ArticleNucleic acids research2016
Functional interplay between SA1 and TRF1 in telomeric DNA binding and DNA-DNA pairing.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Single-trajectory Bayesian modeling reveals multi-state diffusion of the MSH sliding clamp.NPJ systems biology and applications · 2026Article
- The intrinsically disordered tail of ESCO1 binds DNA in a charge-dependent manner.bioRxiv : the preprint server for biology · 2023Article
- 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
- Cohesin-independent STAG proteins interact with RNA and R-loops and promote complex loading.eLife · 2023Article
- The TERB1 MYB domain suppresses telomere erosion in meiotic prophase I.Cell reports · 2022Article
- TIN2 is an architectural protein that facilitates TRF2-mediated trans- and cis-interactions on telomeric DNA.Nucleic acids research · 2021Article
- Dynamics of TRF1 organizing a single human telomere.Nucleic acids research · 2021Article
- Atomic Force Microscopy Reveals that the Drosophila Telomere-Capping Protein Verrocchio Is a Single-Stranded DNA-Binding Protein.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Cohesin SA1 and SA2 are RNA binding proteins that localize to RNA containing regions on DNA.Nucleic acids research · 2020Article
- Single molecule analysis reveals monomeric XPA bends DNA and undergoes episodic linear diffusion during damage search.Nature communications · 2020Article
- Guidelines for DNA recombination and repair studies: Mechanistic assays of DNA repair processes.Microbial cell (Graz, Austria) · 2019Review
- AFM Imaging Reveals Multiple Conformational States of ADAMTS13.Journal of biological engineering · 2019Article
- Towards a Unified Model of SMC Complex Function.Current biology : CB · 2018Review
- Cohesin SA2 is a sequence-independent DNA-binding protein that recognizes DNA replication and repair intermediates.The Journal of biological chemistry · 2018Article
- Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018Review
- Loss of Tumor SuppressorCancer research · 2017Article
- Rad4 recognition-at-a-distance: Physical basis of conformation-specific anomalous diffusion of DNA repair proteins.Progress in biophysics and molecular biology · 2017Review
- Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017Review
- Single-Molecule Methods for Nucleotide Excision Repair: Building a System to Watch Repair in Real Time.Methods in enzymology · 2017Article
Corrections and comments
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Authors and funding
17 authors at 9 institutions in 4 countries.
Funding
Abstract
Proper chromosome alignment and segregation during mitosis depend on cohesion between sister chromatids. Cohesion is thought to occur through the entrapment of DNA within the tripartite ring (Smc1, Smc3 and Rad21) with enforcement from a fourth subunit (SA1/SA2). Surprisingly, cohesin rings do not play a major role in sister telomere cohesion. Instead, this role is replaced by SA1 and telomere binding proteins (TRF1 and TIN2). Neither the DNA binding property of SA1 nor this unique telomere cohesion mechanism is understood. Here, using single-molecule fluorescence imaging, we discover that SA1 displays two-state binding on DNA: searching by one-dimensional (1D) free diffusion versus recognition through subdiffusive sliding at telomeric regions. The AT-hook motif in SA1 plays dual roles in modulating non-specific DNA binding and subdiffusive dynamics over telomeric regions. TRF1 tethers SA1 within telomeric regions that SA1 transiently interacts with. SA1 and TRF1 together form longer DNA-DNA pairing tracts than with TRF1 alone, as revealed by atomic force microscopy imaging. These results suggest that at telomeres cohesion relies on the molecular interplay between TRF1 and SA1 to promote DNA-DNA pairing, while along chromosomal arms the core cohesin assembly might also depend on SA1 1D diffusion on DNA and sequence-specific DNA binding.
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Registered trials
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