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Reference: Perederina A, et al. (2011) Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP. RNA 17(10):1922-31

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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.

Reference Type
Journal Article | Research Support, N.I.H., Extramural
Authors
Perederina A, Khanova E, Quan C, Berezin I, Esakova O, Krasilnikov AS
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