytic RNPs.

PubMed: 32651392
DOI: 10.1038/s41467-020-17308-z

Experimental method

ELECTRON MICROSCOPY (3 Å)