ArticleProceedings of the National Academy of Sciences of the United States of America2025
The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Fission yeast RPA-TERT-Tpz1TPP1 complex promotes telomere extension and suppresses telomere recombination.PLoS genetics · 2026Article
- Fission yeast RPA-TERT-Tpz1bioRxiv : the preprint server for biology · 2026Article
- Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.Science (New York, N.Y.) · 2026Article
- 3,6'-Disinapoyl Sucrose fromAntioxidants (Basel, Switzerland) · 2026Article
- Human RPA is an essential telomerase processivity factor for maintaining telomeres.Science (New York, N.Y.) · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
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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