dc.creator | González Barrera, Sergio | es |
dc.creator | Sánchez, Arancha | es |
dc.creator | Ruiz Pérez, José Francisco | es |
dc.creator | Juárez, Raquel | es |
dc.creator | Picher, Ángel J. | es |
dc.creator | Terrados, Gloria | es |
dc.creator | Andrade, Paula | es |
dc.creator | Blanco, Luis | es |
dc.date.accessioned | 2017-02-15T13:47:00Z | |
dc.date.available | 2017-02-15T13:47:00Z | |
dc.date.issued | 2005 | |
dc.identifier.citation | González Barrera, S., Sánchez, A., Ruiz Pérez, J.F., Juárez, R.E., Picher, Á.J., Terrados, G.,...,Blanco, L. (2005). Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe. Nucleic Acids Research, 33 (15), 4762-4774. | |
dc.identifier.issn | 0305-1048 | es |
dc.identifier.uri | http://hdl.handle.net/11441/54205 | |
dc.description.abstract | As predicted by the amino acid sequence, the purified protein coded by Schizosaccharomyces pombe SPAC2F7.06c is a DNA polymerase (SpPol4) whose biochemical properties resemble those of other X family (PolX) members. Thus, this new PolX is template-dependent, polymerizes in a distributive manner, lacks a detectable 30!50 proofreading activity and its preferred substrates are small gaps with a 50- phosphate group. Similarly to Polm, SpPol4 can incorporate a ribonucleotide (rNTP) into a primer DNA. However, it is not responsible for the 1–2 rNTPs proposed to be present at the mating-type locus and those necessary for mating-type switching. Unlike Polm, SpPol4 lacks terminal deoxynucleotidyl- transferase activity and realigns the primer terminus to alternative template bases only under certain sequence contexts and, therefore, it is less error- prone than Polm. Nonetheless, the biochemical prop- erties of this gap-filling DNA polymerase are suitable for a possible role of SpPol4 in non-homologous end-joining. Unexpectedly based on sequence ana- lysis, SpPol4 has deoxyribose phosphate lyase activ- ity like Polb and Poll, and unlike Polm, suggesting also a role of this enzyme in base excision repair. Therefore, SpPol4 is a unique enzyme whose enzym- atic properties are hybrid of those described for mammalian Polb, Poll and Polm | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Oxford University Press | es |
dc.relation.ispartof | Nucleic Acids Research, 33 (15), 4762-4774. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe | 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 | 10.1093/nar/gki780 | es |
idus.format.extent | 13 p. | es |
dc.journaltitle | Nucleic Acids Research | es |
dc.publication.volumen | 33 | es |
dc.publication.issue | 15 | es |
dc.publication.initialPage | 4762 | es |
dc.publication.endPage | 4774 | es |