研究组蛋白修饰的化学方法。
Chemical approaches for studying histone modifications.
机构信息
Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA.
出版信息
J Biol Chem. 2010 Apr 9;285(15):11045-50. doi: 10.1074/jbc.R109.080291. Epub 2010 Feb 10.
Abstract
Histones form the protein core around which genomic DNA is wrapped in eukaryotic chromatin. Numerous genetic studies have established that the structure and transcriptional state of chromatin are closely related to histone post-translational modifications. Further elucidation of the precise mechanistic roles for individual histone modifications requires the ability to isolate and study homogeneously modified histones. However, the highly heterogeneous nature of histone modifications in vivo poses a significant challenge for such studies. Chemical tools that have enabled biochemical and biophysical studies of site-specifically modified histones are the focus of this minireview.
摘要
组蛋白形成了真核染色质中基因组 DNA 缠绕的蛋白核心。大量的遗传学研究已经确立，染色质的结构和转录状态与组蛋白的翻译后修饰密切相关。要进一步阐明单个组蛋白修饰的确切机制作用，就需要能够分离和研究同质修饰的组蛋白。然而，组蛋白修饰在体内的高度不均一性对这类研究提出了重大挑战。本文综述了能够实现特异性修饰组蛋白的生化和生物物理研究的化学工具。
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