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

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, lac...

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Autores principales: González-Barrera, Sergio, Sánchez, Arancha, Ruiz, José F., Juárez, Raquel, Picher, Angel J., Terrados, Gloria, Andrade, Paula, Blanco, Luis
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1192829/
https://www.ncbi.nlm.nih.gov/pubmed/16120966
http://dx.doi.org/10.1093/nar/gki780
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author González-Barrera, Sergio
Sánchez, Arancha
Ruiz, José F.
Juárez, Raquel
Picher, Angel J.
Terrados, Gloria
Andrade, Paula
Blanco, Luis
author_facet González-Barrera, Sergio
Sánchez, Arancha
Ruiz, José F.
Juárez, Raquel
Picher, Angel J.
Terrados, Gloria
Andrade, Paula
Blanco, Luis
author_sort González-Barrera, Sergio
collection PubMed
description 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 Polβ and Polλ, 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 Polβ, Polλ and Polμ.
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spelling pubmed-11928292005-08-29 Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe González-Barrera, Sergio Sánchez, Arancha Ruiz, José F. Juárez, Raquel Picher, Angel J. Terrados, Gloria Andrade, Paula Blanco, Luis Nucleic Acids Res Article 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 Polβ and Polλ, 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 Polβ, Polλ and Polμ. Oxford University Press 2005 2005-08-24 /pmc/articles/PMC1192829/ /pubmed/16120966 http://dx.doi.org/10.1093/nar/gki780 Text en © The Author 2005. Published by Oxford University Press. All rights reserved
spellingShingle Article
González-Barrera, Sergio
Sánchez, Arancha
Ruiz, José F.
Juárez, Raquel
Picher, Angel J.
Terrados, Gloria
Andrade, Paula
Blanco, Luis
Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe
title Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe
title_full Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe
title_fullStr Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe
title_full_unstemmed Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe
title_short Characterization of SpPol4, a unique X-family DNA polymerase in Schizosaccharomyces pombe
title_sort characterization of sppol4, a unique x-family dna polymerase in schizosaccharomyces pombe
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1192829/
https://www.ncbi.nlm.nih.gov/pubmed/16120966
http://dx.doi.org/10.1093/nar/gki780
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