TIN2 is an Architecture Protein that Facilitates TRF2-Mediated Higher-Order DNA and RNA Structures at Telomeres
نویسندگان
چکیده
Previous single-molecule studies of dynamics shelterin assembles on DNA focused short telomeric repeats (32 TTAGGG) in the context λ sequences. Studies based sequences showed that complexes form individual DNA. However, previous electron microscopy, atomic force microscopy and bulk biochemical assays also demonstrated TRF2 forms multi-protein compacts There are discrepancies from these whether TIN2 regulates compaction by physiologically long To directly address long-standing questions, we have studied regulated substrates purified mouse liver tissue. We how helps protecting telomeres forming T-loops. Given human cells, TRF1, TRF2, TIN2, RapI approximately 10 times more abundant than POT1 TPP1, majority TRF1 proteins exist without TPP1 at telomeres. Therefore, this study, (TIN2S TIN2L) binding livers.
منابع مشابه
TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres.
Human telomeres contain two related telomeric DNA-binding proteins, TRF1 and TRF2. The TRF1 complex contains the TRF1 interacting partner, TIN2, as well as PIP1 and POT1 and regulates telomere-length homeostasis. The TRF2 complex is primarily involved in telomere protection and contains the TRF2 interacting partner human (h)Rap1 as well as several factors involved in the DNA damage response. A ...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2021
ISSN: ['0006-3495', '1542-0086']
DOI: https://doi.org/10.1016/j.bpj.2020.11.1035