ArticleThe Journal of biological chemistry2010
Multiple mechanisms for elongation processivity within the reconstituted tetrahymena telomerase holoenzyme.
Article in The Journal of biological chemistry, 2010. 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, 43 citations in OpenAlex.
- La1: an evolutionarily conserved player in the Arabidopsis telomerase complex.Plant cell reports · 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
- RPA-like single-stranded DNA-binding protein complexes including CST serve as specialized processivity factors for polymerases.Current opinion in structural biology · 2023Review
- Telomerase structural biology comes of age.Current opinion in structural biology · 2022Review
- Structural Characterization of the Helicase nsp10 Encoded by Porcine Reproductive and Respiratory Syndrome Virus.Journal of virology · 2020Article
- Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019Review
- Telomere DNA G-quadruplex folding within actively extending human telomerase.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity.Journal of virology · 2018Article
- Evolutionary rates of mammalian telomere-stability genes correlate with karyotype features and female germline expression.Nucleic acids research · 2018Article
- Current Perspectives of Telomerase Structure and Function in Eukaryotes with Emerging Views on Telomerase in Human Parasites.International journal of molecular sciences · 2018Review
- Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017Review
- Shared Subunits of Tetrahymena Telomerase Holoenzyme and Replication Protein A Have Different Functions in Different Cellular Complexes.The Journal of biological chemistry · 2017Article
- Evolution of Arabidopsis protection of telomeres 1 alters nucleic acid recognition and telomerase regulation.Nucleic acids research · 2016Article
- Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.Science (New York, N.Y.) · 2015Article
- Human telomerase: biogenesis, trafficking, recruitment, and activation.Genes & development · 2015Review
- Direct single-stranded DNA binding by Teb1 mediates the recruitment of Tetrahymena thermophila telomerase to telomeres.Molecular and cellular biology · 2014Article
- The 3' overhangs at Tetrahymena thermophila telomeres are packaged by four proteins, Pot1a, Tpt1, Pat1, and Pat2.Eukaryotic cell · 2014Article
- Progress in structural studies of telomerase.Current opinion in structural biology · 2014Review
- Tetrahymena telomerase holoenzyme assembly, activation, and inhibition by domains of the p50 central hub.Molecular and cellular biology · 2013Article
- Single-stranded DNA-binding proteins: multiple domains for multiple functions.Structure (London, England : 1993) · 2013Review
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
To maintain telomeres, telomerase evolved a unique biochemical activity: the use of a single-stranded RNA template for the synthesis of single-stranded DNA repeats. High repeat addition processivity (RAP) of the Tetrahymena telomerase holoenzyme requires association of the catalytic core with the telomere adaptor subcomplex (TASC) and an RPA1-related subunit (p82 or Teb1). Here, we used DNA binding and holoenzyme reconstitution assays to investigate the mechanism by which Teb1 and TASC confer high RAP. We show that TASC association with the recombinant telomerase catalytic core increases enzyme activity. Subsequent association of the Teb1 C-terminal domain with TASC confers the capacity for high RAP even though the Teb1 C-terminal domain does not provide a high-affinity DNA interaction site. Efficient RAP also requires suppression of nascent product folding mediated by the central Teb1 DNA-binding domains (DBDs). These sequence-specific high-affinity DBDs of Teb1 can be functionally substituted by the analogous DBDs of Tetrahymena Rpa1 to suppress nascent product folding but only if the Rpa1 high-affinity DBDs are physically tethered into holoenzyme context though the Teb1 C-terminal domain. Overall, our findings reveal multiple mechanisms and multiple surfaces of protein-DNA and protein-protein interaction that give rise to elongation processivity in the synthesis of a single-stranded nucleic acid product.
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