ArticleMolecular and cellular biology2004
Functional organization of repeat addition processivity and DNA synthesis determinants in the human telomerase multimer.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 113 citations in OpenAlex.
- Structures of nucleotide-bound human telomerase at several steps of its telomeric DNA repeat addition cycle.Nature communications · 2026Article
- Recent progress in human telomerase structure and its therapeutic targeting.Frontiers in molecular biosciences · 2025Review
- Many Functions of Telomerase Components: Certainties, Doubts, and Inconsistencies.International journal of molecular sciences · 2022Review
- Structural biology of human telomerase: progress and prospects.Biochemical Society transactions · 2021Review
- Composition and Function of Telomerase-A Polymerase Associated with the Origin of Eukaryotes.Biomolecules · 2020Review
- Single-Molecule Analysis of Reverse Transcriptase Enzymes.Cold Spring Harbor perspectives in biology · 2019Review
- Direct observation of nucleic acid binding dynamics by the telomerase essential N-terminal domain.Nucleic acids research · 2018Article
- Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo.Protoplasma · 2017Article
- The protein subunit of telomerase displays patterns of dynamic evolution and conservation across different metazoan taxa.BMC evolutionary biology · 2017Article
- Telomerase Regulation from Beginning to the End.Genes · 2016Review
- Evolutionary perspectives of telomerase RNA structure and function.RNA biology · 2016Review
- Article
- Chimeric bifunctional oligonucleotides as a novel tool to invade telomerase assembly.Nucleic acids research · 2014Article
- Human telomerase specialization for repeat synthesis by unique handling of primer-template duplex.The EMBO journal · 2014Article
- Single-molecule fluorescence resonance energy transfer studies of the human telomerase RNA pseudoknot: temperature-/urea-dependent folding kinetics and thermodynamics.The journal of physical chemistry. B · 2014Article
- A translocation-defective telomerase with low levels of activity and processivity stabilizes short telomeres and confers immortalization.Molecular biology of the cell · 2013Article
- Identification of telomerase RNAs from filamentous fungi reveals conservation with vertebrates and yeasts.PloS one · 2013Article
- The human telomerase catalytic subunit and viral telomerase RNA reconstitute a functional telomerase complex in a cell-free system, but not in human cells.Cellular & molecular biology letters · 2012Article
- It all comes together at the ends: telomerase structure, function, and biogenesis.Mutation research · 2012Review
- Telomerase and telomere-associated proteins: structural insights into mechanism and evolution.Structure (London, England : 1993) · 2012Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Human telomerase is a multimer containing two human telomerase RNAs (hTRs) and most likely two human telomerase reverse transcriptases (hTERTs). Telomerase synthesizes multiple telomeric repeats using a unique repeat addition form of processivity. We investigated hTR and hTERT sequences that were essential for DNA synthesis and processivity using a direct primer extension telomerase assay. We found that hTERT consists of two physically separable functional domains, a polymerase domain containing RNA interaction domain 2 (RID2), reverse transcriptase (RT), and C-terminal sequences, and a major accessory domain, RNA interaction domain 1 (RID1). RID2 mutants defective in high-affinity hTR interactions and an RT catalytic mutant exhibited comparable DNA synthesis defects. The RID2-interacting hTR P6.1 helix was also essential for DNA synthesis. RID1 interacted with the hTR pseudoknot-template domain and hTERT's RT motifs and putative thumb and was essential for processivity, but not DNA synthesis. The hTR pseudoknot was essential for processivity, but not DNA synthesis, and processivity was reduced or abolished in dimerization-defective pseudoknot mutants. trans-acting hTERTs and hTRs complemented the processivity defects of RID1 and pseudoknot mutants, respectively. These data provide novel insight into the catalytic organization of the human telomerase complex and suggest that repeat addition processivity is one of the major catalytic properties conferred by telomerase multimerization.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.