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

TitleStability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP.
Publication TypeJournal Article
Year of Publication2020
AuthorsP Garcia, D, Leach, RW, Wadsworth, GM, Choudhary, K, Li, H, Aviran, S, Kim, HD, Zakian, VA
JournalNat Commun
Date Published2020 May 01
KeywordsCell Nucleus, DNA-Binding Proteins, Methylation, Protein Binding, Ribonuclease P, Ribonucleoproteins, RNA, RNA 3' End Processing, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Telomerase, Telomere

<p>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.</p>

Alternate JournalNat Commun
PubMed ID32358529
PubMed Central IDPMC7195438
Grant ListR01 GM112882 / GM / NIGMS NIH HHS / United States