8OX1

Structure of TRF1core in complex with telomeric nucleosome

Summary for 8OX1

• Entry DOI: 10.2210/pdb8ox1/pdb
• EMDB information: 17252
• Descriptor: Histone H3.1, Histone H4, Histone H2A type 1-C, ... (9 entities in total)
• Functional Keywords: telomeric nucleosome, shelterin, telomere, dna binding protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 12
• Total formula weight: 303144.35

Authors

Hu, H.,van Roon, A.M.M.,Ghanim, G.E.,Ahsan, B.,Oluwole, A.,Peak-Chew, S.,Robinson, C.V.,Nguyen, T.H.D. (deposition date: 2023-04-28, release date: 2023-08-30, Last modification date: 2024-10-23)

Primary citation

Hu, H.,van Roon, A.M.,Ghanim, G.E.,Ahsan, B.,Oluwole, A.O.,Peak-Chew, S.Y.,Robinson, C.V.,Nguyen, T.H.D.
Structural basis of telomeric nucleosome recognition by shelterin factor TRF1.
Sci Adv, 9:eadi4148-eadi4148, 2023

PubMed Abstract: 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.

PubMed: 37624885
DOI: 10.1126/sciadv.adi4148

Experimental method

ELECTRON MICROSCOPY (2.7 Å)