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.
journal_name
Celljournal_title
Cellauthors
Lemieux B,Laterreur N,Perederina A,Noël JF,Dubois ML,Krasilnikov AS,Wellinger RJdoi
10.1016/j.cell.2016.04.018subject
Has Abstractpub_date
2016-05-19 00:00:00pages
1171-1181issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(16)30409-3journal_volume
165pub_type
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