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首页> 外文期刊>Journal of proteome research >Mapping Post-translational Modifications of Mammalian Testicular Specific Histone Variant TH2B in Tetraploid and Haploid Germ Cells and Their Implications on the Dynamics of Nucleosome Structure
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Mapping Post-translational Modifications of Mammalian Testicular Specific Histone Variant TH2B in Tetraploid and Haploid Germ Cells and Their Implications on the Dynamics of Nucleosome Structure

机译：四倍体和单倍体生殖细胞中哺乳动物睾丸特异组蛋白变体TH2B的翻译后翻译图谱及其对核小体结构动力学的影响

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摘要

Histones regulate a variety of chromatin templated events by their post-translational modifications (PTMs). Although there are extensive reports on the PTMs of canonical histones, the information on the histone variants remains very scanty. Here, we report the identification of different PTMs, such as acetylation, methylation, and phosphorylation of a major mammalian histone variant TH2B. Our mass spectrometric analysis has led to the identification of both conserved and unique modifications across tetraploid spermatocytes and haploid spermatids. We have also computationally derived the 3-dimensional model of a TH2B containing nucleosome in order to study the spatial orientation of the PTMs identified and their effect on nucleosome stability and DNA binding potential. From our nucleosome model, it is evident that substititution of specific amino acid residues in TH2B results in both differential histone-DNA and histone-histone contacts. Furthermore, we have also observed that acetylation on the N-terminal tail of TH2B weakens the interactions with the DNA. These results provide direct evidence that, similar to somatic H2B, the testis specific histone TH2B also undergoes multiple PTMs, suggesting the possibility of chromatin regulation by such covalent modifications in mammalian male germ cells.
机译：组蛋白通过其翻译后修饰（PTM）调节各种染色质模板化事件。尽管有大量有关规范组蛋白PTM的报道，但是有关组蛋白变体的信息仍然很少。在这里，我们报告鉴定不同的PTMs，例如主要哺乳动物组蛋白变体TH2B的乙酰化，甲基化和磷酸化。我们的质谱分析已鉴定出跨四倍体精细胞和单倍体精细胞的保守修饰和独特修饰。我们还计算出了含有核小体的TH2B的3维模型，以研究鉴定出的PTM的空间方向及其对核小体稳定性和DNA结合潜力的影响。从我们的核小体模型中可以明显看出，TH2B中特定氨基酸残基的取代会导致组蛋白-DNA和组蛋白-组蛋白的差异接触。此外，我们还观察到TH2B N末端尾部的乙酰化作用减弱了与DNA的相互作用。这些结果提供了直接的证据，证明与体细胞H2B相似，睾丸特异性组蛋白TH2B也经历了多个PTM，这表明在哺乳动物雄性生殖细胞中通过此类共价修饰来调节染色质的可能性。

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