ArticleProceedings of the National Academy of Sciences of the United States of America2007
High-resolution physical and functional mapping of the template adjacent DNA binding site in catalytically active telomerase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed, 42 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
- 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
- Structural basis of template-boundary definition in Tetrahymena telomerase.Nature structural & molecular biology · 2015Article
- The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids.Nucleic acids research · 2015Article
- 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
- A translocation-defective telomerase with low levels of activity and processivity stabilizes short telomeres and confers immortalization.Molecular biology of the cell · 2013Article
- Article
- 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
- Roles of telomerase reverse transcriptase N-terminal domain in assembly and activity of Tetrahymena telomerase holoenzyme.The Journal of biological chemistry · 2012Article
- Exclusion of exon 2 is a common mRNA splice variant of primate telomerase reverse transcriptases.PloS one · 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 domain interactions capture DNA for TEN domain-dependent processive elongation.Molecular cell · 2011Article
- Telomerase: an RNP enzyme synthesizes DNA.Cold Spring Harbor perspectives in biology · 2011Review
- Direct involvement of the TEN domain at the active site of human telomerase.Nucleic acids research · 2011Article
- InTERTpreting telomerase structure and function.Nucleic acids research · 2010Review
- Multiple mechanisms for elongation processivity within the reconstituted tetrahymena telomerase holoenzyme.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Telomerase is a cellular reverse transcriptase, which utilizes an integral RNA template to extend single-stranded telomeric DNA. We used site-specific photocrosslinking to map interactions between DNA primers and the catalytic protein subunit (tTERT) of Tetrahymena thermophila telomerase in functional enzyme complexes. Our assays reveal contact of the single-stranded DNA adjacent to the primer-template hybrid and tTERT residue W187 at the periphery of the N-terminal domain. This contact was detected in complexes with three different registers of template in the active site, suggesting that it is maintained throughout synthesis of a complete telomeric repeat. Substitution of nearby residue Q168, but not W187, alters the K(m) for primer elongation, implying that it plays a role in the DNA recognition. These findings are the first to directly demonstrate the physical location of TERT-DNA contacts in catalytically active telomerase and to identify amino acid determinants of DNA binding affinity. Our data also suggest a movement of the TERT active site relative to the template-adjacent single-stranded DNA binding site within a cycle of 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.