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A second catalytic domain in the Elp3 histone acetyltransferases: a candidate for histone demethylase activity?
- Source :
-
Trends in biochemical sciences [Trends Biochem Sci] 2002 Mar; Vol. 27 (3), pp. 115-7. - Publication Year :
- 2002
-
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.
- Subjects :
- Acetyltransferases genetics
Amino Acid Sequence
Animals
Binding Sites
Catalysis
Histone Acetyltransferases
Histones chemistry
Histones metabolism
Humans
Methylation
Molecular Sequence Data
Multigene Family
Sequence Homology, Amino Acid
Acetyltransferases chemistry
Acetyltransferases metabolism
Catalytic Domain physiology
Saccharomyces cerevisiae Proteins
Subjects
Details
- Language :
- English
- ISSN :
- 0968-0004
- Volume :
- 27
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Trends in biochemical sciences
- Publication Type :
- Academic Journal
- Accession number :
- 11893502
- Full Text :
- https://doi.org/10.1016/s0968-0004(02)02058-3