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 - Funding Information:
We thank S. Benjira for help during project setup, D. Engelke, V. Lundblad, M. Schmitt, and D. Zappulla for valuable tools such as numerous yeast strains and plasmids, I. Berezin for help with protein purification, and members of the R.J.W. lab for input. We also thank F.-M. Boisvert for use of his MS facility. This work was supported by a grant from the Canadian Institutes of Health Research (CIHR 97874) (to R.J.W.) and the Canadian Research Chair in Telomere Biology and support by the CRCHUS (to R.J.W.). A.S.K. was supported by an NIH grant (GM085149).
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 -