Structural Mechanisms of Nucleosome Recognition by Linker Histones

By Bing-Rui Zhou, Jiansheng Jiang, H. Feng, R. Ghirlando, T. Xiao, Yawen Bai. 2015

210 citations recorded by the source corpus.

Summary Linker histones bind to the nucleosome and regulate the structure of chromatin and gene expression. Despite more than three decades of effort, structural basis of nucleosome recognition by linker histones remains elusive. Here, we report the crystal structure of the globular domain of chicken linker histone H5 in complex with the nucleosome at 3.5 Å resolution, which is validated using nuclear magnetic resonance spectroscopy. The globular domain sits on the dyad of the nucleosome and interacts with both DNA linkers. Our structure integrates results from mutation analyses, previous cross-linking and fluorescence recovery after photobleach experiments, and helps resolve the long debate on structural mechanisms of nucleosome recognition by linker histones. The on-dyad binding mode of the H5 globular domain is different from the recently reported off-dyad binding mode of Drosophila linker histone H1. We demonstrate that linker histones with different binding modes could fold chromatin to form distinct higher-order structures.

Subfields: Molecular Biology, Plant Science

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Citations in the corpus

Distinct Structures and Dynamics of Chromatosomes with Different Human Linker Histone Isoforms (2020, background): “0) (Zhou et al., 2015) and the chromatosome containing the full-length Xenopus H1.”
Revisit of reconstituted 30-nm nucleosome arrays reveals an ensemble of dynamic structures (2018, methodology): “0 condensed the nucleosome array to a similar extent (Figure 4G and 1C, D), whereas full-length Drosophila H1 had much less effect on the nucleosome array compaction [8].”
ChromEMT: Visualizing 3D chromatin structure and compaction n interphase and mitotic cells (2017, methodology): “The unmatched densities may reflect off-dyad H1 binding (67), histone-tail structures, or proteins other than nucleosomes that interact with DNA and chromatin in the nucleus, such as high-mobility groups (HMGs) (68).”
Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1. (2017, methodology): “The GH5-bound nucleosome structure was determined using the isolated GH5 domain bound to a 167 bp nucleosome bearing short (10 bp) linker DNA arms (Zhou et al., 2015).”