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AP-site cleavage activity of tyrosyl-DNA phosphodiesterase 1
Authors:Lebedeva Natalia A  Rechkunova Nadejda I  Lavrik Olga I
Institution:SB RAS Institute of Chemical Biology and Fundamental Medicine, Novosibirsk, Russia.
Abstract:APE-independent base excision repair (BER) pathway plays an important role in the regulation of DNA repair mechanisms. In this study it has been found that recently discovered tyrosyl-DNA phosphodiesterase 1 (Tdp1) catalyzes the AP site cleavage reaction to generate breaks with the 3'- and 5'-phosphate termini. The removal of the 3'-phosphate is performed by polynucleotide kinase phosphatase (PNKP). Tdp1 is known to interact stably with BER proteins: DNA polymerase beta (Pol β), XRCC1, PARP1 and DNA ligase III. The data suggest a role of Tdp1 in the new APE-independent BER pathway in mammals.
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