ArticleProceedings of the National Academy of Sciences of the United States of America2005
Human POT1 disrupts telomeric G-quadruplexes allowing telomerase extension in vitro.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 188 papers.
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Who cites it
188 citing papers in PubMed, 384 citations in OpenAlex.
- How telomere attrition protects against cancer.Nature reviews. Genetics · 2026Review
- BRIP1, a G-quadruplex DNA helicase, protects against AID-induced genomic instability by limiting R-loop accumulation.Molecular medicine (Cambridge, Mass.) · 2026Article
- Telomere length of both parents contributes to heritable POT1 cancer-predisposition syndrome.Nature communications · 2026Article
- Telomere length of both parents contribute to heritable POT1 cancer-predisposition syndrome.bioRxiv : the preprint server for biology · 2026Article
- Indirect identification of genomic G-quadruplexes via a small protein probe that specifically recognizes C-rich single-stranded DNA.Nucleic acids research · 2026Article
- Evidence that G-quadruplexes form in pathogenic fungi and represent promising antifungal targets.EMBO molecular medicine · 2025Article
- Impact of Molecular Crowding on Accessibility of Telomeric Overhangs Forming Multiple G-Quadruplexes.Biomacromolecules · 2025Article
- Twisting tetraplex DNA: A strand dynamics regulating i-motif function in diverse molecular crowding environments.Nucleic acids research · 2025Article
- Impact of Molecular Crowding on Accessibility of Telomeric Overhangs Forming Multiple G-quadruplexes.bioRxiv : the preprint server for biology · 2025Article
- Rapid dynamics allow the low-abundance RTEL1 helicase to promote telomere replication.Nucleic acids research · 2025Article
- Neurological Diseases can be Regulated by Phase Separation.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Small molecule telomerase inhibitors are also potent inhibitors of telomeric C-strand synthesis.RNA (New York, N.Y.) · 2024Article
- A Phenotypic Approach to the Discovery of Potent G-Quadruplex Targeted Drugs.Molecules (Basel, Switzerland) · 2024Review
- Structural Motifs at the Telomeres and Their Role in Regulatory Pathways.Biochemistry · 2024Review
- Guardians of the Genome: How the Single-Stranded DNA-Binding Proteins RPA and CST Facilitate Telomere Replication.Biomolecules · 2024Review
- G-Quadruplexes in Human Telomere: Structures, Properties, and Applications.Molecules (Basel, Switzerland) · 2023Review
- Telomeric i-motifs and C-strands inhibit parallel G-quadruplex extension by telomerase.Nucleic acids research · 2023Article
- Pot1b -/- tumors activate G-quadruplex-induced DNA damage to promote telomere hyper-elongation.Nucleic acids research · 2023Article
- RPA engages telomeric G-quadruplexes more effectively than CST.Nucleic acids research · 2023Article
- Co-evolution of large inverted repeats and G-quadruplex DNA in fungal mitochondria may facilitate mitogenome stability: the case of Malassezia.Scientific reports · 2023Article
128 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The POT1 (protection of telomeres 1) protein binds the ssDNA overhangs at the ends of chromosomes in diverse eukaryotes. POT1 is essential for chromosome end-protection, as best demonstrated in fission yeast. In human cells, hPOT1 is also involved in telomere-length regulation. We now show that telomeric oligonucleotides, such as d[GGG(TTAGGG)(3)], which form intramolecular G-quadruplexes through Hoogsteen base-pairing, serve as only marginal primers for extension by recombinant human telomerase; telomerase stalls after every nucleotide addition. Addition of hPOT1 to the reaction restores the normal processive elongation pattern seen with primers that cannot form G-quadruplexes. hPOT1 does not act catalytically but, instead, forms a stoichiometric complex with the DNA, freeing its 3' tail. An antisense oligonucleotide, which base-pairs near the 5' end of the telomeric sequence, leaving a telomerase-extendable 3' tail, duplicates the effect of hPOT1 on activation of G-quadruplex primers. Thus, hPOT1 may function simply by trapping the unfolded forms of these telomeric primers in an equilibrium population. We propose an additional role for hPOT1 in telomere maintenance: disrupting G-quadruplex structures in telomeric DNA, thereby allowing proper elongation by telomerase.
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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.