ArticleNucleic acids research2014
TRF1 and TRF2 use different mechanisms to find telomeric DNA but share a novel mechanism to search for protein partners at telomeres.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed, 75 citations in OpenAlex.
- Quantifying telomere length: from bulk assays to single-molecule resolution.Biophysics reports · 2026Article
- Single-trajectory Bayesian modeling reveals multi-state diffusion of the MSH sliding clamp.NPJ systems biology and applications · 2026Article
- Cancer-associated TRF1 mutations alter PARP1 interaction dynamics: an in silico study.Mammalian genome : official journal of the International Mammalian Genome Society · 2026Article
- TRF1 and TRF2 form distinct shelterin subcomplexes at telomeres.Cell reports · 2025Article
- Preparation of a Substrate for Studying Nucleosomes on Single Molecules of DNA.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Single-molecule fluorescence imaging of DNA maintenance protein binding dynamics and activities on extended DNA.Current opinion in structural biology · 2024Review
- Investigating the Relationship between Telomere-Related Gene Variants and Leukocyte Telomere Length in Optic Neuritis Patients.Journal of clinical medicine · 2024Article
- Structural Motifs at the Telomeres and Their Role in Regulatory Pathways.Biochemistry · 2024Review
- Single-molecule imaging of genome maintenance proteins encountering specific DNA sequences and structures.DNA repair · 2023Review
- Assembly path dependence of telomeric DNA compaction by TRF1, TIN2, and SA1.Biophysical journal · 2023Article
- PARP1 associates with R-loops to promote their resolution and genome stability.Nucleic acids research · 2023Article
- Possible molecular mechanisms underlying the development of atherosclerosis in cancer survivors.Frontiers in cardiovascular medicine · 2023Review
- Resolving the subtle details of human DNA alkyltransferase lesion search and repair mechanism by single-molecule studies.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
- Curcumol inhibits ferritinophagy to restrain hepatocyte senescence through YAP/NCOA4 in non-alcoholic fatty liver disease.Cell proliferation · 2021Article
- Shaping human telomeres: from shelterin and CST complexes to telomeric chromatin organization.Nature reviews. Molecular cell biology · 2021Review
- Hopping and Flipping of RNA Polymerase on DNA during Recycling for Reinitiation after Intrinsic Termination in Bacterial Transcription.International journal of molecular sciences · 2021Article
- Cohesin SA1 and SA2 are RNA binding proteins that localize to RNA containing regions on DNA.Nucleic acids research · 2020Article
- Alkyltransferase-like protein clusters scan DNA rapidly over long distances and recruit NER to alkyl-DNA lesions.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Human telomeres are maintained by the shelterin protein complex in which TRF1 and TRF2 bind directly to duplex telomeric DNA. How these proteins find telomeric sequences among a genome of billions of base pairs and how they find protein partners to form the shelterin complex remains uncertain. Using single-molecule fluorescence imaging of quantum dot-labeled TRF1 and TRF2, we study how these proteins locate TTAGGG repeats on DNA tightropes. By virtue of its basic domain TRF2 performs an extensive 1D search on nontelomeric DNA, whereas TRF1's 1D search is limited. Unlike the stable and static associations observed for other proteins at specific binding sites, TRF proteins possess reduced binding stability marked by transient binding (∼ 9-17 s) and slow 1D diffusion on specific telomeric regions. These slow diffusion constants yield activation energy barriers to sliding ∼ 2.8-3.6 κ(B)T greater than those for nontelomeric DNA. We propose that the TRF proteins use 1D sliding to find protein partners and assemble the shelterin complex, which in turn stabilizes the interaction with specific telomeric DNA. This 'tag-team proofreading' represents a more general mechanism to ensure a specific set of proteins interact with each other on long repetitive specific DNA sequences without requiring external energy sources.
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