A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?
A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?
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DOI：
10.1016/s0968-0004(02)02058-3
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发表时间：
2002-03-01
影响因子：
13.8
通讯作者：
Chinenov, Y
中科院分区：
文献类型：
--
作者：
Chinenov, Y
一个新的与Elp3相关的双结构域组蛋白乙酰转移酶（HATS）亚家族已经被发现。除了在C端有一个HAT结构域外，这些蛋白还有一个类似于s -腺苷蛋氨酸自由基酶的催化结构域的n端结构域。进化过程中保留了两域结构，这表明两种酶活性在功能或机制上是耦合的，并指向高度保守的底物。讨论了这种相似性的功能含义以及elp3相关蛋白作为组蛋白去甲基化酶的可能作用。
A new subfamily of two-domain histone acetyltransferases (HATS) related to Elp3 has been identified. In addition to a HAT domain in the C terminus, these proteins have an N-terminal domain similar to the catalytic domain of S-adenosylmethionine radical enzymes. Two-domain organization is preserved in evolution, suggesting that both enzymatic activities are functionally or mechanistically coupled and directed towards highly conserved substrates. The functional implications of this similarity and a possible role for Elp3-related proteins as histone demethylases are discussed.