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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.

DOI:10.1016/s0167-4781(97)00215-7
PMID:9565683
Abstract

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.

摘要

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引用本文的文献

1
Drosophila damage-specific DNA-binding protein 1 (D-DDB1) is controlled by the DRE/DREF system.果蝇损伤特异性DNA结合蛋白1（D-DDB1）受DRE/DREF系统调控。
Nucleic Acids Res. 2002 Sep 1;30(17):3795-808. doi: 10.1093/nar/gkf490.