Elp3组蛋白乙酰转移酶中的第二个催化结构域：组蛋白去甲基化酶活性的候选者？

A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?

作者信息

Chinenov Yurii

机构信息

Howard Hughes Medical Institute, University of Michigan Medical Center, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-0650, USA.

出版信息

Trends Biochem Sci. 2002 Mar;27(3):115-7. doi: 10.1016/s0968-0004(02)02058-3.

DOI:10.1016/s0968-0004(02)02058-3

PMID:11893502

Abstract

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.

摘要

已鉴定出一个与Elp3相关的两结构域组蛋白乙酰转移酶（HAT）新亚家族。除了C末端的HAT结构域外，这些蛋白质还有一个与S-腺苷甲硫氨酸自由基酶催化结构域相似的N末端结构域。两结构域组织在进化过程中得以保留，这表明两种酶活性在功能上或机制上相互关联，并作用于高度保守的底物。本文讨论了这种相似性的功能意义以及Elp3相关蛋白作为组蛋白去甲基化酶的可能作用。