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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
PubMed

Insights

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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