A new Drosophila ultraviolet light-damaged DNA recognition endonuclease that selectively nicks a (6-4) photoproduct site.
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.
Kai
M
M
Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, 2641 Yamazaki,Noda-shi, Chiba-ken 278, Japan.
Todo
T
T
Wada
M
M
Ryo
H
H
Masutani
C
C
Kobayashi
H
H
Morioka
H
H
Ohtsuka
E
E
Hanaoka
F
F
Sakaguchi
K
K
D000818:Animals; D001483:Base Sequence; D004249:DNA Damage; D004260:DNA Repair; D004269:DNA, Bacterial / Q000528:radiation effects*; D004268:DNA-Binding Proteins / Q000235:genetics*; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics*; D004706:Endodeoxyribonucleases / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D014466:Ultraviolet Rays
D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D004706:Endodeoxyribonucleases; C112206:DdbP1 protein, Drosophila