探索组蛋白伴侣的作用机制。
Towards a mechanism for histone chaperones.
作者信息
Elsässer Simon J, D'Arcy Sheena
机构信息
Laboratory of Chromatin Biology and Epigenetics, The Rockefeller University, Box 374, 1230 York Ave, New York, NY 10065, USA.
Howard Hughes Medical Institute, Colorado State University, Fort Collins CO 80523, USA; Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins CO 80523, USA.
出版信息
Biochim Biophys Acta. 2013 Mar-Apr;1819(3-4):211-221. doi: 10.1016/j.bbagrm.2011.07.007.
Histone chaperones can be broadly defined as histone-binding proteins that influence chromatin dynamics in an ATP-independent manner. Their existence reflects the importance of chromatin homeostasis and the unique and unusual biochemistry of the histone proteins. Histone supply and demand at chromatin is regulated by a network of structurally and functionally diverse histone chaperones. At the core of this network is a mechanistic variability that is only beginning to be appreciated. In this review, we highlight the challenges in determining histone chaperone mechanism and discuss possible mechanisms in the context of nucleosome thermodynamics. We discuss how histone chaperones prevent promiscuous histone interactions, and consider if this activity represents the full extent of histone chaperone function in governing chromatin dynamics. This article is part of a Special Issue entitled: Histone chaperones and Chromatin assembly.
组蛋白伴侣可广义地定义为以不依赖ATP的方式影响染色质动态变化的组蛋白结合蛋白。它们的存在反映了染色质稳态的重要性以及组蛋白独特而非同寻常的生物化学性质。染色质上组蛋白的供需由结构和功能多样的组蛋白伴侣网络调控。该网络的核心是一种刚刚开始被认识到的机制变异性。在本综述中，我们强调了确定组蛋白伴侣机制所面临的挑战，并在核小体热力学的背景下讨论了可能的机制。我们讨论了组蛋白伴侣如何防止组蛋白的随意相互作用，并思考这种活性是否代表了组蛋白伴侣在调控染色质动态变化中的全部功能。本文是名为“组蛋白伴侣与染色质组装”的特刊的一部分。
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