New perspectives for the regulation of acetyltransferase MOF.
New perspectives for the regulation of acetyltransferase MOF.
复制标题
DOI：
10.4161/epi.5.3.11372
复制
发表时间：
2010-04
期刊：
影响因子：
3.7
通讯作者：
Dou Y
中科院分区：
文献类型：
--
作者：
Li X;Dou Y
在高等真核生物中，组蛋白乙酰转移酶（MOF）是使组蛋白H4赖氨酸16乙酰化的主要酶，赖氨酸16是与染色质去浓缩相关的普遍标记。最近的研究表明，MOF存在于两个不同但进化上保守的复合物MSL和MOF- msl1v1中。尽管这两种MOF复合物在组蛋白H4 K16上具有不可区分的活性，但它们在乙酰化非组蛋白底物p53方面存在显著差异。这些复合物中MOF活性的调控仍然难以捉摸。鉴于MOF的进化保守性以及H4 K16乙酰化在维持高阶染色质结构中的重要性，了解MOF的功能和调控具有重要意义。在这里，我们讨论了两种MOF复合物的关键差异，这些差异可能揭示了它们不同的乙酰转移酶活性的调节。我们还讨论了两种MOF复合物与不同组蛋白甲基转移酶复合物在转录调控中的协调功能。
In higher eukaryotes, histone acetyltransferase MOF (male absent on the first) is the major enzyme that acetylates histone H4 lysine 16, a prevalent mark associated with chromatin decondensation. Recent studies show that MOF resides in two different but evolutionarily conserved complexes, MSL and MOF-MSL1v1. Although these two MOF complexes have indistinguishable activity on histone H4 K16, they differ dramatically in acetylating non-histone substrate p53. The regulation of MOF activity in these complexes remains elusive. Given the evolution conservation of MOF and the importance of H4 K16 acetylation in maintaining higher order chromatin structures, understanding the function and regulation of MOF bears great significance. Here, we discussed the key differences in two MOF complexes that may shed light on the regulation of their distinct acetyltransferase activities. We also discussed coordinated functions of two MOF complexes with different histone methyltransferase complexes in transcription regulation.