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-Structure paper
Title | Structural insight into precursor ribosomal RNA processing by ribonuclease MRP. |
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Journal, issue, pages | Science, Vol. 369, Issue 6504, Page 656-663, Year 2020 |
Publish date | Aug 7, 2020 |
Authors | Pengfei Lan / Bin Zhou / Ming Tan / Shaobai Li / Mi Cao / Jian Wu / Ming Lei / |
PubMed Abstract | Ribonuclease (RNase) MRP is a conserved eukaryotic ribonucleoprotein complex that plays essential roles in precursor ribosomal RNA (pre-rRNA) processing and cell cycle regulation. In contrast to ...Ribonuclease (RNase) MRP is a conserved eukaryotic ribonucleoprotein complex that plays essential roles in precursor ribosomal RNA (pre-rRNA) processing and cell cycle regulation. In contrast to RNase P, which selectively cleaves transfer RNA-like substrates, it has remained a mystery how RNase MRP recognizes its diverse substrates. To address this question, we determined cryo-electron microscopy structures of RNase MRP alone and in complex with a fragment of pre-rRNA. These structures and the results of biochemical studies reveal that coevolution of both protein and RNA subunits has transformed RNase MRP into a distinct ribonuclease that processes single-stranded RNAs by recognizing a short, loosely defined consensus sequence. This broad substrate specificity suggests that RNase MRP may have myriad yet unrecognized substrates that could play important roles in various cellular contexts. |
External links | Science / PubMed:32586950 |
Methods | EM (single particle) |
Resolution | 2.5 - 2.8 Å |
Structure data | EMDB-30296, PDB-7c79: EMDB-30297, PDB-7c7a: |
Chemicals | ChemComp-MG: ChemComp-ZN: |
Source |
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Keywords | RNA BINDING PROTEIN / Ribonuclease MRP / RNA-protein complex |