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A new Drosophila ultraviolet light-damaged DNA recognition endonuclease that selectively nicks a (6-4) photoproduct site.
Kai, M; Todo, T; Wada, M; Ryo, H; Masutani, C; Kobayashi, H; Morioka, H; Ohtsuka, E; Hanaoka, F; Sakaguchi, K.
Afiliación
  • Kai M; Department of Applied Biological Science, Faculty of Science and Technology, Science University of Tokyo, 2641 Yamazaki,Noda-shi, Chiba-ken 278, Japan.
Biochim Biophys Acta ; 1397(2): 180-8, 1998 Apr 29.
Article en En | MEDLINE | ID: mdl-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.
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Bases de datos: MEDLINE Asunto principal: Rayos Ultravioleta / Daño del ADN / ADN Bacteriano / Proteínas de Drosophila / Proteínas de Unión al ADN / Drosophila melanogaster / Endodesoxirribonucleasas Límite: Animals Idioma: En Revista: Biochim Biophys Acta Año: 1998 Tipo del documento: Article País de afiliación: Japón
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Bases de datos: MEDLINE Asunto principal: Rayos Ultravioleta / Daño del ADN / ADN Bacteriano / Proteínas de Drosophila / Proteínas de Unión al ADN / Drosophila melanogaster / Endodesoxirribonucleasas Límite: Animals Idioma: En Revista: Biochim Biophys Acta Año: 1998 Tipo del documento: Article País de afiliación: Japón