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首页> 外文期刊>Molecular and Cellular Biology >Acetylation-Dependent Chromatin Reorganization by BRDT, a Testis-Specific Bromodomain-Containing Protein
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Acetylation-Dependent Chromatin Reorganization by BRDT, a Testis-Specific Bromodomain-Containing Protein

机译：BRDT，一种睾丸特异性溴结构域蛋白，乙酰化依赖的染色质重组

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The association between histone acetylation and replacement observed during spermatogenesis prompted us to consider the testis as a source for potential factors capable of remodelling acetylated chromatin. A systematic search of data banks for open reading frames encoding testis-specific bromodomain-containing proteins focused our attention on BRDT, a testis-specific protein of unknown function containing two bromodomains. BRDT specifically binds hyperacetylated histone H4 tail depending on the integrity of both bromodomains. Moreover, in somatic cells, the ectopic expression of BRDT triggered a dramatic reorganization of the chromatin only after induction of histone hyperacetylation by trichostatin A (TSA). We then defined critical domains of BRDT involved in its activity. Both bromodomains of BRDT, as well as flanking regions, were found indispensable for its histone acetylation-dependent remodelling activity. Interestingly, we also observed that recombinant BRDT was capable of inducing reorganization of the chromatin of isolated nuclei in vitro only when the nuclei were from TSA-treated cells. This assay also allowed us to show that the action of BRDT was ATP independent, suggesting a structural role for the protein in the remodelling of acetylated chromatin. This is the first demonstration of a large-scale reorganization of acetylated chromatin induced by a specific factor.
机译：精子发生过程中观察到的组蛋白乙酰化与置换之间的联系促使我们考虑将睾丸视为能够重塑乙酰化染色质的潜在因素的来源。对数据库进行系统搜索以查找编码睾丸特异性含溴结构域蛋白的开放阅读框，使我们的注意力集中在BRDT上，BRDT是一种功能未知的睾丸特异性蛋白，包含两个溴结构域。 BRDT会根据两个溴结构域的完整性特异性结合高乙酰化的组蛋白H4尾巴。此外，在体细胞中，仅在曲古抑菌素A（TSA）诱导组蛋白超乙酰化后，BRDT的异位表达才触发染色质的显着重组。然后，我们定义了参与其活动的BRDT的关键领域。发现BRDT的两个溴结构域以及侧翼区域对于其依赖于组蛋白乙酰化的重塑活性都是必不可少的。有趣的是，我们还观察到重组BRDT仅在细胞核来自TSA处理的细胞时才能够在体外诱导分离的细胞核的染色质重组。该测定法还使我们能够证明BRDT的作用与ATP无关，表明该蛋白质在乙酰化染色质重塑中的结构作用。这是由特定因子诱导的乙酰化染色质大规模重组的首次证明。

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