ArticleThe Journal of biological chemistry2012
Global identification of new substrates for the yeast endoribonuclease, RNase mitochondrial RNA processing (MRP).
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Structural and evolutionary insights into the eukaryotic RNase MRP ribonucleoprotein complex.Nature communications · 2026Article
- Composition and RNA binding specificity of metazoan RNase MRP.Nucleic acids research · 2025Article
- Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components.Cell reports · 2025Article
- Coevolution of RNA and protein subunits in RNase P and RNase MRP, two RNA processing enzymes.The Journal of biological chemistry · 2024Review
- Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.Nature communications · 2020Article
- A cell separation checkpoint that enforces the proper order of late cytokinetic events.The Journal of cell biology · 2019Article
- Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.RNA (New York, N.Y.) · 2015Article
- Article
- Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.Nucleic acids research · 2013Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
RNase mitochondrial RNA processing (MRP) is an essential, evolutionarily conserved endoribonuclease composed of 10 different protein subunits and a single RNA. RNase MRP has established roles in multiple pathways including ribosome biogenesis, cell cycle regulation, and mitochondrial DNA replication. Although each of these functions is important to cell growth, additional functions may exist given the essential nature of the complex. To identify novel RNase MRP substrates, we utilized RNA immunoprecipitation and microarray chip analysis to identify RNA that physically associates with RNase MRP. We identified several new potential substrates for RNase MRP including a cell cycle-regulated transcript, CTS1; the yeast homolog of the mammalian p27(Kip1), SIC1; and the U2 RNA component of the spliceosome. In addition, we found RNase MRP to be involved in the regulation of the Ty1 transposon RNA. These results reinforce and broaden the role of RNase MRP in cell cycle regulation and help to identify new roles of this endoribonuclease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.