Li Rina, Lin Xingcheng
Department of Physics, North Carolina State University, Raleigh, North Carolina 27607, United States.
Bioinformatics Research Center, North Carolina State University, Raleigh, North Carolina 27607, United States.
Biochemistry. 2025 Mar 18;64(6):1222-1232. doi: 10.1021/acs.biochem.4c00647. Epub 2025 Mar 3.
Histone acetylation is a key regulatory post-translational modification closely associated with gene transcription. In particular, H4K16 acetylation (H4K16ac) is a crucial gene activation marker that induces an open chromatin configuration. While previous studies have explored the effects of H4K16ac on nucleosome interactions, how this local modification affects higher-order chromatin organization remains unclear. To bridge the chemical modifications of these histone tail lysine residues to global chromatin structure, we utilized a residue-resolution coarse-grained chromatin model and enhanced sampling techniques to simulate charge-neutralization effects of histone acetylation on nucleosome stability, internucleosome interactions, and higher-order chromatin structure. Our simulations reveal that H4K16ac stabilizes a single nucleosome due to the reduced entropic contribution of histone tails during DNA unwrapping. In addition, acetylation modestly weakens internucleosome interactions by diminishing contacts between histone tails, DNA, and nucleosome acidic patches. These weakened interactions are amplified when nucleosomes are connected by linker DNA, where increases in linker DNA entry-exit angles lead to significant chromatin destacking and decompaction, exposing nucleosomes to transcriptional activity. Our findings suggest that the geometric constraint imposed by chromatin DNA plays a critical role in driving chromatin structural reorganization upon post-translational modifications.
组蛋白乙酰化是一种与基因转录密切相关的关键翻译后调控修饰。特别是,H4K16乙酰化(H4K16ac)是一种诱导开放染色质构型的关键基因激活标记。虽然先前的研究已经探讨了H4K16ac对核小体相互作用的影响,但这种局部修饰如何影响高阶染色质组织仍不清楚。为了将这些组蛋白尾巴赖氨酸残基的化学修饰与整体染色质结构联系起来,我们利用了一种残基分辨率的粗粒度染色质模型和增强采样技术,来模拟组蛋白乙酰化对核小体稳定性、核小体间相互作用和高阶染色质结构的电荷中和效应。我们的模拟结果表明,H4K16ac通过减少DNA解旋过程中组蛋白尾巴的熵贡献来稳定单个核小体。此外,乙酰化通过减少组蛋白尾巴、DNA和核小体酸性斑块之间的接触,适度减弱了核小体间的相互作用。当核小体通过连接DNA连接时,这些减弱的相互作用会被放大,连接DNA进出角度的增加会导致明显的染色质去堆叠和松散,使核小体暴露于转录活性中。我们发现,染色质DNA施加的几何约束在驱动翻译后修饰后的染色质结构重组中起着关键作用。