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