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PROBING PHOTODYNAMIC DAMAGE IN NUCLEIC ACIDS WITH A DAMAGE-SPECIFIC DNA BINDING PROTEIN: A COMPARISON OF THE B and Z DNA CONFORMATIONS
Authors:Ross S.  Feldberg Caroline  Brown Josephine A.  Carew Judith L.  Lucas
Affiliation:Department of Biology, Tufts University, Medford, MA 02155, USA
Abstract:—We have employed a damage-specific DNA binding protein from human cells as a probe for base damage in polymers irradiated with white light in the presence of methylene blue. Protein-recognizable damage is introduced only into guanine-containing polymers and quenching of damage introduction by H2O and sodium azide suggest the involvement of a singlet oxygen mechanism. Using poly d(G-m5C), we have demonstrated that the left-handed double helical Z conformation is much less susceptible to guanine photooxidation than is the usual B conformation. We speculate that this difference in reactivity may reflect steric hindrance at the purine C-4 position and could provide some insight into the initial steps of the reaction between singlet oxygen and guanine in nucleic acid polymers.
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