EMD-15172

Single-particle
8.9 Å
EMD-15172 Deposition: 15/06/2022
Map released: 14/12/2022
Last modified: 15/02/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-15172

H1-free palindromic nucleosome, state E

EMD-15172

Single-particle
8.9 Å
EMD-15172 Deposition: 15/06/2022
Map released: 14/12/2022
Last modified: 15/02/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: 197-bp H1-free palindromic nucleosome

Deposition Authors: Alegrio Louro J , Beinsteiner B , Cheng TC, Patel AKM , Boopathi R , Angelov D , Hamiche A , Bednar J , Kale S , Dimitrov S , Klaholz B
Nucleosome dyad determines the H1 C-terminus collapse on distinct DNA arms.
PUBMED: 36610392
DOI: doi:10.1016/j.str.2022.12.005
ISSN: 0969-2126
ASTM: STRUE6
Abstract:
Nucleosomes are symmetric structures. However, binding of linker histones generates an inherently asymmetric H1-nucleosome complex, and whether this asymmetry is transmitted to the overall nucleosome structure, and therefore also to chromatin, is unclear. Efforts to investigate potential asymmetry due to H1s have been hampered by the DNA sequence, which naturally differs in each gyre. To overcome this issue, we designed and analyzed by cryo-EM a nucleosome reconstituted with a palindromic (601L) 197-bp DNA. As in the non-palindromic 601 sequence, H1 restricts linker DNA flexibility but reveals partial asymmetrical unwrapping. However, in contrast to the non-palindromic nucleosome, in the palindromic nucleosome H1 CTD collapses to the proximal linker. Molecular dynamics simulations show that this could be dictated by a slightly tilted orientation of the globular domain (GD) of H1, which could be linked to the DNA sequence of the nucleosome dyad.