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TitleStructural insight into precursor ribosomal RNA processing by ribonuclease MRP.
Journal, issue, pagesScience, Vol. 369, Issue 6504, Page 656-663, Year 2020
Publish dateAug 7, 2020
AuthorsPengfei Lan / Bin Zhou / Ming Tan / Shaobai Li / Mi Cao / Jian Wu / Ming Lei /
PubMed AbstractRibonuclease (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 linksScience / PubMed:32586950
MethodsEM (single particle)
Resolution2.5 - 2.8 Å
Structure data

EMDB-30296, PDB-7c79:
Cryo-EM structure of yeast Ribonuclease MRP
Method: EM (single particle) / Resolution: 2.5 Å

EMDB-30297, PDB-7c7a:
Cryo-EM structure of yeast Ribonuclease MRP with substrate ITS1
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae s288c (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsRNA BINDING PROTEIN / Ribonuclease MRP / RNA-protein complex

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