First Author | Chinenov Y | Year | 2002 |
Journal | Trends Biochem Sci | Volume | 27 |
Issue | 3 | Pages | 115-7 |
PubMed ID | 11893502 | Mgi Jnum | J:75354 |
Mgi Id | MGI:2176369 | Doi | 10.1016/s0968-0004(02)02058-3 |
Citation | Chinenov Y (2002) A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?. Trends Biochem Sci 27(3):115-7 |
abstractText | 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. |