组蛋白H3赖氨酸79二甲基化和组蛋白H4赖氨酸20三甲基化对核小体及染色质结构的影响。
The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure.
作者信息
Lu Xu, Simon Matthew D, Chodaparambil Jayanth V, Hansen Jeffrey C, Shokat Kevan M, Luger Karolin
机构信息
Department of Biochemistry and Molecular Biology, Colorado State University, 1870 Campus Delivery, 1385 Center Avenue, Fort Collins, Colorado 80523-1870, USA.
出版信息
Nat Struct Mol Biol. 2008 Oct;15(10):1122-4. doi: 10.1038/nsmb.1489. Epub 2008 Sep 14.
Abstract
Histone methylation regulates chromatin function dependent on the site and degree of the modification. In addition to creating binding sites for proteins, methylated lysine residues are likely to influence chromatin structure directly. Here we present crystal structures of nucleosomes reconstituted with methylated histones and investigate the folding behavior of resulting arrays. We demonstrate that dimethylation of histone H3 at lysine residue 79 locally alters the nucleosomal surface, whereas trimethylation of H4 at lysine residue 20 affects higher-order structure.
摘要
组蛋白甲基化通过修饰位点和程度来调节染色质功能。除了为蛋白质创造结合位点外，甲基化的赖氨酸残基可能直接影响染色质结构。在此，我们展示了用甲基化组蛋白重构的核小体的晶体结构，并研究了所得阵列的折叠行为。我们证明，赖氨酸残基79处的组蛋白H3二甲基化局部改变了核小体表面，而赖氨酸残基20处的H4三甲基化影响了高阶结构。
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