ArticleRNA biology
The P3 domain of eukaryotic RNases P/MRP: making a protein-rich RNA-based enzyme.
Article in RNA biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- Anti-Th/To Antibodies in Scleroderma: Good Prognosis or Serious Concern?Journal of clinical medicine · 2024Review
- The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021Review
- In vitro reconstitution and analysis of eukaryotic RNase P RNPs.Nucleic acids research · 2018Article
- Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding.Journal of molecular biology · 2018Article
- 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
- Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.Nucleic acids research · 2013Article
- Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions.RNA (New York, N.Y.) · 2012Article
- Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy.Nucleic acids research · 2012Article
- Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.RNA (New York, N.Y.) · 2011Article
- Archaeal/eukaryal RNase P: subunits, functions and RNA diversification.Nucleic acids research · 2010Review
- The Pol III transcriptome: Basic features, recurrent patterns, and emerging roles in cancer.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Nuclear Ribonuclease (RNase) P is a universal essential RNA-based enzyme made of a catalytic RNA component and a protein part; eukaryotic RNase P is closely related to a universal eukaryotic ribonucleoprotein RNase MRP. The protein part of the eukaryotic RNases P/MRP is dramatically more complex than that in bacterial and archaeal RNases P. The increase in the complexity of the protein part in eukaryotic RNases P/MRP was accompanied by the appearance of a novel structural element in the RNA component: an essential and phylogenetically conserved helix-loop-helix P3 RNA domain. The crystal structure of the P3 RNA domain in a complex with protein components Pop6 and Pop7 has been recently solved. Here we discuss the most salient structural features of the P3 domain as well as its possible role in the evolutionary transition to the protein-rich eukaryotic RNases P/MRP.
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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.