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Global Control of Histone Modification by the Anaphase-Promoting Complex

机译：后期促进复合物对组蛋白修饰的全局控制

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Acetylation and phosphorylation of the amino-terminal tails of the core histones fluctuate on a global scale in concert with other major events in chromosome metabolism. A ubiquitin ligase, the anaphase-promoting complex (APC), controls events in chromosome metabolism such as sister chromatid cohesion and may regulate H3 phosphorylation by targeting Aurora A, one of several S10-directed H3 kinases in vertebrate cells, for destruction by the proteasome. Our analysis of apc10Δ and apc11ts loss-of-function mutants reveals that the APC controls the global level of H3 S10 phosphorylation in cycling yeast cells. Surprisingly, it also regulates dephosphorylation of H3 and global deacetylation of H2B, H3, and H4 during exit from the cell cycle into G0. Genetic, biochemical, and microarray analyses suggest that APC-dependent cell cycle control of H3 phosphorylation is exerted at the level of an Aurora H3 kinase, Ipl1p, while APC-dependent transcriptional induction of GLC7, an essential H3 phosphatase, contributes to sustained H3 dephosphorylation upon cell cycle withdrawal. Collectively, our results establish that core histone acetylation state and H3 phosphorylation are physiologically regulated by the APC and suggest a model in which global reconfiguration of H3 phosphorylation state involves APC-dependent control of both an H3 kinase and a conserved phosphatase.
机译：核心组蛋白氨基末端的乙酰化和磷酸化与染色体代谢中的其他主要事件一致地在全球范围内波动。泛素连接酶，即后期促进复合物（APC），控制染色体代谢中的事件，例如姐妹染色单体凝聚，并可能通过靶向Aurora A（脊椎动物细胞中几种S10定向H3激酶之一）来破坏H3磷酸化，从而被蛋白酶体破坏。 。我们对apc10Δ和 apc11 ts 功能丧失突变体的分析揭示，APC控制着循环酵母细胞中H3 S10磷酸化的整体水平。出人意料的是，它还调节细胞周期退出G 0 期间H3的去磷酸化和H2B，H3和H4的整体脱乙酰化。遗传，生化和微阵列分析表明，APC依赖的H3磷酸化的细胞周期控制是在Aurora H3激酶Ipl1p的水平上进行的，而APC依赖的 GLC7 的转录诱导则是必需的H3。磷酸酶有助于细胞周期退出后持续的H3脱磷酸作用。总的来说，我们的研究结果确定核心组蛋白乙酰化状态和H3磷酸化受APC生理调节，并提出了一个模型，其中H3磷酸化状态的整体重配置涉及H3激酶和保守的磷酸酶的APC依赖性控制。

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