ArticleNucleic acids research2008
Multiple DNA-binding sites in Tetrahymena telomerase.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- 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
- Contributions of the TEL-patch amino acid cluster on TPP1 to telomeric DNA synthesis by human telomerase.Journal of molecular biology · 2015Article
- A self-regulating template in human telomerase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Human telomerase specialization for repeat synthesis by unique handling of primer-template duplex.The EMBO journal · 2014Article
- Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013Review
- Tracing the path of DNA substrates in active Tetrahymena telomerase holoenzyme complexes: mapping of DNA contact sites in the RNA subunit.Nucleic acids research · 2012Article
- 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
- Functional importance of telomerase pseudoknot revealed by single-molecule analysis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- 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
- Direct involvement of the TEN domain at the active site of human telomerase.Nucleic acids research · 2011Article
- Ribonucleoprotein multimers and their functions.Critical reviews in biochemistry and molecular biology · 2010Review
- InTERTpreting telomerase structure and function.Nucleic acids research · 2010Review
- Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA.Nature structural & molecular biology · 2010Article
- 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
- A single-molecule assay for telomerase structure-function analysis.Nucleic acids research · 2010Article
- Human telomerase reverse transcriptase (hTERT) Q169 is essential for telomerase function in vitro and in vivo.PloS one · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Telomerase is a ribonucleoprotein enzyme that maintains chromosome ends through de novo addition of telomeric DNA. The ability of telomerase to interact with its DNA substrate at sites outside its catalytic centre ('anchor sites') is important for its unique ability to undergo repeat addition processivity. We have developed a direct and quantitative equilibrium primer-binding assay to measure DNA-binding affinities of regions of the catalytic protein subunit of recombinant Tetrahymena telomerase (TERT). There are specific telomeric DNA-binding sites in at least four regions of TERT (the TEN, RBD, RT and C-terminal domains). Together, these sites contribute to specific and high-affinity DNA binding, with a K(d) of approximately 8 nM. Both the K(m) and K(d) increased in a stepwise manner as the primer length was reduced; thus recombinant Tetrahymena telomerase, like the endogenous enzyme, contains multiple anchor sites. The N-terminal TEN domain, which has previously been implicated in DNA binding, shows only low affinity binding. However, there appears to be cooperativity between the TEN and RNA-binding domains. Our data suggest that different DNA-binding sites are used by the enzyme during different stages of the addition cycle.
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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.