| Type: | Domain | Name: | Histone acetyltransferase domain, MYST-type |
| Description: | Histone acetyltransferases (HATs) fall into at least four different families based on sequence conservation within the HAT domain []. The MYST family is the largest family of HATs and is named after the founding members: MOZ, Ybf2/ Sas3, Sas2 and Tip60. MYST proteins mediate many biological functions including gene regulation, DNA repair, cell-cycle regulation and development [] and have been shown to acetylate several non-histone substrates []. MYST proteins are autoregulated by posttranslational modifications [].The MYST-type HAT domain contains three regions: a central region associated with acetyl-CoA cofactor binding and catalysis in addition to flanking N- andC-terminal regions harboring respectively a C2HC-type zinc finger and a helix- turn-helix DNA-binding motif. The N- and C-terminal segmentsdirectly flanking the catalytic core are likely to play an important role in histone substrate binding [, ]. The catalytic mechanism for the MYST-type HAT domain is still unresolved but seems to involve a conserved glutamate that functions to abstract a proton from lysine to promote the nucleophilic attack on the acetyl carbonyl carbon of acetyl-CoA [, , , ]. | Short Name: | HAT_MYST-type |
