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Binding activity of replication protein A to UV-damaged single-stranded DNA
T Hashimoto1, H Morioka, S Izuta
1Faculty of Science, Kumamoto University, Kumamoto 860-8555, Japan.
Nucleic Acids Symposium Series
|August 9, 2003
Abstract:
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.