Nucleosome dyad determines the H1 C-terminus collapse on distinct DNA arms
Oluşturanlar
- 1. IGBMC Inst Genet & Mol & Cellular Biol, Ctr Integrat Biol CBI, Dept Integrated Struct Biol, 1 Rue Laurent Fries, F-67404 Illkirch Graffenstaden, France
- 2. Univ Lyon, Ecole Normale Super Lyon, CNRS, Lab Biol & Modelisat Cellule LBMC, 46 Allee Italie, F-69007 Lyon, France
- 3. Univ Grenoble Alpes, Inst Adv Biosci IAB, CNRS UMR 5309, INSERM U1209, Site Sante Allee Alpes, F-38700 La Tronche, France
- 4. Dokuz Eylul Univ Hlth Campus, Izmir Biomed & Genome Ctr, TR-35330 Izmir, Turkiye
Açıklama
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.
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