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

Research paper by Anna A Perederina, Elena E Khanova, Chao C Quan, Igor I Berezin, Olga O Esakova, Andrey S AS Krasilnikov

Indexed on: 01 Sep '11Published on: 01 Sep '11Published in: RNA (New York, N.Y.)



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.