Histone acetyltransferase
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histone acetyltransferase 1
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| Identifiers | |
| Symbol | HAT1 |
| HUGO | 4821 |
| Entrez | 8520 |
| OMIM | 603053 |
| RefSeq | NM_003642 |
| UniProt | O14929 |
| Other data | |
| EC number | 2.3.1.48 |
| Locus | Chr. 2 q31.2-33.1 |
Histone acetyltransferases (HAT) are enzymes that acetylate conserved lysine amino acids on histone proteins by transferring an acetyl group from acetyl CoA to lysine to form ε-N-acetyl lysine.
Histone acetylation is generally linked to transcriptional activation. These are generally associated with euchromatin. Initially, it was thought that acetylation of lysine neutralizes the positive charge normally present, thus reducing affinity between histone and (negatively charged) DNA which renders DNA more accessible to transcription factors. More recently, it has emerged that lysine acetylation and other posttranslational modifications of histones generate binding sites for specific protein-protein interaction domains, such as the acetyl-lysine binding bromodomain.
[edit] See also
- Histone deacetylase
- Histone methyltransferase
- RNA polymerase control by chromatin structure
- Acetyltransferase
[edit] External links
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Carnitine O-palmitoyltransferase - Glyceronephosphate O-acyltransferase - Lecithin-cholesterol acyltransferase - Citrate synthase
Acetyltransferases: Beta-galactoside transacetylase - Choline acetyltransferase - Chloramphenicol acetyltransferase - Histone acetyltransferase (P300/CBP)- N-Acetylglutamate synthase -
Serotonin N-acetyl transferase
Aminoacyltransferases: Peptidyl transferase - Transglutaminase (Tissue transglutaminase, Factor XIII)
