Laboratory of RNA Epigenetics, Institutes of Biomedical Sciences & Shanghai Public Health Clinical Center, Shanghai Medical College, Fudan University, Shanghai 200032, China.
Int J Mol Sci. 2024 Jul 10;25(14):7562. doi: 10.3390/ijms25147562.
Histone arginine residue methylation is crucial for individual development and gene regulation. However, the dynamics of histone arginine methylation in response to cellular stress remains largely unexplored. In addition, the interplay and regulatory mechanisms between this and other histone modifications are important scientific questions that require further investigation. This study aimed to investigate the changes in histone arginine methylation in response to DNA damage. We report a global decrease in histone H3R26 symmetric dimethylation (H3R26me2s) and hypoacetylation at the H3K27 site in response to DNA damage. Notably, H3R26me2s exhibits a distribution pattern similar to that of H3K27ac across the genome, both of which are antagonistic to H3K27me3. Additionally, histone deacetylase 1 (HDAC1) may be recruited to the H3R26me2s demethylation region to mediate H3K27 deacetylation. These findings suggest crosstalk between H3R26me2s and H3K27ac in regulating gene expression.
组蛋白精氨酸残基甲基化对于个体发育和基因调控至关重要。然而，组蛋白精氨酸甲基化对细胞应激的反应动力学在很大程度上仍未得到探索。此外，这种甲基化与其他组蛋白修饰之间的相互作用和调控机制是需要进一步研究的重要科学问题。本研究旨在探讨 DNA 损伤对组蛋白精氨酸甲基化的影响。我们报告了 DNA 损伤后组蛋白 H3R26 对称二甲基化（H3R26me2s）和 H3K27 位点乙酰化程度降低。值得注意的是，H3R26me2s 在基因组上的分布模式与 H3K27ac 相似，两者均与 H3K27me3 呈拮抗关系。此外，组蛋白去乙酰化酶 1（HDAC1）可能被招募到 H3R26me2s 去甲基化区域，介导 H3K27 去乙酰化。这些发现表明 H3R26me2s 和 H3K27ac 之间存在相互作用，共同调节基因表达。
