Skip Navigation

Nucleic Acids Research 2005 33(15):4762-4774; doi:10.1093/nar/gki780
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (464K) Freely available
Right arrow Screen PDF (465K) Freely available
Right arrow Supplementary Material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (2)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by González-Barrera, S.
Right arrow Articles by Blanco, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by González-Barrera, S.
Right arrow Articles by Blanco, L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 GeneticsHome page
A. Decottignies
Microhomology-Mediated End Joining in Fission Yeast Is Repressed by Pku70 and Relies on Genes Involved in Homologous Recombination
Genetics, July 1, 2007; 176(3): 1403 - 1415.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.