Centre National de la Recherche Scientifique (CNRS)
フランス
Agence Nationale de la Recherche (ANR)
フランス
French Infrastructure for Integrated Structural Biology (FRISBI)
フランス
Instruct-ERIC Center (Strasbourg Centre)
フランス
Foundation for Medical Research (France)
フランス
Institut National du Cancer (inCA)
フランス
European Regional Development Fund
epiRNA - (Region Grand Est; Competitivite Alsace 2014-2020)
European Union
引用
ジャーナル: Structure / 年: 2023 タイトル: Nucleosome dyad determines the H1 C-terminus collapse on distinct DNA arms. 著者: Jaime Alegrio Louro / Ramachandran Boopathi / Brice Beinsteiner / Abdul Kareem Mohideen Patel / Tat Cheung Cheng / Dimitar Angelov / Ali Hamiche / Jan Bendar / Seyit Kale / Bruno P Klaholz / Stefan Dimitrov / 要旨: 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 ...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.