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Nucleic Acids Research 2005 33(15):4762-4774; doi:10.1093/nar/gki780
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Published online 24 August 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org


Article

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

Sergio González-Barrera, Arancha Sánchez, José F. Ruiz, Raquel Juárez, Angel J. Picher, Gloria Terrados, Paula Andrade and Luis Blanco*

Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma Madrid, Spain

*To whom correspondence should be addressed. Tel: +34 91 497 8493; Fax: +34 91 497 4799; Email: lblanco{at}cbm.uam.es

Received May 25, 2005. Revised August 3, 2005. Accepted August 3, 2005.

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 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{lambda}, 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{lambda} and Polµ.


Present address: José F. Ruiz, Departamento de Genética, Facultad de Biología, Universidad de Sevilla, Spain


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