Nady Nataliya, Min Jinrong, Kareta Michael S, Chédin Frédéric, Arrowsmith Cheryl H
Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, Ontario, M5G 1L7, Canada.
Trends Biochem Sci. 2008 Jul;33(7):305-13. doi: 10.1016/j.tibs.2008.04.014. Epub 2008 Jun 4.
Post-translational modifications of histones serve as docking sites and signals for effector proteins and chromatin-remodeling enzymes, thereby influencing many fundamental cellular processes. Nevertheless, there are huge gaps in the knowledge of which proteins read and write the 'histone code'. Several techniques have been used to decipher complex histone-modification patterns. However, none is entirely satisfactory owing to the inherent limitations of in vitro studies of histones, such as deficits in the knowledge of the proteins involved, and the associated difficulties in the consistent and quantitative generation of histone marks. An alternative technique that could prove to be a useful tool in the study of the histone code is the use of synthetic peptide arrays (SPOT blot analysis) as a screening approach to characterize macromolecules that interact with specific covalent modifications of histone tails.
组蛋白的翻译后修饰充当效应蛋白和染色质重塑酶的停靠位点及信号,从而影响许多基本的细胞过程。然而,在识别和书写“组蛋白密码”的蛋白质知识方面存在巨大差距。已经使用了几种技术来破译复杂的组蛋白修饰模式。然而,由于组蛋白体外研究的固有局限性,例如对所涉及蛋白质的了解不足,以及在一致且定量地生成组蛋白标记方面存在相关困难,没有一种技术是完全令人满意的。一种可能被证明是研究组蛋白密码有用工具的替代技术是使用合成肽阵列(斑点印迹分析)作为筛选方法,以表征与组蛋白尾部特定共价修饰相互作用的大分子。