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Characterization of a lysine-specific histone demethylase from Arabidopsis thaliana

机译：拟南芥赖氨酸特异性组蛋白脱甲基酶的表征

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摘要

Arabidopsis thaliana has four genes with close homology to human histone H3 lysine 4 demethylase (HsLSD1), a component of various transcriptional corepressor complexes that often also contain histone deacetylases and the corepressor protein CoREST. All four Arabidopsis proteins contain a flavin amine oxidase domain and a SWIRM domain, the latter being present in a number of proteins involved in chromatin regulation. Here, we describe the heterologous expression and biochemical characterization of one of these Arabidopsis proteins (AtLSD1) and show that, similarly to HsLSD1, it has demethylase activity toward mono- and dimethylated Lys4 but not dimethylated Lys9 and Lys27 of histone 3. Modeling of the AtLSD1 three-dimensional structure using the HsLSD1 crystal structure as a template revealed a high degree of conservation of the residues building up the active site and some important differences. Among these differences, the most prominent is the lack of the HsLSD1 Tower domain, which has been shown to interact with CoREST and to be indispensable for HsLSD1 demethylase activity. This observation, together with AtLSD1 peculiar surface electrostatic potential distribution, suggests that the molecular partners of AtLSD1 are probably different from those of the human orthologue.
机译：拟南芥具有四个与人组蛋白H3赖氨酸4去甲基化酶（HsLSD1）紧密同源的基因，后者是各种转录共核心蛋白复合物的组成部分，通常还含有组蛋白脱乙酰基酶和共核心蛋白CoREST。所有四种拟南芥蛋白均含有黄素胺氧化酶结构域和SWIRM结构域，后者存在于许多涉及染色质调节的蛋白中。在这里，我们描述了这些拟南芥蛋白之一（AtLSD1）的异源表达和生化特征，并表明，与HsLSD1相似，它对组蛋白3的单和二甲基化Lys4具有去甲基化酶活性，但对二甲基化Lys9和Lys27不具有二甲基化活性。使用HsLSD1晶体结构作为模板的AtLSD1三维结构显示了高度保留的残基，这些残基构成了活性位点，并且存在一些重要差异。在这些差异中，最突出的是缺少HsLSD1塔结构域，该结构域已显示与CoREST相互作用并且对于HsLSD1脱甲基酶活性是必不可少的。该观察结果与AtLSD1特有的表面静电势分布一起表明，AtLSD1的分子伴侣可能与人类直系同源物的分子伴侣不同。

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