Linked Life Data

48887BiochemicalReaction2229

Source:http://www.reactome.org/biopax/48887BiochemicalReaction2229

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Authored: Matthews, L, 2003-09-07 08:47:00, Presumably the proteins must be released from the DNA prior to end joining but precisely when this step occurs is not known. Mg-ATP and the protein kinase activity of DNA-PKcs are required for repair of DNA double strand breaks (Kurimasa et al, 1999; Kienker et al, 2000; Baumann and West, 1998). In vitro, DNA-PK undergoes autophosphorylation which correlates with loss of protein kinase activity and disruption of the DNA-PKcs-Ku-DNA complex (Chan and Lees-Miller, 1996; Douglas et al, 2001; 2002; Merkle et al, 2002). Moreover, autophosphorylation of DNA-PKcs is required for NHEJ in vivo (Chan et al, 2002; Ding et al, 2003), suggesting that autophosphorylation may serve as a mechanism to remove DNA-PKcs from DNA prior to end joining.
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Removal of repair proteins and ligation of the processed ends of the DNA double-strand break
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