Association of DFF40 with chromatin

Direct interactions between the histone H1 C-terminal domain and DFF40/CAD possibly target the nuclease to chromatin linker DNA promoting the linker DNA cleavage during the terminal stages of apoptosis (Widlak et al., 2005). Noteworthy, it has been reported that DFF40/DFF45 complexes could also associate with chromatin and be activated with caspase-3 in DNA-bound state (Korn et al., 2005).

直接相互作用于组蛋白H1的C端结构域与DFF40/CAD，可能靶向核酸酶至染色质连接DNA，从而在细胞凋亡的终末阶段促进连接DNA的切割（Widlak等，2005年）。值得注意的是，已有研究报道DFF40/DFF45复合物亦能结合染色质，并在DNA结合状态下被caspase-3激活（Korn等，2005年）。