ArticleNucleic acids research2018
Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Structures of nucleotide-bound human telomerase at several steps of its telomeric DNA repeat addition cycle.Nature communications · 2026Article
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- Article
- Crystal structures of N-terminally truncated telomerase reverse transcriptase from fungi‡.Nucleic acids research · 2021Article
- A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase.Scientific reports · 2020Article
- Human Telomerase RNA: Telomerase Component or More?Biomolecules · 2020Review
- Article
- Structural biology of telomeres and telomerase.Cellular and molecular life sciences : CMLS · 2020Review
- Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019Review
- Circular RNAs in Cancer: emerging functions in hallmarks, stemness, resistance and roles as potential biomarkers.Molecular cancer · 2019Review
- Telomerase structures and regulation: shedding light on the chromosome end.Current opinion in structural 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
- Article
- Direct observation of nucleic acid binding dynamics by the telomerase essential N-terminal domain.Nucleic acids research · 2018Article
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Authors and funding
16 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The elongation of single-stranded DNA repeats at the 3'-ends of chromosomes by telomerase is a key process in maintaining genome integrity in eukaryotes. Abnormal activation of telomerase leads to uncontrolled cell division, whereas its down-regulation is attributed to ageing and several pathologies related to early cell death. Telomerase function is based on the dynamic interactions of its catalytic subunit (TERT) with nucleic acids-telomerase RNA, telomeric DNA and the DNA/RNA heteroduplex. Here, we present the crystallographic and NMR structures of the N-terminal (TEN) domain of TERT from the thermotolerant yeast Hansenula polymorpha and demonstrate the structural conservation of the core motif in evolutionarily divergent organisms. We identify the TEN residues that are involved in interactions with the telomerase RNA and in the recognition of the 'fork' at the distal end of the DNA product/RNA template heteroduplex. We propose that the TEN domain assists telomerase biological function and is involved in restricting the size of the heteroduplex during telomere repeat synthesis.
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