Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP

P. Daniela Garcia; Robert W. Leach; Gable M. Wadsworth; Krishna Choudhary; Hua Li; Sharon Aviran; Harold D. Kim; Virginia A. Zakian

doi:10.1038/s41467-020-15875-9

Nature Communications (May 2020)

Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP

P. Daniela Garcia,
Robert W. Leach,
Gable M. Wadsworth,
Krishna Choudhary,
Hua Li,
Sharon Aviran,
Harold D. Kim,
Virginia A. Zakian

Affiliations

P. Daniela Garcia: Department of Molecular Biology, Princeton University
Robert W. Leach: Bioinformatics Group, Genomics Core Facility, Carl Icahn Laboratory, Princeton University
Gable M. Wadsworth: School of Physics, Georgia Institute of Technology
Krishna Choudhary: Department of Biomedical Engineering and Genome Center, University of California
Hua Li: Department of Biomedical Engineering and Genome Center, University of California
Sharon Aviran: Department of Biomedical Engineering and Genome Center, University of California
Harold D. Kim: School of Physics, Georgia Institute of Technology
Virginia A. Zakian: Department of Molecular Biology, Princeton University

DOI: https://doi.org/10.1038/s41467-020-15875-9
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 19

Abstract

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Pop1 and 6 are subunits of RNase P and RNase MRP, which process ribosomal and tRNAs. The authors show that when Pop1 and 6 are impaired, the telomerase subunit Est1 binds telomerase RNA at normal levels, but the binding is unstable. As a result, nuclear import of the telomerase holoenzyme is inhibited.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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