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


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.

SUBMITTER: Lemieux B 

PROVIDER: S-EPMC4874874 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature

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

Lemieux Bruno B   Laterreur Nancy N   Perederina Anna A   Noël Jean-François JF   Dubois Marie-Line ML   Krasilnikov Andrey S AS   Wellinger Raymund J RJ  

Cell 20160505 5


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  ...[more]

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