Elucidation of constructing and working mechanisms of histone modification network

我们以前的组蛋白修饰理论认为，多种组蛋白修饰之间的相互控制形成了复杂的组蛋白修饰网络。本研究利用芽殖酵母的组蛋白点突变文库，将组蛋白可修饰残基的点突变引起的网络异常作为表型变化进行了全面的研究，以阐明该网络是如何在活细胞中构建和工作的。因此，组蛋白H3-Lys 4，-Lys 36和组蛋白H4-Lys 12，-Lys 16被鉴定为作为“功能枢纽”的可修饰残基，其在维持生物学功能中起重要作用。

Our previous theory on histone modifications suggested that mutual controls among a wide variety of histone modifications form complex histone modification network. In this study, to elucidate how the network is built and working in iving cells, the aberrances of the network caused by the point mutation of histone modifiable residues were comprehensively examined as phenotypic changes using the histone point-mutant library of the budding yeast. As a result, histone H3-Lys4, -Lys36 and histone H4-Lys12, -Lys16 were identified as modifiable residues working as "functional hubs", which play an important role in the maintenance of biological functions.