Inhibition of poly(ADP-ribose)polymerase binding to DNA by thymidine dimer.
The ability of poly(ADP-ribose)polymerase to bind damaged DNA was assessed by electrophoretic mobility shift assay. DNA binding domain of poly(ADP-ribose)polymerase (PARPDBD) binds to synthetic deoxyribonucleotide duplex 10-mer. However, the synthetic deoxyribonucleotide duplex containing cys-syn thymidine dimer which produces the unwinding of DNA helix structure lost its affinity to PARPDBD. It was shown that the binding of PARPDBD to the synthetic deoxyribonucleotide duplex was not affected by O6-Me-dG which causes only minor distortion of DNA helix structure. This study suggests that the stabilized DNA helix structure is important for poly(ADP-ribose)polymerase binding to DNA breaks, which are known to stimulate catalytic activity of poly(ADP-ribose)polymerase.
Yang
W S
WS
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejon, South Korea.
Kim
J W
JW
Lee
J H
JH
Choi
B S
BS
Joe
C O
CO
D004247:DNA / Q000378:metabolism; D019281:Dimerization; D009838:Oligodeoxyribonucleotides / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013936:Thymidine
D009838:Oligodeoxyribonucleotides; D011993:Recombinant Fusion Proteins; D004247:DNA; D011065:Poly(ADP-ribose) Polymerases; D013936:Thymidine