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Centromeric Histone H4 Acetylation in Hordeum vulgare

机译:大麦中的着丝粒组蛋白H4乙酰化

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Histone acetylation is a post-translational modification of lysine residues in the N-terminal regions of nucleosomal histones. In this study, structural significance of histone H4 acetylation was revealed in Hordeum vulgare by using a three-dimensional imaging method. The centromeres were clustered near the nuclear membrane at one pole of a nucleus. A ring-like distribution of the highly acetylated histone H4 at lysine 5 in non-fixed nuclei, which is very similar to the centromere cluster, was visualized. The centromeres and the highly acetylated regions were co-localized, however, the signals did not completely overlap with each other. During the mitotic stage, when large-scale changes in chromosome structure occurred, the centromeric acetylation of K5 changed dramatically. These findings suggest that the highly acetylated lysine residues of histone H4 is related to the structural changes of barley centromeres.
机译:组蛋白乙酰化是核小体组蛋白N端区域中赖氨酸残基的翻译后修饰。在这项研究中,通过使用三维成像方法,揭示了大麦中组蛋白H4乙酰化的结构意义。着丝粒聚集在核的一个极点的核膜附近。观察到高度固定化的组蛋白H4在赖氨酸5在非固定核中的环状分布,这与着丝粒簇非常相似。着丝粒和高度乙酰化的区域共定位,但是,信号并不完全相互重叠。在有丝分裂阶段,当染色体结构发生大规模变化时,K5的着丝粒乙酰化发生了巨大变化。这些发现表明,组蛋白H4的高度乙酰化的赖氨酸残基与大麦着丝粒的结构变化有关。

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