The Effects of Histone H2B Ubiquitylations on the Nucleosome Structure and Internucleosomal Interactions.
The Effects of Histone H2B Ubiquitylations on the Nucleosome Structure and Internucleosomal Interactions.
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DOI：
10.1021/acs.biochem.2c00422
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发表时间：
2022-10-18
期刊：
影响因子：
2.9
通讯作者：
Lee, Tae-Hee
中科院分区：
文献类型：
--
作者：
Sengupta, Bhaswati;Huynh, Mai;Smith, Charlotte B.;McGinty, Robert K.;Krajewski, Wladyslaw;Lee, Tae-Hee
真核生物基因压缩发生在多个层次上，将DNA包装到染色质和染色体上。DNA包装的两个最基本的水平是在核小体和双核小体堆叠。核小体是基本的基因包装单位，由DNA包裹在组蛋白核心周围组成。核小体彼此堆叠以进一步压缩DNA。第一个堆叠步骤导致双核体形成，这是由两个核小体的各个部分之间的核小体间相互作用驱动的。组蛋白是翻译后修饰的重要靶点，其中一些修饰会影响核小体的结构和核小体之间的相互作用。这些效应通常涉及各种基因组交易的调节。特别是，组蛋白H2B泛素化与促进转录和六酶体形成有关。在这里，我们采用半合成泛素化组蛋白H2B和单分子FRET研究H2B泛素化赖氨酸34（H2BK 34）和赖氨酸120（H2BK 120）的核小体的结构和两个核小体之间的相互作用的影响。我们的研究结果表明，H2BK 34泛素化扩大了核小体中的DNA回旋间隙，并稳定了长距离和短距离的核小体间的相互作用，而H2BK 120泛素化不影响核小体的结构或核小体间的相互作用。这些结果表明，H2B泛素化在促进转录和六酶体形成，同时保持染色质的结构完整性的潜在作用。
Eukaryotic gene compaction takes place at multiple levels to package DNA to chromatin and chromosomes. Two of the most fundamental levels of DNA packaging are at the nucleosome and dinucleosome stacks. The nucleosome is the basic gene packing unit and is composed of DNA wrapped around a histone core. Nucleosomes stack with one another for further compaction of DNA. The first stacking step leads to dinucleosome formation, which is driven by internucleosomal interactions between various parts of two nucleosomes. Histone proteins are rich targets for post-translational modifications, some of which affect the structure of the nucleosome and the interactions between nucleosomes. These effects are often implicated in the regulation of various genomic transactions. In particular, histone H2B ubiquitylation has been associated with facilitated transcription and hexasome formation. Here, we employed semi-synthetically ubiquitylated histone H2B and single-molecule FRET to investigate the effects of H2B ubiquitylations at lysine 34 (H2BK34) and lysine 120 (H2BK120) on the structure of the nucleosome and the interactions between two nucleosomes. Our results suggest that H2BK34 ubiquitylation widens the DNA gyre gap in the nucleosome and stabilizes long- and short-range internucleosomal interactions while H2BK120 ubiquitylation does not affect the nucleosome structure or internucleosomal interactions. These results suggest potential roles for H2B ubiquitylations in facilitated transcription and hexasome formation while maintaining the structural integrity of chromatin.
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