Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs

Anna Perederina, Olga Esakova, Hasan Koc, Mark E. Schmitt, Andrey S. Krasilnikov

Research output: Contribution to journalArticle

33 Scopus citations

Abstract

Pop6 and Pop7 are protein subunits of Saccharomyces cerevisiae RNase MRP and RNase P. Here we show that bacterially expressed Pop6 and Pop7 form a soluble heterodimer that binds the RNA components of both RNase MRP and RNase P. Footprint analysis of the interaction between the Pop6/7 heterodimer and the RNase MRP RNA, combined with gel mobility assays, demonstrates that the Pop6/7 complex binds to a conserved region of the P3 domain. Binding of these proteins to the MRP RNA leads to local rearrangement in the structure of the P3 loop and suggests that direct interaction of the Pop6/7 complex with the P3 domain of the RNA components of RNases MRP and P may mediate binding of other protein components. These results suggest a role for a key element in the RNase MRP and RNase P RNAs in protein binding, and demonstrate the feasibility of directly studying RNA-protein interactions in the eukaryotic RNases MRP and P complexes. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)1648-1655
Number of pages8
JournalRNA
Volume13
Issue number10
DOIs
StatePublished - Oct 1 2007

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this