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A Single Templating RNA in Yeast Telomerase.

Emmanuel Bajon1, Nancy Laterreur1, Raymund J Wellinger1

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Telomerase, a key enzyme for DNA replication, functions as a single unit (monomer) in yeast cells. This study reveals telomerase is a monomer both during its assembly and when actively extending telomeres.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • The composition of active telomerase ribonucleoprotein (RNP) complexes is crucial for understanding enzyme function but remains largely unknown.
  • Determining the stoichiometry of telomerase components is essential for elucidating its mechanism of action.

Purpose of the Study:

  • To determine the number of essential telomerase components within active RNPs.
  • To investigate the assembly, maturation, and functional state of telomerase in yeast cells.

Main Methods:

  • Multi-color fluorescence in situ hybridization (FISH) to detect differentially tagged TLC1 RNAs.
  • Co-immunoprecipitation assays to assess interactions between differentially tagged reverse-transcriptase subunits.
  • Probabilistic calculations and direct quantification of FISH signals.

Main Results:

  • Two differentially tagged TLC1 RNAs did not co-localize, indicating a single RNA molecule per RNP.
  • Telomerase reverse-transcriptase subunits could not be co-immunoprecipitated, suggesting a monomeric state.
  • Telomerase is assembled, matured, and exists as a monomer in yeast cells when not associated with telomeres.

Conclusions:

  • Yeast telomerase functions as a monomeric enzyme.
  • The enzyme acts as a monomer during its assembly and maturation phases.
  • Evidence suggests telomerase also functions as a monomer while elongating telomeres.