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Título: | DNA polymerase λ, a novel DNA repair enzyme in human cells |
Autor: | García-Díaz, Miguel; Bebenek, Katarzyna; Sabariegos, Rosario; Domı́nguez, Orlando; Rodrı́guez, Josana; Kirchhoff, Tomas; Garcı́a-Palomero, Esther; Picher, Ángel J.; Juárez, Raquel; Ruiz, José F. CSIC ORCID; Kunkel, Thomas A.; Blanco, Luis CSIC ORCID | Fecha de publicación: | 12-abr-2002 | Editor: | Elsevier American Society for Biochemistry and Molecular Biology |
Citación: | Journal of Biological Chemistry 277(15): 13184-13191 (2002) | Resumen: | DNA polymerase lambda (pol λ) is a novel family X DNA polymerase that has been suggested to play a role in meiotic recombination and DNA repair. The recent demonstration of an intrinsic 5′-deoxyribose-5-phosphate lyase activity in pol λ supports a function of this enzyme in base excision repair. However, the biochemical properties of the polymerization activity of this enzyme are still largely unknown. We have cloned and purified human pol λ to homogeneity in a soluble and active form, and we present here a biochemical description of its polymerization features. In support of a role in DNA repair, pol λ inserts nucleotides in a DNA template-dependent manner and is processive in small gaps containing a 5′-phosphate group. These properties, together with its nucleotide insertion fidelity parameters and lack of proofreading activity, indicate that pol λ is a novel β-like DNA polymerase. However, the high affinity of pol λ for dNTPs (37-fold over pol β) is consistent with its possible involvement in DNA transactions occurring under low cellular levels of dNTPs. This suggests that, despite their similarities, pol β and pol λ have nonredundant in vivo functions. | Versión del editor: | http://dx.doi.org/10.1074/jbc.M111601200 | URI: | http://hdl.handle.net/10261/338479 | DOI: | 10.1074/jbc.M111601200 | Identificadores: | issn: 0021-9258 e-issn: 1083-351X |
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