The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.

Corinne A Moeller-McCoy, Thomas A Wieser, Johnathan W Lubin, Abigail E Gillespie, Jocelyn A Ramirez, Margherita Paschini, Deborah S Wuttke, Victoria Lundblad

Salk Institute for Biological Studies, La Jolla, CA 92037.Salk Institute for Biological Studies, La Jolla, CA 92037. · pubmed

Paper

Abstract

In most eukaryotic organisms, cells that rely on continuous cell division employ the enzyme telomerase which replenishes chromosome termini through the addition of telomeric repeats. In budding yeast, the telomerase holoenzyme is composed of a catalytic core associated with two regulatory subunits, Est1 and Est3. The Est1 protein binds a telomere-specific RPA-like complex to recruit telomerase to chromosome ends. However, the regulatory function of the Est3 subunit has remained elusive. We report here that an interaction between Est3 and the canonical RPA complex is required for in vivo telomerase function, as revealed by mutations in

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Research summary

The paper claims that the interaction between Est3 and the canonical RPA complex is necessary for the in vivo function of telomerase in yeast. This research is relevant as it explores the mechanisms of telomerase regulation, which is crucial for understanding cellular aging and the maintenance of chromosome integrity, both of which are fundamental to longevity research.

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