Abstract
Recently we present the evidence for novel roles of histone acetylases. The TIP60 histone acetylase is purified as a multimeric protein complex. This complex has a RuvB homologue which has a role in DNA recombinational repair in E.coli. Ectopic expression of mutated TIP60 lacking histone acetylase activity results in cells with defective double-strand DNA break repair. Importantly, the resulting cells lose their apoptotic competence , suggesting a defect in the cells' ability to signal the existence of DNA damage to the apoptotic machinery. These results indicate that the histone acetylase TIP60-containing complex plays a role in DNA repair and apoptosis. We present here that how the histone acetylase TIP60-containing complex is involved in DNA damaged repair. Recently, we purified the TIP60 complex after DNA damage and revealed that TIP60 complex come to have a g-H2AX after DNA damage. Interestingly we also cleared that histone acetylase of TIP60 complex is required for the phosphorylation of H2AX. [J Radiat Res 44:410 (2003)]
