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

Author

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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
    Gladstone Institute of Data Science and Biotechnology)

  • 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)

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.

Suggested Citation

  • P. Daniela Garcia & Robert W. Leach & Gable M. Wadsworth & Krishna Choudhary & Hua Li & Sharon Aviran & Harold D. Kim & Virginia A. Zakian, 2020. "Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP," Nature Communications, Nature, vol. 11(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15875-9
    DOI: 10.1038/s41467-020-15875-9
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    Cited by:

    1. Jennifer Porat & Moaine El Baidouri & Jorg Grigull & Jean-Marc Deragon & Mark A. Bayfield, 2022. "The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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