TY - JOUR
T1 - Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP
AU - Lemieux, Bruno
AU - Laterreur, Nancy
AU - Perederina, Anna
AU - Noël, Jean François
AU - Dubois, Marie Line
AU - Krasilnikov, Andrey S.
AU - Wellinger, Raymund J.
N1 - Publisher Copyright:
© 2016 Elsevier Inc.
PY - 2016/5/19
Y1 - 2016/5/19
N2 - 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.
AB - 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.
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U2 - 10.1016/j.cell.2016.04.018
DO - 10.1016/j.cell.2016.04.018
M3 - Article
C2 - 27156450
AN - SCOPUS:84964959770
SN - 0092-8674
VL - 165
SP - 1171
EP - 1181
JO - Cell
JF - Cell
IS - 5
ER -