Binding activity of replication protein A to UV-damaged single-stranded DNA.
To obtain the information for the exact role of replication protein A (RPA) on both eukaryotic DNA replication and repair, the binding preference of RPA purified from Xenopus egg extract against the undamaged and UV-damaged single-stranded DNA was studied by the gel shift assay. Chemically synthesized oligonucleotide containing the pyrimidine(6-4)pyrimidone photoproduct at one site was used as a model of UV-damaged DNA. Results of competition assay and Scatchard plots indicate that RPA preferentially binds to the 6-4 photoproduct oligonucleotide than the undamaged DNA.
Hashimoto
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T
Faculty of Science, Kumamoto University, Kumamoto 860-8555, Japan.
Morioka
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Izuta
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D000818:Animals; D001483:Base Sequence; D001667:Binding, Competitive; D004249:DNA Damage; D004260:DNA Repair; D004261:DNA Replication; D004277:DNA, Single-Stranded / Q000378:metabolism* / Q000528:radiation effects*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D024202:Electrophoretic Mobility Shift Assay; D005260:Female; D066298:In Vitro Techniques; D007700:Kinetics; D009838:Oligodeoxyribonucleotides / Q000737:chemistry / Q000378:metabolism / Q000528:radiation effects; D010777:Photochemistry; D051716:Replication Protein A; D014466:Ultraviolet Rays; D014982:Xenopus laevis
D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D009838:Oligodeoxyribonucleotides; D051716:Replication Protein A