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Título: | DNA polymerase mu (Pol μ), homologous to TdT, could act as a DNA mutator in eukaryotic cells |
Autor: | Domínguez, Orlando; Ruiz, José F. CSIC ORCID; Laín de Lera, T.; García-Díaz, Miguel; González, Manuel A.; Kirchhoff, Tomas; Martínez-A, Carlos CSIC ORCID; Bernad, Antonio CSIC ORCID; Blanco, Luis CSIC ORCID | Palabras clave: | Human DNA polymerase Mutator Somatic hypermutation Terminal deoxynucleotidyl transferase |
Fecha de publicación: | 3-abr-2000 | Editor: | EMBO Press | Citación: | EMBO Journal 19(7): 1731-1742 (2000) | Resumen: | A novel DNA polymerase has been identified in human cells. Human DNA polymerase mu (Pol μ), consisting of 494 amino acids, has 41% identity to terminal deoxynucleotidyltransferase (TdT). Human Pol μ, overproduced in Escherichia coli in a soluble form and purified to homogeneity, displays intrinsic terminal deoxynucleotidyltransferase activity and a strong preference for activating Mn2+ ions. Interestingly, unlike TdT, the catalytic efficiency of polymerization carried out by Pol μ was enhanced by the presence of a template strand. Using activating Mg2+ ions, template-enhanced polymerization was also template-directed, leading to the preferred insertion of complementary nucleotides, although with low discrimination values. In the presence of Mn2+ ions, template-enhanced polymerization produced a random insertion of nucleotides. Northern-blotting and in situ analysis showed a preferential expression of Pol μ mRNA in peripheral lymphoid tissues. Moreover, a large proportion of the human expressed sequence tags corresponding to Pol μ, present in the databases, derived from germinal center B cells. Therefore, Pol μ is a good candidate to be the mutator polymerase responsible for somatic hypermutation of immunoglobulin genes. | Versión del editor: | https://doi.org/10.1093/emboj/19.7.1731 | URI: | http://hdl.handle.net/10261/338504 | DOI: | 10.1093/emboj/19.7.1731 | Identificadores: | issn: 0261-4189 e-issn: 1460-2075 |
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