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.
| Original language | English (US) |
|---|---|
| Article number | 3474 |
| Journal | Nature communications |
| Volume | 11 |
| Issue number | 1 |
| DOIs | |
| State | Published - Dec 1 2020 |
| Externally published | Yes |
Bibliographical note
Funding Information:We are grateful to J.-P. Armache, P. Bevilacqua, L. Lindahl, and J. Reese for valuable suggestions, and to M. Schmitt for the generous gift of the YSW1 yeast strain. We are grateful to the staff of the cryo-EM and Proteomics Core facilities at the Huck Institutes of Life Sciences Core for assistance with data collection and processing, and mass spectrometry analysis, respectively. This work was supported by a grant from the National Institutes of Health R01GM135598 to ASK. The cryo-EM facility is supported, in part, by a grant TSF SAP #4100077246 from the Pennsylvania Department of Health.
Publisher Copyright:
© 2020, The Author(s).