Eberharter Anton, Ferreira Roger, Becker Peter
Adolf-Butenandt-Institut, Abt. Molekularbiologie, Universität München, Schillerstr. 44, D-80336 München, Germany.
Biol Chem. 2005 Aug;386(8):745-51. doi: 10.1515/BC.2005.087.
The flexibility of chromatin that enables translation of environmental cues into changes in genome utilisation, relies on a battery of enzymes able to modulate chromatin structure in a highly targeted and regulated manner. The most dynamic structural changes are brought about by two kinds of enzymes with different functional principles. Changes in the acetylation status of histones modulate the folding of the nucleosomal fibre. The histone-DNA interactions that define the nucleosome itself can be disrupted by ATP-dependent remodelling factors. This review focuses on recent developments that illustrate various strategies for integrating these disparate activities into complex regulatory schemes. Synergies may be brought about by consecutive or parallel action during the stepwise process of chromatin opening or closing. Tight co-ordination may be achieved by direct interaction of (de-)acetylation enzymes and remodelling ATPases or even permanent residence within the same multi-enzyme complex. The fact that remodelling ATPases can be acetylated by histone acetyltransferases themselves suggests exciting possibilities for the co-ordinate modulation of chromatin structure and remodelling enzymes.
染色质的灵活性使其能够将环境信号转化为基因组利用的变化，这依赖于一系列能够以高度靶向和调控的方式调节染色质结构的酶。最动态的结构变化是由两种具有不同功能原理的酶引起的。组蛋白乙酰化状态的变化调节核小体纤维的折叠。定义核小体本身的组蛋白 - DNA相互作用可被ATP依赖性重塑因子破坏。本综述重点关注最近的进展，这些进展阐明了将这些不同活动整合到复杂调控方案中的各种策略。在染色质打开或关闭的逐步过程中，连续或并行作用可能会产生协同作用。（去）乙酰化酶与重塑ATP酶的直接相互作用，甚至在同一多酶复合物中的永久存在，都可以实现紧密协调。重塑ATP酶本身可被组蛋白乙酰转移酶乙酰化这一事实，为染色质结构和重塑酶的协同调节提供了令人兴奋的可能性。
