Characterization of the binding of distamycin A to damaged DNA: a comparison with the DNA recognition of the human DDB protein.

Yoshie Fujiwara, Aki Inase, Yusuke Kawasaki, Shinya Yoshikawa, Shigenori Iwai

Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.

Nucleic acids symposium series (2004) 2006

filter terms:

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.

Citation

Yoshie Fujiwara, Aki Inase, Yusuke Kawasaki, Shinya Yoshikawa, Shigenori Iwai. Characterization of the binding of distamycin A to damaged DNA: a comparison with the DNA recognition of the human DDB protein. Nucleic acids symposium series (2004). 2006(50):235-6