ArticleMolecular and cellular biology2007
Characterization of physical and functional anchor site interactions in human telomerase.
Article in Molecular and cellular biology, 2007. 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, 70 citations in OpenAlex.
- Telomerase reverse transcriptase degradation via a rationally designed covalent proteolysis targeting chimera.Bioorganic & medicinal chemistry letters · 2025Article
- Interaction hub critical for telomerase recruitment and primer-template handling for catalysis.Life science alliance · 2023Article
- Structural basis of human telomerase recruitment by TPP1-POT1.Science (New York, N.Y.) · 2022Article
- DNA Methylation Profiling of hTERT Gene Alongside with the Telomere Performance in Gastric Adenocarcinoma.Journal of gastrointestinal cancer · 2020Review
- Article
- 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
- A single nucleotide incorporation step limits human telomerase repeat addition activity.The EMBO journal · 2018Article
- Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase.Nucleic acids research · 2018Article
- The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids.Nucleic acids research · 2015Article
- A self-regulating template in human telomerase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Coordinated DNA dynamics during the human telomerase catalytic cycle.Nature communications · 2014Article
- Human telomerase specialization for repeat synthesis by unique handling of primer-template duplex.The EMBO journal · 2014Article
- Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase.The Plant journal : for cell and molecular biology · 2014Article
- Molecular adaptation of telomere associated genes in mammals.BMC evolutionary biology · 2013Article
- A translocation-defective telomerase with low levels of activity and processivity stabilizes short telomeres and confers immortalization.Molecular biology of the cell · 2013Article
- It all comes together at the ends: telomerase structure, function, and biogenesis.Mutation research · 2012Review
- RNA/DNA hybrid binding affinity determines telomerase template-translocation efficiency.The EMBO journal · 2012Article
- A mutation in the catalytic subunit of yeast telomerase alters primer-template alignment while promoting processivity and protein-DNA binding.Journal of cell science · 2011Article
- Human telomerase model shows the role of the TEN domain in advancing the double helix for the next polymerization step.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Telomerase is a ribonucleoprotein reverse transcriptase (RT) that processively synthesizes telomeric repeats onto the ends of linear chromosomes to maintain genomic stability. It has been proposed that the N terminus of the telomerase protein subunit, telomerase RT (TERT), contains an anchor site that forms stable interactions with DNA to prevent enzyme-DNA dissociation during translocation and to promote realignment events that accompany each round of telomere synthesis. However, it is not known whether human TERT (hTERT) can directly interact with DNA in the absence of the telomerase RNA subunit. Here we use a novel primer binding assay to establish that hTERT forms stable and specific contacts with telomeric DNA in the absence of the human telomerase RNA component (hTR). We show that hTERT-mediated primer binding can be functionally uncoupled from telomerase-mediated primer extension. Our results demonstrate that the first 350 amino acids of hTERT have a critical role in regulating the strength and specificity of protein-DNA interactions, providing additional evidence that the TERT N terminus contains an anchor site. Furthermore, we establish that the RT domain of hTERT mediates important protein-DNA interactions. Collectively, these data suggest that hTERT contains distinct anchor regions that cooperate to help regulate telomerase-mediated DNA recognition and elongation.
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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.