Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP
Anna Perederina1, Di Li1, Hyunwook Lee1
1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, 16802, PA, USA.
Nature Communications
|July 12, 2020
Summary
The cryo-EM structure of the S. cerevisiae RNase MRP holoenzyme reveals RNA-driven protein remodeling. This remodeling allows functional diversification of RNase MRP and RNase P, explaining how catalytic RNPs acquire new functions.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- RNase MRP is a crucial eukaryotic ribonucleoprotein complex.
- It plays roles in rRNA maturation and cell cycle regulation.
- RNase MRP is related to RNase P but has evolved distinct functions.
Purpose of the Study:
- To determine the cryo-EM structure of the S. cerevisiae RNase MRP holoenzyme.
- To elucidate the interactions between RNase MRP components and its catalytic RNA organization.
- To understand the structural basis for functional diversification of RNase MRP and RNase P.
Main Methods:
- Cryo-electron microscopy (cryo-EM) at 3.0 Å resolution.
- Structural analysis of the 450 kDa RNase MRP complex.
- Investigation of protein-RNA interactions and component organization.
Main Results:
- Detailed structure of the S. cerevisiae RNase MRP holoenzyme.
- Identification of RNA-driven remodeling in shared RNase MRP/RNase P proteins.
- Demonstration of how this remodeling and auxiliary elements drive functional diversification.
Conclusions:
- The structure provides insights into the functional divergence of RNase MRP and RNase P.
- RNA-driven protein remodeling is key to the evolution of catalytic RNPs.
- Structural mechanisms for the acquisition of new functions by RNase MRP are revealed.
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