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| Title | Structural basis for linker histone H5-nucleosome binding and chromatin fiber compaction. |
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| Journal, issue, pages | Cell Res, Vol. 34, Issue 10, Page 707-724, Year 2024 |
| Publish date | Aug 5, 2024 |
 Authors | Wenyan Li / Jie Hu / Feng Song / Juan Yu / Xin Peng / Shuming Zhang / Lin Wang / Mingli Hu / Jia-Cheng Liu / Yu Wei / Xue Xiao / Yan Li / Dongyu Li / Hui Wang / Bing-Rui Zhou / Linchang Dai / Zongjun Mou / Min Zhou / Haonan Zhang / Zheng Zhou / Huidong Zhang / Yawen Bai / Jin-Qiu Zhou / Wei Li / Guohong Li / Ping Zhu /   |
| PubMed Abstract | The hierarchical packaging of chromatin fibers plays a critical role in gene regulation. The 30-nm chromatin fibers, a central-level structure bridging nucleosomal arrays to higher-order ...The hierarchical packaging of chromatin fibers plays a critical role in gene regulation. The 30-nm chromatin fibers, a central-level structure bridging nucleosomal arrays to higher-order organizations, function as the first level of transcriptional dormant chromatin. The dynamics of 30-nm chromatin fiber play a crucial role in biological processes related to DNA. Here, we report a 3.6-angstrom resolution cryogenic electron microscopy structure of H5-bound dodecanucleosome, i.e., the chromatin fiber reconstituted in the presence of linker histone H5, which shows a two-start left-handed double helical structure twisted by tetranucleosomal units. An atomic structural model of the H5-bound chromatin fiber, including an intact chromatosome, is built, which provides structural details of the full-length linker histone H5, including its N-terminal domain and an HMG-motif-like C-terminal domain. The chromatosome structure shows that H5 binds the nucleosome off-dyad through a three-contact mode in the chromatin fiber. More importantly, the H5-chromatin structure provides a fine molecular basis for the intra-tetranucleosomal and inter-tetranucleosomal interactions. In addition, we systematically validated the physiological functions and structural characteristics of the tetranucleosomal unit through a series of genetic and genomic studies in Saccharomyces cerevisiae and in vitro biophysical experiments. Furthermore, our structure reveals that multiple structural asymmetries of histone tails confer a polarity to the chromatin fiber. These findings provide structural and mechanistic insights into how a nucleosomal array folds into a higher-order chromatin fiber with a polarity in vitro and in vivo. |
 External links | Cell Res / PubMed:39103524 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.3 - 3.6 Å |
| Structure data |  EMDB-37637: Structural basis for the nucleosome binding and chromatin compaction by the linker histone H5  EMDB-37638: Structural basis for the nucleosome binding and chromatin compaction by the linker histone H5 EMDB-38407, PDB-8xjv: |
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 Keywords | GENE REGULATION / Chromatin Fiber / Histone / DNA / Linker Histone / Nucleosome / Epigenetics / Genome Folding / Interaction |
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