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XB-ART-58064
J Mol Biol 2021 Mar 19;4336:166881. doi: 10.1016/j.jmb.2021.166881.
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Binding Dynamics of Disordered Linker Histone H1 with a Nucleosomal Particle.

Wu H , Dalal Y , Papoian GA .


Abstract
Linker histone H1 is an essential regulatory protein for many critical biological processes, such as eukaryotic chromatin packaging and gene expression. Mis-regulation of H1s is commonly observed in tumor cells, where the balance between different H1 subtypes has been shown to alter the cancer phenotype. Consisting of a rigid globular domain and two highly charged terminal domains, H1 can bind to multiple sites on a nucleosomal particle to alter chromatin hierarchical condensation levels. In particular, the disordered H1 amino- and carboxyl-terminal domains (NTD/CTD) are believed to enhance this binding affinity, but their detailed dynamics and functions remain unclear. In this work, we used a coarse-grained computational model, AWSEM-DNA, to simulate the H1.0b-nucleosome complex, namely chromatosome. Our results demonstrate that H1 disordered domains restrict the dynamics and conformation of both globular H1 and linker DNA arms, resulting in a more compact and rigid chromatosome particle. Furthermore, we identified regions of H1 disordered domains that are tightly tethered to DNA near the entry-exit site. Overall, our study elucidates at near-atomic resolution the way the disordered linker histone H1 modulates nucleosome's structural preferences and conformational dynamics.

PubMed ID: 33617899
PMC ID: PMC9272445
Article link: J Mol Biol
Grant support: [+]

Species referenced: Xenopus laevis

References [+] :
Allan, The structure of histone H1 and its location in chromatin. 1980, Pubmed