St-Patrick Research Group in Basic Oncology, Laval University Cancer Research Center, Centre de Recherche du CHU de Québec-Axe Oncologie, Hôtel-Dieu de Québec, Quebec City, Quebec G1R 2J6, Canada.
Genes Dev. 2014 May 15;28(10):1029-41. doi: 10.1101/gad.236331.113.
Histone modifiers like acetyltransferases, methyltransferases, and demethylases are critical regulators of most DNA-based nuclear processes, de facto controlling cell cycle progression and cell fate. These enzymes perform very precise post-translational modifications on specific histone residues, which in turn are recognized by different effector modules/proteins. We now have a better understanding of how these enzymes exhibit such specificity. As they often reside in multisubunit complexes, they use associated factors to target their substrates within chromatin structure and select specific histone mark-bearing nucleosomes. In this review, we cover the current understanding of how histone modifiers select their histone targets. We also explain how different experimental approaches can lead to conflicting results about the histone specificity and function of these enzymes.
组蛋白修饰酶（如乙酰转移酶、甲基转移酶和去甲基酶）是大多数基于 DNA 的核过程的关键调控因子，实际上控制着细胞周期进程和细胞命运。这些酶在特定的组蛋白残基上进行非常精确的翻译后修饰，进而被不同的效应模块/蛋白识别。我们现在对这些酶如何表现出这种特异性有了更好的理解。由于它们通常存在于多亚基复合物中，它们使用相关因子在染色质结构中靶向其底物，并选择特定的组蛋白标记核小体。在这篇综述中，我们介绍了目前对组蛋白修饰酶如何选择其组蛋白靶标的理解。我们还解释了不同的实验方法如何导致关于这些酶的组蛋白特异性和功能的相互矛盾的结果。
