Localization | Comment | Organism | GeneOntology No. | Textmining |
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Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 acetyl-CoA + histone H4 | Saccharomyces cerevisiae | - |
4 CoA + tetraacetylhistone H4 | NuA4 randomly acetylates free and nucleosomal H4, with a small preference for lysines 5, 8, and 12 over 16 | ? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
yeast piccolo NuA4 complex | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine | non-processive mechanism, where the NuA4 histone acetyltransferasecomplex dissociates from substrate after each acetylation event | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 acetyl-CoA + histone H4 | - |
Saccharomyces cerevisiae | 4 CoA + tetraacetylhistone H4 | NuA4 randomly acetylates free and nucleosomal H4, with a small preference for lysines 5, 8, and 12 over 16 | ? | |
additional information | removal of lysine residues does not substantially affect the ability of NuA4 histone actyltransferase complex to acetylate remaining sites, and insertion of an additional lysine into the substrate histone H4 tail leads to rapid quintuple-acetylation. Conversion of the native histone H2A tail to an H4-like sequence results in enhanced multi-site acetylation. NuA4's site selectivity is dictated by accessibility on the nucleosome surface, the relative proximity from the histone fold domain, and a preference for intervening glycine residues with a minimal (n + 2) spacing between lysines | Saccharomyces cerevisiae | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Esa1 | component of the NuA4 histone acetyltransferase complex | Saccharomyces cerevisiae |