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

Cited 0 time in webofscience Cited 0 time in scopus
  • Hit : 260
  • Download : 0
DC FieldValueLanguage
dc.contributor.authorYang, Wan Seok-
dc.contributor.authorKim, Jin Woo-
dc.contributor.authorLee, Joon-Hwa-
dc.contributor.authorChoi, Byong-Seok-
dc.contributor.authorJoe, Cheol O.-
dc.date.accessioned2011-09-19T01:17:21Z-
dc.date.available2011-09-19T01:17:21Z-
dc.date.issued1999-04-16-
dc.identifier.citationFEBS Letters, Vol.449, pp.33-35en
dc.identifier.issn0014-5793-
dc.identifier.urihttp://hdl.handle.net/10203/25217-
dc.description.abstractThe 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.en
dc.description.sponsorshipThis work was supported by a grant from Science Research Center for Cell Di¡erentiation, Seoul National University, a grant from Ministry of Science and Technology and a grant from Korea Research Foundation, Republic of Korea.en
dc.language.isoen_USen
dc.publisherElsevieren
dc.subjectPoly(ADP-ribose)polymeraseen
dc.subjectThymidine dimeren
dc.subjectDNA bindingen
dc.titleInhibition of poly(ADP-ribose)polymerase binding to DNA by thymidine dimer.en
dc.typeArticleen
Appears in Collection
BS-Journal Papers(저널논문)

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0