Alternative Protein Topology-Mediated Evolution of a Catalytic Ribonucleoprotein
Autor: | Lien B. Lai, Hong-Duc Phan, Walter J. Zahurancik, Venkat Gopalan |
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Rok vydání: | 2020 |
Předmět: |
Mitochondrial RNA processing
RNase P Computational biology Biochemistry Article Non-coding RNAs Alternative protein 03 medical and health sciences 0302 clinical medicine Ribonucleases stomatognathic system Cryoelectron microscopy Endoribonucleases RNA Precursors Ribozymes RNA Processing Post-Transcriptional Molecular Biology Topology (chemistry) Selection (genetic algorithm) 030304 developmental biology Ribonucleoprotein 0303 health sciences Chemistry Yeast Ribonucleoproteins RNA Ribosomal RNA 030217 neurology & neurosurgery |
Zdroj: | Nature Communications |
ISSN: | 0968-0004 |
Popis: | 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. Ribozyme-based RNase MRP is an essential eukaryotic enzyme involved in the maturation of rRNA and is evolutionarily related to RNase P. Here, the authors present the 3.0 Å cryo-EM structure of the S. cerevisiae RNase MRP holoenzyme, a 450 kDa ribonucleoprotein complex and compare it with RNase P. |
Databáze: | OpenAIRE |
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