SGD Paper 
Perederina A, et al. (2011) Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP. RNA 17(10):1922-31
Abstract: Ribonuclease (RNase) MRP is a multicomponent ribonucleoprotein complex closely related to RNase P. RNase MRP and eukaryotic RNase P share most of their protein components, as well as multiple features of their catalytic RNA moieties, but have distinct substrate specificities. While RNase P is practically universally found in all three domains of life, RNase MRP is essential in eukaryotes. The structural organizations of eukaryotic RNase P and RNase MRP are poorly understood. Here, we show that Pop5 and Rpp1, protein components found in both RNase P and RNase MRP, form a heterodimer that binds directly to the conserved area of the putative catalytic domain of RNase MRP RNA. The Pop5/Rpp1 binding site corresponds to the protein binding site in bacterial RNase P RNA. Structural and evolutionary roles of the Pop5/Rpp1 heterodimer in RNases P and MRP are discussed.
| Status: Published | Type: Journal Article | Research Support, N.I.H., Extramural | PubMed ID: 21878546 |
Topics addressed in this paper
Number of different genes curated to this paper: 3
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| Topics | Genes linked to topics | ||
|---|---|---|---|
| NME1 | POP5 | RPP1 | |
| Additional Literature |  | ||
| DNA/RNA Sequence Features | | ||
| Non-Fungal Related Genes/Proteins | | | |
| Primary Literature | | | |
| Protein Physical Properties | | | |
| Protein Sequence Features | | | |
| Protein-Nucleic Acid Interactions | | | |
| Protein-protein Interactions | | | |
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| Techniques and Reagents | | | |
