ArticleMolecular biology of the cell2005
An anchor site-type defect in human telomerase that disrupts telomere length maintenance and cellular immortalization.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 58 citations in OpenAlex.
- Structures of nucleotide-bound human telomerase at several steps of its telomeric DNA repeat addition cycle.Nature communications · 2026Article
- Therapeutic Targets in Telomerase and Telomere Biology of Cancers.Indian journal of clinical biochemistry : IJCB · 2020Review
- Quantitative Biology of Human Shelterin and Telomerase: Searching for the Weakest Point.International journal of molecular sciences · 2019Review
- Identification of an RNA aptamer binding hTERT-derived peptide and inhibiting telomerase activity in MCF7 cells.Molecular and cellular biochemistry · 2017Article
- Telomerase Regulation from Beginning to the End.Genes · 2016Review
- A translocation-defective telomerase with low levels of activity and processivity stabilizes short telomeres and confers immortalization.Molecular biology of the cell · 2013Article
- Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013Review
- 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
- 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
- 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
- The TPR-containing domain within Est1 homologs exhibits species-specific roles in telomerase interaction and telomere length homeostasis.BMC molecular biology · 2011Article
- Human telomerase domain interactions capture DNA for TEN domain-dependent processive elongation.Molecular cell · 2011Article
- 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
- The N-terminus of hTERT contains a DNA-binding domain and is required for telomerase activity and cellular immortalization.Nucleic acids research · 2010Article
- A novel motif in telomerase reverse transcriptase regulates telomere repeat addition rate and processivity.Nucleic acids research · 2010Article
- Multiple DNA-binding sites in Tetrahymena telomerase.Nucleic acids research · 2008Article
- Striking similarities in diverse telomerase proteins revealed by combining structure prediction and machine learning approaches.Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing · 2008Article
- Characterization of physical and functional anchor site interactions in human telomerase.Molecular and cellular biology · 2007Article
- Modeling and structure function analysis of the putative anchor site of yeast telomerase.Nucleic acids research · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Telomerase-mediated telomeric DNA synthesis is important for eukaryotic cell immortality. Telomerase adds tracts of short telomeric repeats to DNA substrates using a unique repeat addition form of processivity. It has been proposed that repeat addition processivity is partly regulated by a telomerase reverse transcriptase (TERT)-dependent anchor site; however, anchor site-mediating residues have not been identified in any TERT. We report the characterization of an N-terminal human TERT (hTERT) RNA interaction domain 1 (RID1) mutation that caused telomerase activity defects consistent with disruption of a template-proximal anchor site, including reduced processivity on short telomeric primers and reduced activity on substrates with nontelomeric 5' sequences, but not on primers with nontelomeric G-rich 5' sequences. This mutation was located within a subregion of RID1 previously implicated in biological telomerase functions unrelated to catalytic activity (N-DAT domain). Other N-DAT and C-terminal DAT (C-DAT) mutants and a C-terminally tagged hTERT-HA variant were defective in elongating short telomeric primers, and catalytic phenotypes of DAT variants were partially or completely rescued by increasing concentrations of DNA primers. These observations imply that RID1 and the hTERT C terminus contribute to telomerase's affinity for its substrate, and that RID1 may form part of the human telomerase anchor site.
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Registered trials
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