ArticleNucleic acids research2004
Yeast telomerase is capable of limited repeat addition processivity.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.Science (New York, N.Y.) · 2026Article
- Molecular and Evolutionary Analysis of RNA-Protein Interactions in Telomerase Regulation.Non-coding RNA · 2024Review
- Crystal structures of N-terminally truncated telomerase reverse transcriptase from fungi‡.Nucleic acids research · 2021Article
- The Biochemical Activities of theGenes · 2019Article
- TheThe Journal of biological chemistry · 2018Article
- Rnr1, but not Rnr3, facilitates the sustained telomerase-dependent elongation of telomeres.PLoS genetics · 2017Article
- Analysis of Yeast Telomerase by Primer Extension Assays.Methods in molecular biology (Clifton, N.J.) · 2017Article
- TeloPCR-seq: a high-throughput sequencing approach for telomeres.FEBS letters · 2016Article
- Physical Connectivity Mapping by Circular Permutation of Human Telomerase RNA Reveals New Regions Critical for Activity and Processivity.Molecular and cellular biology · 2016Article
- Article
- Cdc13 at a crossroads of telomerase action.Frontiers in oncology · 2013Article
- Telomere lengthening and other functions of telomerase.Acta naturae · 2012Article
- A novel motif in telomerase reverse transcriptase regulates telomere repeat addition rate and processivity.Nucleic acids research · 2010Article
- The N-terminus of hTERT contains a DNA-binding domain and is required for telomerase activity and cellular immortalization.Nucleic acids research · 2010Article
- Evidence for an additional base-pairing element between the telomeric repeat and the telomerase RNA template in Kluyveromyces lactis and other yeasts.Molecular and cellular biology · 2009Article
- Modeling and structure function analysis of the putative anchor site of yeast telomerase.Nucleic acids research · 2007Article
- A physical and functional constituent of telomerase anchor site.The Journal of biological chemistry · 2005Article
- Telomerase can act as a template- and RNA-independent terminal transferase.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Functional organization of repeat addition processivity and DNA synthesis determinants in the human telomerase multimer.Molecular and cellular biology · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Telomerase is a ribonucleoprotein reverse transcriptase responsible for the maintenance of one strand of telomere terminal repeats. Telomerase-mediated sequence addition is dictated by a short 'template' region of the RNA component. Despite the short template segment, telomerases from many organisms have been shown to mediate the synthesis of long extension products. This synthesis presumably depends on two types of translocation events: simultaneous translocation of the RNA-DNA duplex relative to the active site after each nucleotide incorporation (type I or nucleotide addition processivity), and translocation of the RNA relative to the DNA product after each round of repeat synthesis (type II or repeat addition processivity). In contrast, telomerases from yeasts have been shown to synthesize mostly short products, implying a defect in one or both types of translocation. In this report, we analyzed the processivity of yeast telomerase in vitro, and identified two position-specific elongation barriers within the 5' region of the RNA template that can account for the synthesis of incomplete first round products. These barriers respond differently to variations in nucleotide concentration, primer sequence and mutations in the catalytic protein subunit, consistent with their having distinct mechanistic bases. In addition, by using optimal primers and high concentrations of dGTP, we were able to detect significant type II translocation by the yeast enzyme. Thus, the difference between the elongation property of yeast and other telomerases appears to be quantitative rather than qualitative. Our results suggest that yeast may be a useful system for investigating the physiologic significance of repeat addition processivity.
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