ArticleThe Journal of biological chemistry2011
Single molecule studies of physiologically relevant telomeric tails reveal POT1 mechanism for promoting G-quadruplex unfolding.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 102 citations in OpenAlex.
- Polymeric Properties of Telomeric G-Quadruplex Multimers: Effects of Chemically Inert Crowders.Biomacromolecules · 2025Article
- Canonical and non-canonical functions of the non-coding RNA component (TERC) of telomerase complex.Cell & bioscience · 2025Review
- Article
- BG4 antibody can recognize telomeric G-quadruplexes harboring destabilizing base modifications and lesions.Nucleic acids research · 2024Article
- Structure, Topology, and Stability of Multiple G-quadruplexes in Long Telomeric Overhangs.Journal of molecular biology · 2024Review
- G-Quadruplexes in Human Telomere: Structures, Properties, and Applications.Molecules (Basel, Switzerland) · 2023Review
- RPA engages telomeric G-quadruplexes more effectively than CST.Nucleic acids research · 2023Article
- Shelterin reduces the accessibility of telomeric overhangs.Nucleic acids research · 2022Article
- Dynamic folding and accessibility of telomeric overhang.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Targeting telomeres: advances in telomere maintenance mechanism-specific cancer therapies.Nature reviews. Cancer · 2022Review
- DNA-RNA hybrid G-quadruplex tends to form near the 3' end of telomere overhang.Biophysical journal · 2022Article
- Emerging accessibility patterns in long telomeric overhangs.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- TIN2 is an architectural protein that facilitates TRF2-mediated trans- and cis-interactions on telomeric DNA.Nucleic acids research · 2021Article
- TRF2 promotes dynamic and stepwise looping of POT1 bound telomeric overhang.Nucleic acids research · 2021Article
- Multiple hPOT1-TPP1 cooperatively unfold contiguous telomeric G-quadruplexes proceeding from 3' toward 5', a feature due to a 3'-end binding preference and to structuring of telomeric DNA.Nucleic acids research · 2021Article
- Interrogating accessibility of telomeric sequences with FRET-PAINT: evidence for length-dependent telomere compaction.Nucleic acids research · 2021Article
- Frustrated folding of guanine quadruplexes in telomeric DNA.Nucleic acids research · 2021Article
- Active and Passive Destabilization of G-Quadruplex DNA by the Telomere POT1-TPP1 Complex.Journal of molecular biology · 2021Article
- Shaping human telomeres: from shelterin and CST complexes to telomeric chromatin organization.Nature reviews. Molecular cell biology · 2021Review
- Parallel reaction pathways accelerate folding of a guanine quadruplex.Nucleic acids research · 2021Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Human telomeres are composed of duplex TTAGGG repeats and a 3' single-stranded DNA tail. The telomeric DNA is protected and regulated by the shelterin proteins, including the protection of telomeres 1 (POT1) protein that binds telomeric single-stranded DNA. The single-stranded tail can fold into G-quadruplex (G4) DNA. Both POT1 and G4 DNA play important roles in regulating telomere length homeostasis. To date, most studies have focused on individual quadruplexes formed by four TTAGGG repeats. Telomeric tails in human cells have on average six times as many repeats, and no structural studies have examined POT1 binding in competition with G4 DNA folding. Using single molecule atomic force microscopy imaging, we observed that the majority of the telomeric tails of 16 repeats formed two quadruplexes even though four were possible. The result that physiological telomeric tails rarely form the maximum potential number of G4 units provides a structural basis for the coexistence of G4 and POT1 on the same DNA molecule, which is observed directly in the captured atomic force microscopy images. We further observed that POT1 is significantly more effective in disrupting quadruplex DNA on long telomeric tails than an antisense oligonucleotide, indicating a novel POT1 activity beyond simply preventing quadruplex folding.
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