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首页> 外文期刊>Molecular and Cellular Biology >Mutational Analysis of the Sir3 BAH Domain Reveals Multiple Points of Interaction with Nucleosomes
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Mutational Analysis of the Sir3 BAH Domain Reveals Multiple Points of Interaction with Nucleosomes

机译：Sir3 BAH域的突变分析揭示了与核小体相互作用的多个点。

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Sir3, a component of the transcriptional silencing complex in the yeast Saccharomyces cerevisiae, has an N-terminal BAH domain that is crucial for the protein's silencing function. Previous work has shown that the N-terminal alanine residue of Sir3 (Ala2) and its acetylation play an important role in silencing. Here we show that the silencing defects of Sir3 Ala2 mutants can be suppressed by mutations in histones H3 and H4, specifically, by H3 D77N and H4 H75Y mutations. Additionally, a mutational analysis demonstrates that three separate regions of the Sir3 BAH domain are important for its role in silencing. Many of these BAH mutations also can be suppressed by the H3 D77N and H4 H75Y mutations. In agreement with the results of others, in vitro experiments show that the Sir3 BAH domain can interact with partially purified nucleosomes. The silencing-defective BAH mutants are defective for this interaction. These results, together with the previously characterized interaction between the C-terminal region of Sir3 and the histone H3/H4 tails, suggest that Sir3 utilizes multiple domains to interact with nucleosomes.
机译：Sir3是酵母（Saccharomyces cerevisiae）中转录沉默复合物的组成部分，其N端BAH结构域对蛋白质的沉默功能至关重要。先前的工作表明，Sir3（Ala2）的N末端丙氨酸残基及其乙酰化在沉默中起重要作用。在这里我们显示，Sir3 Ala2突变体的沉默缺陷可以通过组蛋白H3和H4的突变，特别是H3 D77N和H4 H75Y突变来抑制。此外，突变分析表明，Sir3 BAH结构域的三个独立区域对其沉默具有重要作用。许多这些BAH突变也可以被H3 D77N和H4 H75Y突变抑制。与其他研究结果一致，体外实验表明，Sir3 BAH结构域可与部分纯化的核小体相互作用。沉默缺陷的BAH突变体对于这种相互作用是有缺陷的。这些结果以及Sir3的C末端区域和组蛋白H3 / H4尾巴之间先前表征的相互作用，表明Sir3利用多个域与核小体相互作用。

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