放线菌素A与受损DNA结合的特性：与人DDB蛋白的DNA识别的比较。

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

作者信息

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

机构信息

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

出版信息

Nucleic Acids Symp Ser (Oxf). 2006(50):235-6. doi: 10.1093/nass/nrl117.

DOI:10.1093/nass/nrl117

PMID:17150904

Abstract

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.

摘要

放线菌素A与含有（6-4）光产物的DNA结合，（6-4）光产物是一种主要的紫外线损伤，可被人类细胞中的损伤DNA结合（DDB）蛋白识别。我们分析了放线菌素A的结合特性，并将结果与DDB蛋白的结果进行了比较。在两种实验中均未观察到放线菌素A引起DNA双链体的结构变化，而该蛋白则诱导了螺旋的大幅弯曲。尽管药物和蛋白质之间的底物特异性不同，但二者均能识别胸腺嘧啶二醇，并测试了放线菌素A对DDB蛋白与含（6-4）光产物的DNA结合的抑制作用。