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

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 RPA2 that confer an Est (Ever shorter telomeres) phenotype, characteristic of a defect in the telomerase pathway. Binding between RPA and telomerase,

SUBMITTER: Moeller-McCoy CA 

PROVIDER: S-EPMC11848354 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature