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Título: | Identification of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in human DNA polymerase λ: A possible role in base excision repair |
Autor: | Garcı́a-Dı́az, Miguel; Bebenek, Katarzyna; Kunkel, Thomas A.; Blanco, Luis CSIC ORCID | Fecha de publicación: | 14-sep-2001 | Editor: | Elsevier American Society for Biochemistry and Molecular Biology |
Citación: | Journal of Biological Chemistry 276(37): 34659-34663 (2001) | Resumen: | Base excision repair (BER) is a major repair pathway in eukaryotic cells responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Pivotal to this process is the 5′-deoxyribose-5-phosphate lyase (dRP lyase) activity of DNA polymerase β (Pol β). DNA polymerase λ (Pol λ) is a recently identified eukaryotic DNA polymerase that is homologous to Pol β. We show here that human Pol λ exhibits dRP lyase, but not AP lyase, activityin vitro and that this activity is consistent with a β-elimination mechanism. Accordingly, a single amino acid substitution (K310A) eliminated more than 90% of the wild-type dRP lyase activity, thus suggesting that Lys310 of Pol λ is the main nucleophile involved in the reaction. The dRP lyase activity of Pol λ, in coordination with its polymerization activity, efficiently repaired uracil-containing DNA in an in vitroreconstituted BER reaction. These results suggest that Pol λ may participate in “single-nucleotide” base excision repair in mammalian cells. | Versión del editor: | http://dx.doi.org/10.1074/jbc.M106336200 | URI: | http://hdl.handle.net/10261/338865 | DOI: | 10.1074/jbc.M106336200 | Identificadores: | issn: 0021-9258 e-issn: 1083-351X |
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