Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.
Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.
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DOI：
10.1093/nar/gku150
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发表时间：
2014-04
影响因子：
14.9
通讯作者：
Ottesen JJ
中科院分区：
文献类型：
--
作者：
North JA;Šimon M;Ferdinand MB;Shoffner MA;Picking JW;Howard CJ;Mooney AM;van Noort J;Poirier MG;Ottesen JJ
核小体含有DNA146bpDNA，包裹在组蛋白八聚体周围，控制∼对转录和修复复合体的可及性。组蛋白的翻译后修饰(PTM)调节核小体功能。到目前为止，只有核小体结构的轻微变化直接归因于组蛋白PTMS。组蛋白残基H3(T118)位于核小体二聚体附近，可被磷酸化。这种PTM破坏了核小体的稳定性，并参与了转录和修复的调节。在这里，我们报道了两个在结构上与核小体不同的DNA-组蛋白复合体的凝胶迁移率、蔗糖梯度沉淀、热解、微球菌核酸酶消化和原子力显微镜测量。我们发现，H3(T118ph)促进了两个DNA分子包裹在两个组蛋白八聚体周围的核小体双链的形成，以及一个包含一个DNA分子包裹两个组蛋白八聚体的阿尔托体复合体的形成。核小体双链复合体在短∼150bpDNA分子内形成，而阿尔茨海默体至少需要∼250bpDNA，并沿3000bpDNA分子重复形成。这些结果是组蛋白PTM显著改变核小体结构的第一个报告。
Nucleosomes contain ∼146 bp of DNA wrapped around a histone protein octamer that controls DNA accessibility to transcription and repair complexes. Posttranslational modification (PTM) of histone proteins regulates nucleosome function. To date, only modest changes in nucleosome structure have been directly attributed to histone PTMs. Histone residue H3(T118) is located near the nucleosome dyad and can be phosphorylated. This PTM destabilizes nucleosomes and is implicated in the regulation of transcription and repair. Here, we report gel electrophoretic mobility, sucrose gradient sedimentation, thermal disassembly, micrococcal nuclease digestion and atomic force microscopy measurements of two DNA–histone complexes that are structurally distinct from nucleosomes. We find that H3(T118ph) facilitates the formation of a nucleosome duplex with two DNA molecules wrapped around two histone octamers, and an altosome complex that contains one DNA molecule wrapped around two histone octamers. The nucleosome duplex complex forms within short ∼150 bp DNA molecules, whereas altosomes require at least ∼250 bp of DNA and form repeatedly along 3000 bp DNA molecules. These results are the first report of a histone PTM significantly altering the nucleosome structure.
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影响因子：
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影响因子：
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作者：
Lowary, PT;Widom, J
通讯作者：
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HERSKOWITZ, I
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