ArticleNucleic acids research2007
Interactions between subunits of Saccharomyces cerevisiae RNase MRP support a conserved eukaryotic RNase P/MRP architecture.
Article in Nucleic acids research, 2007. 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, 26 citations in OpenAlex.
- Post-Translational Dosage Compensation Buffers Genetic Perturbations to Stoichiometry of Protein Complexes.PLoS genetics · 2017Article
- 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
- RNase MRP RNA and RNase P activity in plants are associated with a Pop1p containing complex.Nucleic acids research · 2012Article
- Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy.Nucleic acids research · 2012Article
- 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
- GAMETOPHYTE DEFECTIVE 1, a putative subunit of RNases P/MRP, is essential for female gametogenesis and male competence in Arabidopsis.PloS one · 2012Article
- Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.RNA (New York, N.Y.) · 2011Article
- RNA binding properties of conserved protein subunits of human RNase P.Nucleic acids research · 2011Article
- Of proteins and RNA: the RNase P/MRP family.RNA (New York, N.Y.) · 2010Review
- Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a prerequisite for interaction with the P3 arm of RNase MRP RNA.Nucleic acids research · 2010Article
- Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes.RNA (New York, N.Y.) · 2008Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Ribonuclease MRP is an endonuclease, related to RNase P, which functions in eukaryotic pre-rRNA processing. In Saccharomyces cerevisiae, RNase MRP comprises an RNA subunit and ten proteins. To improve our understanding of subunit roles and enzyme architecture, we have examined protein-protein and protein-RNA interactions in vitro, complementing existing yeast two-hybrid data. In total, 31 direct protein-protein interactions were identified, each protein interacting with at least three others. Furthermore, seven proteins self-interact, four strongly, pointing to subunit multiplicity in the holoenzyme. Six protein subunits interact directly with MRP RNA and four with pre-rRNA. A comparative analysis with existing data for the yeast and human RNase P/MRP systems enables confident identification of Pop1p, Pop4p and Rpp1p as subunits that lie at the enzyme core, with probable addition of Pop5p and Pop3p. Rmp1p is confirmed as an integral subunit, presumably associating preferentially with RNase MRP, rather than RNase P, via interactions with Snm1p and MRP RNA. Snm1p and Rmp1p may act together to assist enzyme specificity, though roles in substrate binding are also indicated for Pop4p and Pop6p. The results provide further evidence of a conserved eukaryotic RNase P/MRP architecture and provide a strong basis for studies of enzyme assembly and subunit function.
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