Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP

Bruno Lemieux, Nancy Laterreur, Anna Perederina, Jean François Noël, Marie Line Dubois, Andrey S. Krasilnikov, Raymund J. Wellinger

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

Telomerase is the ribonucleoprotein enzyme that replenishes telomeric DNA and maintains genome integrity. Minimally, telomerase activity requires a templating RNA and a catalytic protein. Additional proteins are required for activity on telomeres in vivo. Here, we report that the Pop1, Pop6, and Pop7 proteins, known components of RNase P and RNase MRP, bind to yeast telomerase RNA and are essential constituents of the telomerase holoenzyme. Pop1/Pop6/Pop7 binding is specific and involves an RNA domain highly similar to a protein-binding domain in the RNAs of RNase P/MRP. The results also show that Pop1/Pop6/Pop7 function to maintain the essential components Est1 and Est2 on the RNA in vivo. Consistently, addition of Pop1 allows for telomerase activity reconstitution with wild-Type telomerase RNA in vitro. Thus, the same chaperoning module has allowed the evolution of functionally and, remarkably, structurally distinct RNPs, telomerase, and RNases P/MRP from unrelated progenitor RNAs.

Original languageEnglish (US)
Pages (from-to)1171-1181
Number of pages11
JournalCell
Volume165
Issue number5
DOIs
StatePublished - May 19 2016

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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