Dyson M H, Rose S, Mahadevan L C
Nuclear Signalling Laboratory, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Front Biosci. 2001 Aug 1;6:D853-65. doi: 10.2741/dyson.
Acetylated histones are generally associated with active chromatin. The bromodomain has recently been identified as a protein module capable of binding to acetylated lysine residues, and hence is able to mediate the recruitment of factors to acetylated chromatin. Functional studies of bromodomain-containing proteins indicate how this domain contributes to the activity of a number of nuclear factors including histone acetyltransferases and chromatin remodelling complexes. Here, we review the characteristics of acetyllysine-binding by bromodomains, discuss associated domains found in these proteins, and address the function of the bromodomain in the context of chromatin. Finally, the modulation of bromodomain binding by neighbouring post-translational modifications within histone tails might provide a mechanism through which combinations of covalent marks could exert control on chromatin function.
乙酰化组蛋白通常与活性染色质相关。最近，溴结构域被鉴定为一种能够结合乙酰化赖氨酸残基的蛋白质模块，因此能够介导因子向乙酰化染色质的募集。对含溴结构域蛋白的功能研究表明了该结构域如何对包括组蛋白乙酰转移酶和染色质重塑复合物在内的多种核因子的活性产生影响。在这里，我们综述了溴结构域结合乙酰赖氨酸的特性，讨论了这些蛋白质中发现的相关结构域，并阐述了溴结构域在染色质环境中的功能。最后，组蛋白尾部相邻的翻译后修饰对溴结构域结合的调节可能提供了一种机制，通过这种机制，共价标记的组合可以对染色质功能施加控制。
