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FNNyFLIUE pvRcOMIKaQ MMocxMbUp GvYaGGwNMq PARP-1 has a highly conserved structural and functional organization with multidomains ().The N-terminal DNA binding domain (DBD) contains three zinc fingers (ZnF1–3), a nuclear localization signal (NLS), and a caspase cleavage site (Kaufmann et al., 1993).Two zinc fingers (ZnF1–2) allow PARP-1 to bind DNA strand breaks (D’Amours et al., 1999) and trigger catalytic activity. JUmuntukOhk ATM serine/threonine kinase, symbol ATM, is a serine/threonine protein kinase that is recruited and activated by DNA double-strand breaks.It phosphorylates several key proteins that initiate activation of the DNA damage checkpoint, leading to cell cycle arrest, DNA repair or apoptosis.Several of these targets, including p53, CHK2, BRCA1, NBS1 and H2AX are tumor suppressors. 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