Structural basis of telomeric nucleosome recognition by shelterin factor TRF1

• DOI: 10.1126/sciadv.adi4148
• Publication Date: 2023-08-25T17:58:21Z
• Authors: Hongmiao Hu; Anne-Marie M. van...; George E. Ghanim; Bilal Ahsan; Abraham O. Oluwole; Sew-Yeu Peak-Chew; Carol V. Robinson; Thi Hoang Duong N...
• Keywords: Shelterin

Shelterin and nucleosomes are the key players that organize mammalian chromosome ends into 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 bound to shelterin factor TRF1. Our reveal TRF1 binds unwrapped nucleosomal DNA by engaging histone octamer. Unexpectedly, binding shifts register 1 bp. discovered phosphorylation C terminus noncanomical surface on critical for its association nucleosomes. These insights shelterin-chromatin interactions have crucial implications understanding chromatin organization roles including replication transcription.