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 O-6-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. (C) 1999 Federation of European Biochemical Societies.
Publisher
ELSEVIER SCIENCE BV
Issue Date
1999-04
Language
ENG
Keywords

STRAND BREAKS; CIS-SYN; POLYMERASE; IDENTIFICATION; ACTIVATION; INVITRO; REPAIR; NICKS

Citation

FEBS LETTERS, v.449, no.1, pp.33 - 35

ISSN
0014-5793
URI
http://hdl.handle.net/10203/74780
Appears in Collection
BS-Journal Papers(저널논문)
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