ArticleEukaryotic cell2007
Mutual dependence of Candida albicans Est1p and Est3p in telomerase assembly and activation.
Article in Eukaryotic cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.Science (New York, N.Y.) · 2026Article
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- Post-Transcriptional and Post-Translational Modifications in Telomerase Biogenesis and Recruitment to Telomeres.International journal of molecular sciences · 2023Review
- Telomerase gene therapy: a remission toward cancer.Medical oncology (Northwood, London, England) · 2022Review
- Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase.Scientific reports · 2020Article
- Analysis of Yeast Telomerase by Primer Extension Assays.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Monopolin recruits condensin to organize centromere DNA and repetitive DNA sequences.Molecular biology of the cell · 2013Article
- The common ancestral core of vertebrate and fungal telomerase RNAs.Nucleic acids research · 2013Article
- A popular engagement at the ends.Nature structural & molecular biology · 2013Article
- Biogenesis of telomerase ribonucleoproteins.RNA (New York, N.Y.) · 2012Review
- Functional analysis of the single Est1/Ebs1 homologue in Kluyveromyces lactis reveals roles in both telomere maintenance and rapamycin resistance.Eukaryotic cell · 2012Article
- Schizosaccharomyces pombe Ccq1 and TER1 bind the 14-3-3-like domain of Est1, which promotes and stabilizes telomerase-telomere association.Genes & development · 2012Article
- Telomerase and retrotransposons: reverse transcriptases that shaped genomes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Stimulation of yeast telomerase activity by the ever shorter telomere 3 (Est3) subunit is dependent on direct interaction with the catalytic protein Est2.The Journal of biological chemistry · 2011Article
- The Saccharomyces cerevisiae telomerase subunit Est3 binds telomeres in a cell cycle- and Est1-dependent manner and interacts directly with Est1 in vitro.PLoS genetics · 2011Article
- The Candida albicans Ku70 modulates telomere length and structure by regulating both telomerase and recombination.PloS one · 2011Article
- Investigating the role of the Est3 protein in yeast telomere replication.Nucleic acids research · 2010Article
- Rap1 in Candida albicans: an unusual structural organization and a critical function in suppressing telomere recombination.Molecular and cellular biology · 2010Article
- Plasticity of telomere maintenance mechanisms in yeast.Trends in biochemical sciences · 2010Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Telomerase is an RNA-protein complex responsible for extending one strand of the telomere terminal repeats. Analysis of the telomerase complex in budding yeasts has revealed the presence of one catalytic protein subunit (Est2p/TERT) and at least two noncatalytic components (Est1p and Est3p). The TERT subunit is essential for telomerase catalysis, while the functions of Est1p and Est3p have not been precisely elucidated. In an earlier study, we showed that telomerase derived from a Candida est1-null mutant is defective in primer utilization in vitro; it exhibits reduced initiation and processivity on primers that terminate in two regions of the telomere repeat. Here we show that telomerase derived from a Candida est3-null mutant has nearly identical defects in primer utilization and processivity. Further analysis revealed an unexpected mutual dependence of Est1p and Est3p in their assembly into the full telomerase complex, which accounts for the similarity between the mutant enzymes. We also developed an affinity isolation and an in vitro reconstitution protocol for the telomerase complex that will facilitate future mechanistic studies.
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