A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?
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.
Chinenov
Yurii
Y
Howard Hughes Medical Institute, University of Michigan Medical Center, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-0650, USA. yurii@umich.edu
D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D020134:Catalytic Domain / Q000502:physiology*; D051548:Histone Acetyltransferases; D006657:Histones / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008745:Methylation; D008969:Molecular Sequence Data; D005810:Multigene Family; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid
D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases