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-Structure paper
タイトル | Structural basis of telomeric nucleosome recognition by shelterin factor TRF1. |
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ジャーナル・号・ページ | Sci Adv, Vol. 9, Issue 34, Page eadi4148, Year 2023 |
掲載日 | 2023年8月25日 |
著者 | Hongmiao Hu / Anne-Marie M van Roon / George E Ghanim / Bilal Ahsan / Abraham O Oluwole / Sew-Yeu Peak-Chew / Carol V Robinson / Thi Hoang Duong Nguyen / |
PubMed 要旨 | Shelterin and nucleosomes are the key players that organize mammalian chromosome ends into the protective telomere caps. However, how they interact with each other at telomeres remains unknown. We ...Shelterin and nucleosomes are the key players that organize mammalian chromosome ends into the protective telomere caps. However, how they interact with each other at telomeres remains unknown. We report cryo-electron microscopy structures of a human telomeric nucleosome both unbound and bound to the shelterin factor TRF1. Our structures reveal that TRF1 binds unwrapped nucleosomal DNA ends by engaging both the nucleosomal DNA and the histone octamer. Unexpectedly, TRF1 binding shifts the register of the nucleosomal DNA by 1 bp. We discovered that phosphorylation of the TRF1 C terminus and a noncanomical DNA binding surface on TRF1 are critical for its association with telomeric nucleosomes. These insights into shelterin-chromatin interactions have crucial implications for understanding telomeric chromatin organization and other roles of shelterin at telomeres including replication and transcription. |
リンク | Sci Adv / PubMed:37624885 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.52 - 6.67 Å |
構造データ | EMDB-17251, PDB-8ox0: EMDB-17252, PDB-8ox1: EMDB-17253: Structure of TRF1core in complex with telomeric nucleosome (4:1 complex) |
化合物 | ChemComp-HOH: |
由来 |
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キーワード | DNA BINDING PROTEIN / Telomeric nucleosome / shelterin / telomere |