Inhibition of poly(ADP‐ribose)polymerase binding to DNA by thymidine dimer

FEBS Letters

Lee, Joon-Hwa¹  Yang, Wan Seok²  Joe, Cheol O.²  Kim, Jin Woo²  Choi, Byong-Seok¹ 

[1] Department of Chemistry, Korea Advanced Institute of Science and Technology, Taejon 305-701, South Korea;Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejon 305-701, South Korea

关键词: Poly(ADP-ribose)polymerase;    Thymidine dimer;    DNA binding;   

DOI  :  10.1016/S0014-5793(99)00391-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown