dc.creator | García Díaz, Miguel | es |
dc.creator | Bebenek, Katarzyna | es |
dc.creator | Sabariegos, Rosario | es |
dc.creator | Domínguez, Orlando | es |
dc.creator | Rodríguez, Josana Renato | es |
dc.creator | Kirchhoff, Tomas | es |
dc.creator | García Palomero, Esther | es |
dc.creator | Picher, Ángel J. | es |
dc.creator | Juárez, Raquel | es |
dc.creator | Ruiz Pérez, José Francisco | es |
dc.creator | Kunkel, Thomas A. | es |
dc.creator | Blanco, Luis | es |
dc.date.accessioned | 2017-02-15T13:48:20Z | |
dc.date.available | 2017-02-15T13:48:20Z | |
dc.date.issued | 2002 | |
dc.identifier.citation | García Díaz, M., Bebenek, K., Sabariegos, R., Domínguez, O., Rodríguez, J.R., Kirchhoff, T.,...,Blanco, L. (2002). DNA polymerase λ, a novel DNA repair enzyme in human cells. Journal of Biological Chemistry, 277 (15), 13184-13191. | |
dc.identifier.issn | 0021-9258 | es |
dc.identifier.uri | http://hdl.handle.net/11441/54206 | |
dc.description.abstract | 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 A 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 A 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 A 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 | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | American Society for Biochemistry and Molecular Biology Inc. | es |
dc.relation.ispartof | Journal of Biological Chemistry, 277 (15), 13184-13191. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | DNA polymerase λ, a novel DNA repair enzyme in human cells | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | es |
dc.relation.publisherversion | 10.1074/jbc.M111601200 | es |
idus.format.extent | 9 p. | es |
dc.journaltitle | Journal of Biological Chemistry | es |
dc.publication.volumen | 277 | es |
dc.publication.issue | 15 | es |
dc.publication.initialPage | 13184 | es |
dc.publication.endPage | 13191 | es |