EMD-23626

Single-particle
3.7 Å
EMD-23626 Deposition: 15/03/2021
Map released: 29/09/2021
Last modified: 29/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-23626

cryo-EM Structure of Nucleosome containing mouse histone variant H2A.Z

EMD-23626

Single-particle
3.7 Å
EMD-23626 Deposition: 15/03/2021
Map released: 29/09/2021
Last modified: 29/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Xenopus laevis, unidentified, Mus musculus
Sample: Nucleosome core particle containing variant H2A.Z and canonical core histones
Fitted models: 7m1x (Avg. Q-score: 0.391)

Deposition Authors: Tan D , Lewis T
Structural basis of chromatin regulation by histone variant H2A.Z.
Lewis TS, Sokolova V , Jung H , Ng H, Tan D
(2021) Nucleic Acids Res , 49 , 11379 - 11391
PUBMED: 34643712
DOI: doi:10.1093/nar/gkab907
ISSN: 1362-4962
ASTM: NARHAD
Abstract:
The importance of histone variant H2A.Z in transcription regulation has been well established, yet its mechanism-of-action remains enigmatic. Conflicting evidence exists in support of both an activating and a repressive role of H2A.Z in transcription. Here we report cryo-electron microscopy (cryo-EM) structures of nucleosomes and chromatin fibers containing H2A.Z and those containing canonical H2A. The structures show that H2A.Z incorporation results in substantial structural changes in both nucleosome and chromatin fiber. While H2A.Z increases the mobility of DNA terminus in nucleosomes, it simultaneously enables nucleosome arrays to form a more regular and condensed chromatin fiber. We also demonstrated that H2A.Z's ability to enhance nucleosomal DNA mobility is largely attributed to its characteristic shorter C-terminus. Our study provides the structural basis for H2A.Z-mediated chromatin regulation, showing that the increase flexibility of the DNA termini in H2A.Z nucleosomes is central to its dual-functions in chromatin regulation and in transcription.