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PMID: 11893502 Published · ppublish English Journal Article Review

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

Trends in biochemical sciences ·Vol. 27 ·No. 3 ·2002-03-00 ·Pages 115-7

Chinenov Y

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.

MeSH Terms
Acetyltransferases/chemistry,genetics,metabolism Amino Acid Sequence Animals Binding Sites Catalysis Catalytic Domain/physiology Histone Acetyltransferases Histones/chemistry,metabolism Humans Methylation Molecular Sequence Data Multigene Family Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid
Chemicals
Histones Saccharomyces cerevisiae Proteins Acetyltransferases Histone Acetyltransferases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Chinenov Yurii
Howard Hughes Medical Institute, University of Michigan Medical Center, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-0650, USA. [email protected]
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
2002-03-00
Pages
115-7
Language
English
Region
England
NLM ID
7610674
Subset
IM
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