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

Research output: Contribution to journalArticle

7 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1922-1931
Number of pages10
JournalRNA
Volume17
Issue number10
DOIs
StatePublished - Oct 1 2011

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Ribonuclease P
Catalytic Domain
Binding Sites
RNA
Catalytic RNA
Ribonucleoproteins
Substrate Specificity
mitochondrial RNA-processing endoribonuclease
Eukaryota
Protein Binding
Proteins

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this

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title = "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.",
author = "Anna Perederina and Elena Khanova and Chao Quan and Igor Berezin and Esakova, {Olga A.} and Krasilnikov, {Andrey S.}",
year = "2011",
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Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP. / Perederina, Anna; Khanova, Elena; Quan, Chao; Berezin, Igor; Esakova, Olga A.; Krasilnikov, Andrey S.

In: RNA, Vol. 17, No. 10, 01.10.2011, p. 1922-1931.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP

AU - Perederina, Anna

AU - Khanova, Elena

AU - Quan, Chao

AU - Berezin, Igor

AU - Esakova, Olga A.

AU - Krasilnikov, Andrey S.

PY - 2011/10/1

Y1 - 2011/10/1

N2 - 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.

AB - 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.

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U2 - 10.1261/rna.2855511

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