Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP

Anna Perederina, Elena Khanova, Chao Quan, Igor Berezin, Olga Esakova, Andrey S. Krasilnikov

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1922-1931
Number of pages10
Issue number10
StatePublished - Oct 2011

All Science Journal Classification (ASJC) codes

  • Molecular Biology


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