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

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.

SUBMITTER: Perederina A

PROVIDER: S-EPMC3185923 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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

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

RNA (New York, N.Y.) 20110830 10

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 P ...[more]

PMID: 21878546

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