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Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP

Author

Listed:
  • Anna Perederina

    (Pennsylvania State University)

  • Di Li

    (Pennsylvania State University)

  • Hyunwook Lee

    (Pennsylvania State University)

  • Carol Bator

    (Pennsylvania State University)

  • Igor Berezin

    (Pennsylvania State University)

  • Susan L. Hafenstein

    (Pennsylvania State University
    Pennsylvania State University)

  • Andrey S. Krasilnikov

    (Pennsylvania State University
    Pennsylvania State University)

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.

Suggested Citation

  • Anna Perederina & Di Li & Hyunwook Lee & Carol Bator & Igor Berezin & Susan L. Hafenstein & Andrey S. Krasilnikov, 2020. "Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17308-z
    DOI: 10.1038/s41467-020-17308-z
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    Cited by:

    1. Nic Robertson & Vadim Shchepachev & David Wright & Tomasz W. Turowski & Christos Spanos & Aleksandra Helwak & Rose Zamoyska & David Tollervey, 2022. "A disease-linked lncRNA mutation in RNase MRP inhibits ribosome synthesis," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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