ArticleThe Journal of biological chemistry2012
Roles of telomerase reverse transcriptase N-terminal domain in assembly and activity of Tetrahymena telomerase holoenzyme.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- The Missing Piece: Functional Telomerase Restored in the Beetle Model.Genome biology and evolution · 2026Article
- Structures of nucleotide-bound human telomerase at several steps of its telomeric DNA repeat addition cycle.Nature communications · 2026Article
- Interaction hub critical for telomerase recruitment and primer-template handling for catalysis.Life science alliance · 2023Article
- Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019Review
- Mechanisms of template handling and pseudoknot folding in human telomerase and their manipulation to expand the sequence repertoire of processive repeat synthesis.Nucleic acids research · 2018Article
- Structure of Telomerase with Telomeric DNA.Cell · 2018Article
- Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase.Nucleic acids research · 2018Article
- Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017Review
- Progress in Human and Tetrahymena Telomerase Structure Determination.Annual review of biophysics · 2017Review
- Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017Review
- Single-molecule FRET-Rosetta reveals RNA structural rearrangements during human telomerase catalysis.RNA (New York, N.Y.) · 2017Article
- Structure and folding of the Tetrahymena telomerase RNA pseudoknot.Nucleic acids research · 2017Article
- Structural conservation in the template/pseudoknot domain of vertebrate telomerase RNA from teleost fish to human.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Integrative structural biology of Tetrahymena telomerase - insights into catalytic mechanism and interaction at telomeres.The FEBS journal · 2016Review
- Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.Science (New York, N.Y.) · 2015Article
- The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids.Nucleic acids research · 2015Article
- Human telomerase specialization for repeat synthesis by unique handling of primer-template duplex.The EMBO journal · 2014Article
- Article
- Biogenesis of telomerase ribonucleoproteins.RNA (New York, N.Y.) · 2012Review
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Telomerase extends chromosome ends by the addition of single-stranded telomeric repeats. To support processive repeat synthesis, it has been proposed that coordination occurs between DNA interactions with the telomerase RNA template, the active site in the telomerase reverse transcriptase (TERT) core, a TERT N-terminal (TEN) domain, and additional subunits of the telomerase holoenzyme required for telomere elongation in vivo. The roles of TEN domain surface residues in primer binding and product elongation have been studied largely using assays of minimal recombinant telomerase enzymes, which lack holoenzyme subunits that properly fold and conformationally stabilize the ribonucleoprotein and/or control its association with telomere substrates in vivo. Here, we use Tetrahymena telomerase holoenzyme reconstitution in vitro to assess TEN domain sequence requirements in the physiological enzyme context. We find that TEN domain sequence substitutions in the Tetrahymena telomerase holoenzyme influence synthesis initiation and elongation rate but not processivity. Functional and direct physical interaction assays pinpoint a conserved TEN domain surface required for holoenzyme subunit association and for high repeat addition processivity. Our results add to the understanding of telomerase holoenzyme architecture and TERT domain functions with direct implications for the unique mechanism of single-stranded repeat synthesis.
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Registered trials
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.