Single-Molecule Studies of the Linker Histone H1 Binding to DNA and the Nucleosome,Biochemistry

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Single-Molecule Studies of the Linker Histone H1 Binding to DNA and the Nucleosome
Biochemistry ( IF 2.9 ) Pub Date : 2016-03-29 00:00:00 , DOI: 10.1021/acs.biochem.5b01247
Hongjun Yue ₁ , He Fang ₂ , Sijie Wei ₁ , Jeffrey J Hayes ₂ , Tae-Hee Lee ₁

Affiliation

Linker histone H1 regulates chromatin structure and gene expression. Investigating the dynamics and stoichiometry of binding of H1 to DNA and the nucleosome is crucial to elucidating its functions. Because of the abundant positive charges and the strong self-affinity of H1, quantitative in vitro studies of its binding to DNA and the nucleosome have generated results that vary widely and, therefore, should be interpreted in a system specific manner. We sought to overcome this limitation by developing a specially passivated microscope slide surface to monitor binding of H1 to DNA and the nucleosome at a single-molecule level. According to our measurements, the stoichiometry of binding of H1 to DNA and the nucleosome is very heterogeneous with a wide distribution whose averages are in reasonable agreement with previously published values. Our study also revealed that H1 does not dissociate from DNA or the nucleosome on a time scale of tens of minutes. We found that histone chaperone Nap1 readily dissociates H1 from DNA and superstoichiometrically bound H1 from the nucleosome, supporting a hypothesis whereby histone chaperones contribute to the regulation of the H1 profile in chromatin.

中文翻译：

连接组蛋白 H1 与 DNA 和核小体结合的单分子研究

连接组蛋白 H1 调节染色质结构和基因表达。研究 H1 与 DNA 和核小体结合的动力学和化学计量对于阐明其功能至关重要。由于 H1 具有丰富的正电荷和很强的自亲和力，其与 DNA 和核小体结合的定量体外研究产生的结果差异很大，因此应该以系统特定的方式进行解释。我们试图通过开发一种特殊钝化的显微镜载玻片表面来克服这一限制，以在单分子水平上监测 H1 与 DNA 和核小体的结合。根据我们的测量，H1 与 DNA 和核小体结合的化学计量非常异质，分布广泛，其平均值与之前公布的值相当一致。我们的研究还表明，H1 在数十分钟的时间内不会与 DNA 或核小体解离。我们发现组蛋白伴侣 Nap1 很容易将 H1 从 DNA 上解离，并以超化学计量将 H1 从核小体上结合，这支持了组蛋白伴侣有助于调节染色质中 H1 谱的假设。

更新日期：2016-03-29

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