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Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe

AuthorsGonzález-Barrera, Sergio; Sánchez, Arancha ; Ruiz, José F. ; Juárez, Raquel; Picher, Ángel J. ; Terrados, Gloria ; Andrade, Paula ; Blanco, Luis
KeywordsSchizosaccharomyces pombe
Issue Date2005
PublisherOxford University Press
CitationNucleic Acids Research 2005 33(15):4762-4774
AbstractAs 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 3'5' proofreading activity and its preferred substrates are small gaps with a 5'-phosphate group. Similarly to Polµ, 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 Polµ, SpPol4 lacks terminal deoxynucleotidyltransferase activity and realigns the primer terminus to alternative template bases only under certain sequence contexts and, therefore, it is less error-prone than Polµ. Nonetheless, the biochemical properties of this gap-filling DNA polymerase are suitable for a possible role of SpPol4 in non-homologous end-joining. Unexpectedly based on sequence analysis, SpPol4 has deoxyribose phosphate lyase activity like Polß and Pol, and unlike Polµ, suggesting also a role of this enzyme in base excision repair. Therefore, SpPol4 is a unique enzyme whose enzymatic properties are hybrid of those described for mammalian Polß, Pol and Polµ.
Publisher version (URL)http://dx.doi.org/10.1093/nar/gki780
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