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 and Virginia A. Zakian ()
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P. Daniela Garcia: 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: University of California
Hua Li: University of California
Sharon Aviran: University of California
Harold D. Kim: School of Physics, Georgia Institute of Technology
Virginia A. Zakian: Princeton University

Nature Communications, 2020, vol. 11, issue 1, 1-19

Abstract: Abstract RNase P and MRP are highly conserved, multi-protein/RNA complexes with essential roles in processing ribosomal and tRNAs. Three proteins found in both complexes, Pop1, Pop6, and Pop7 are also telomerase-associated. Here, we determine how temperature sensitive POP1 and POP6 alleles affect yeast telomerase. At permissive temperatures, mutant Pop1/6 have little or no effect on cell growth, global protein levels, the abundance of Est1 and Est2 (telomerase proteins), and the processing of TLC1 (telomerase RNA). However, in pop mutants, TLC1 is more abundant, telomeres are short, and TLC1 accumulates in the cytoplasm. Although Est1/2 binding to TLC1 occurs at normal levels, Est1 (and hence Est3) binding is highly unstable. We propose that Pop-mediated stabilization of Est1 binding to TLC1 is a pre-requisite for formation and nuclear localization of the telomerase holoenzyme. Furthermore, Pop proteins affect TLC1 and the RNA subunits of RNase P/MRP in very different ways.

Date: 2020
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DOI: 10.1038/s41467-020-15875-9

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