Histone acetyltransferase
From Proteopedia
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== Function == | == Function == | ||
'''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>. | '''Histone acetyltransferase''' (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation<ref>PMID:11395403</ref>. | ||
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| + | See also [[Histone acetyltransferase 1-2 Complex (HAT1/2)]]. | ||
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| + | *'''Histone acetyltransferase P300''' acetylates all 4 core histones in nucleosomes and also non-histone targets. | ||
== Relevance == | == Relevance == | ||
Current revision
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References
- ↑ Roth SY, Denu JM, Allis CD. Histone acetyltransferases. Annu Rev Biochem. 2001;70:81-120. PMID:11395403 doi:10.1146/annurev.biochem.70.1.81
- ↑ Dekker FJ, van den Bosch T, Martin NI. Small molecule inhibitors of histone acetyltransferases and deacetylases are potential drugs for inflammatory diseases. Drug Discov Today. 2014 May;19(5):654-60. doi: 10.1016/j.drudis.2013.11.012. Epub, 2013 Nov 21. PMID:24269836 doi:http://dx.doi.org/10.1016/j.drudis.2013.11.012
- ↑ Van Beekum O, Kalkhoven E. Aberrant forms of histone acetyltransferases in human disease. Subcell Biochem. 2007;41:233-62. PMID:17484131
- ↑ Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V. Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily. Cell. 1998 Aug 21;94(4):427-38. PMID:9727486
