Characterization of the binding of distamycin A to damaged DNA: a comparison with the DNA recognition of the human DDB protein.
Distamycin A binds to DNA containing the (6-4) photoproduct, a major UV lesion that is recognized by the damaged DNA-binding (DDB) protein in human cells. We analyzed the binding properties of distamycin A and compared the results with those of the DDB protein. Structural change of the DNA duplex was not observed for distamycin A in two types of experiments, whereas the protein induced a large bending of the helix. Although the substrate specificity was different between the drug and the protein, thymine glycol was recognized by both of them, and inhibition of the DDB protein binding to the (6-4) photoproduct-containing DNA by distamycin A was tested.
Fujiwara
Yoshie
Y
Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Inase
Aki
A
Kawasaki
Yusuke
Y
Yoshikawa
Shinya
S
Iwai
Shigenori
S
D001665:Binding Sites; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004249:DNA Damage; D004268:DNA-Binding Proteins / Q000378:metabolism; D004214:Distamycins / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011740:Pyrimidine Dimers / Q000737:chemistry; D020349:Surface Plasmon Resonance; D013941:Thymine / Q000031:analogs & derivatives / Q000737:chemistry
D004268:DNA-Binding Proteins; D004214:Distamycins; D011740:Pyrimidine Dimers; C058406:pyrimidine-pyrimidone dimer; C029389:thymine glycol; C030000:stallimycin; D004247:DNA; D013941:Thymine