A new Drosophila ultraviolet light-damaged DNA recognition endonuclease that selectively nicks a (6-4) photoproduct site.

作者信息

Kai M, Todo T, Wada M, Ryo H, Masutani C, Kobayashi H, Morioka H, Ohtsuka E, Hanaoka F, Sakaguchi K

机构信息

Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, 2641 Yamazaki,Noda-shi, Chiba-ken 278, Japan.

出版信息

Biochim Biophys Acta. 1998 Apr 29;1397(2):180-8. doi: 10.1016/s0167-4781(97)00215-7.

We have previously described the purification of an ultraviolet light (UV) damage-specific DNA-binding protein from Drosophila melanogaster, designated D-DDB P1 [Nucleic Acids Res., 23 (1995) 2600-2607]. Here, we obtained highly purified D-DDB P1 from Drosophila Kc cells, and we found that D-DDB P1 is also a nuclease. D-DDB P1 can selectively bind to pyrimidine (6-4) pyrimidone photoproducts, and in the presence of Mg++, D-DDB P1 can catalyze an incision immediately on the 3' and 5' sides of the (6-4) photoproduct site.