| A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity? |
| |
| 引用本文： | Chinenov Y. A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?[J]. Trends in biochemical sciences, 2002, 27(3): 115-117. DOI: 10.1016/S0968-0004(02)02058-3 |
| |
| 作者姓名： | Chinenov Y |
| |
| 摘 要： |
|
A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity? |
| |
| Chinenov Yurii. A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?[J]. Trends in biochemical sciences, 2002, 27(3): 115-117. DOI: 10.1016/S0968-0004(02)02058-3 |
| |
| Authors: | Chinenov Yurii |
| |
| Affiliation: | Howard Hughes Medical Institute, University of Michigan Medical Center, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-0650, USA. yurii@umich.edu |
| |
| 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. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ |
