ArticlePLoS genetics2011
The Saccharomyces cerevisiae telomerase subunit Est3 binds telomeres in a cell cycle- and Est1-dependent manner and interacts directly with Est1 in vitro.
Article in PLoS genetics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 58 citations in OpenAlex.
- Genomic Landscape Underlying Biofilm Formation Diversity in Nakaseomyces glabratus Clinical Isolates.MicrobiologyOpen · 2026Article
- Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.Science (New York, N.Y.) · 2026Article
- The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Post-Transcriptional and Post-Translational Modifications in Telomerase Biogenesis and Recruitment to Telomeres.International journal of molecular sciences · 2023Review
- Set1 regulates telomere function via H3K4 methylation-dependent and -independent pathways and calibrates the abundance of telomere maintenance factors.Molecular biology of the cell · 2023Article
- Telomerase subunit Est2 marks internal sites that are prone to accumulate DNA damage.BMC biology · 2021Article
- Swc4 positively regulates telomere length independently of its roles in NuA4 and SWR1 complexes.Nucleic acids research · 2020Article
- Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase.Scientific reports · 2020Article
- Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP.Nature communications · 2020Article
- Loss of Ku's DNA end binding activity affects telomere length via destabilizing telomere-bound Est1 rather than altering TLC1 homeostasis.Scientific reports · 2019Article
- Fundamental mechanisms of telomerase action in yeasts and mammals: understanding telomeres and telomerase in cancer cells.Open biology · 2017Review
- Modulation of yeast telomerase activity by Cdc13 and Est1 in vitro.Scientific reports · 2016Article
- Proteomics of yeast telomerase identified Cdc48-Npl4-Ufd1 and Ufd4 as regulators of Est1 and telomere length.Nature communications · 2015Article
- A second essential function of the Est1-binding arm of yeast telomerase RNA.RNA (New York, N.Y.) · 2015Article
- The pif1 helicase, a negative regulator of telomerase, acts preferentially at long telomeres.PLoS genetics · 2015Article
- 21st Century Genetics: Mass Spectrometry of Yeast Telomerase.Cold Spring Harbor symposia on quantitative biology · 2015Article
- Regulated assembly and disassembly of the yeast telomerase quaternary complex.Genes & development · 2014Article
- The principal role of Ku in telomere length maintenance is promotion of Est1 association with telomeres.Genetics · 2014Article
- Normal telomere length maintenance in Saccharomyces cerevisiae requires nuclear import of the ever shorter telomeres 1 (Est1) protein via the importin alpha pathway.Eukaryotic cell · 2014Article
- Genome-wide studies of telomere biology in budding yeast.Microbial cell (Graz, Austria) · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Telomerase is a telomere dedicated reverse transcriptase that replicates the very ends of eukaryotic chromosomes. Saccharomyces cerevisiae telomerase consists of TLC1 (the RNA template), Est2 (the catalytic subunit), and two accessory proteins, Est1 and Est3, that are essential in vivo for telomerase activity but are dispensable for catalysis in vitro. Est1 functions in both recruitment and activation of telomerase. The association of Est3 with telomeres occurred largely in late S/G2 phase, the time when telomerase acts and Est1 telomere binding occurs. Est3 telomere binding was Est1-dependent. This dependence is likely due to a direct interaction between the two proteins, as purified recombinant Est1 and Est3 interacted in vitro. Est3 abundance was neither cell cycle-regulated nor Est1-dependent. Est3 was the most abundant of the three Est proteins (84.3±13.3 molecules per cell versus 71.1±19.2 for Est1 and 37.2±6.5 for Est2), so its telomere association and/or activity is unlikely to be limited by its relative abundance. Est2 and Est1 telomere binding was unaffected by the absence of Est3. Taken together, these data indicate that Est3 acts downstream of both Est2 and Est1 and that the putative activation function of Est1 can be explained by its role in recruiting Est3 to telomeres.
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