ArticleJournal of cell science2013
SA1 binds directly to DNA through its unique AT-hook to promote sister chromatid cohesion at telomeres.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- Tankyrases and Their Binding Proteins: Origins of Their Roles in Diverse Cellular Pathways.Cells · 2026Review
- Review
- Binding to the Other Side: The AT-Hook DNA-Binding Domain Allows Nuclear Factors to Exploit the DNA Minor Groove.International journal of molecular sciences · 2024Review
- Condensin positioning at telomeres by shelterin proteins drives sister-telomere disjunction in anaphase.eLife · 2023Article
- The N-terminus of Stag1 is required to repress the 2C program by maintaining rRNA expression and nucleolar integrity.Stem cell reports · 2023Article
- TERRA R-loops connect and protect sister telomeres in mitosis.Cell reports · 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 Interplay of Cohesin and RNA Processing Factors: The Impact of Their Alterations on Genome Stability.International journal of molecular sciences · 2022Review
- Paralogous synthetic lethality underlies genetic dependencies of the cancer-mutated geneLife science alliance · 2021Article
- Persistent telomere cohesion protects aged cells from premature senescence.Nature communications · 2020Article
- Aurora B and condensin are dispensable for chromosome arm and telomere separation during meiosis II.Molecular biology of the cell · 2020Article
- Redundant and specific roles of cohesin STAG subunits in chromatin looping and transcriptional control.Genome research · 2020Article
- Nuclear PARPs and genome integrity.Genes & development · 2020Review
- Resolution of human ribosomal DNA occurs in anaphase, dependent on tankyrase 1, condensin II, and topoisomerase IIα.Genes & development · 2019Article
- SMC5/6: Multifunctional Player in Replication.Genes · 2018Review
- 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
- Loss of Tumor SuppressorCancer research · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Sister chromatid cohesion relies on cohesin, a complex comprising a tri-partite ring and a peripheral subunit Scc3, which is found as two related isoforms SA1 and SA2 in vertebrates. There is a division of labor between the vertebrate cohesin complexes; SA1-cohesin is required at telomeres and SA2-cohesin at centromeres. Depletion of SA1 has dramatic consequences for telomere function and genome integrity, but the mechanism by which SA1-cohesin mediates cohesion at telomeres is not well understood. Here we dissect the individual contribution of SA1 and the ring subunits to telomere cohesion and show that telomeres rely heavily on SA1 and to a lesser extent on the ring for cohesion. Using chromatin immunoprecipitation we show that SA1 is highly enriched at telomeres, is decreased at mitosis when cohesion is resolved, and is increased when cohesion persists. Overexpression of SA1 alone was sufficient to induce cohesion at telomeres, independent of the cohesin ring and dependent on its unique (not found in SA2) N-terminal domain, which we show binds to telomeric DNA through an AT-hook motif. We suggest that a specialized cohesion mechanism may be required to accommodate the high level of DNA replication-associated repair at telomeres.
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Registered trials
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.