ArticleNucleic acids research2013
Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Structural and evolutionary insights into the eukaryotic RNase MRP ribonucleoprotein complex.Nature communications · 2026Article
- RNase MRP subunit composition and role in 40S ribosome biogenesis.Nature structural & molecular biology · 2026Article
- Composition and RNA binding specificity of metazoan RNase MRP.Nucleic acids research · 2025Article
- The novel pre-rRNA detection workflow "Riboprobing" allows simple identification of undescribed RNA species.RNA (New York, N.Y.) · 2024Article
- Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.Nature communications · 2020Article
- Transcriptome-wide mapping reveals widespread dynamic-regulated pseudouridylation of ncRNA and mRNA.Cell · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ribonuclease (RNase) MRP is a ubiquitous and essential site-specific eukaryotic endoribonuclease involved in the metabolism of a wide range of RNA molecules. RNase MRP is a ribonucleoprotein with a large catalytic RNA moiety that is closely related to the RNA component of RNase P, and multiple proteins, most of which are shared with RNase P. Here, we report the results of an ultraviolet-cross-linking analysis of interactions between a photoreactive RNase MRP substrate and the Saccharomyces cerevisiae RNase MRP holoenzyme. The results show that the substrate interacts with phylogenetically conserved RNA elements universally found in all enzymes of the RNase P/MRP family, as well as with a phylogenetically conserved RNA region that is unique to RNase MRP, and demonstrate that four RNase MRP protein components, all shared with RNase P, interact with the substrate. Implications for the structural organization of RNase MRP and the roles of its components are discussed.
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Registered trials
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