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Nucleic Acids Research, 2001, Vol. 29, No. 18 3822-3834
© 2001 Oxford University Press

Nuclear DNA polymerase beta from Leishmania infantum. Cloning, molecular analysis and developmental regulation

Soraya Taladriz, Tobias Hanke, María J. Ramiro, Miguel García-Díaz1, Mario García de Lacoba, Luis Blanco1 and Vicente Larraga*

Centro de Investigaciones Biológicas, (C.S.I.C), Velázquez, 144. 2800, Madrid, Spain and 1Centro de Biología Molecular ‘Severo Ochoa’ (C.S.I.C.-U.A.M.) Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain

We have identified a novel polymerase beta (Pol ß)-like enzyme from Leishmania infantum, a parasite protozoon causing disease in humans. This protein, named Li Pol ß, shows a nuclear localization that contrasts with the mitochondrial localization of Pol ß from Crithidia fasciculata, a closely related parasite, the only polymerase ß described so far in Trypanosomatidae. Li Pol ß, that belongs to the DNA polymerase X family, displays an evolutionarily conserved Pol ß-type DNA polymerase core, in which most of the key residues involved in DNA binding, nucleotide binding, dRPase and polymerization catalysis are conserved. In agreement with this, Li Pol ß, overproduced in Escherichia coli, displayed intrinsic DNA polymerase activity. Cell synchronization experiments showed a correlation between both Li Pol ß mRNA and protein levels along the parasite cell cycle. Analysis of these parameters at the different growth phases of the parasite, from the proliferative (non-infective) logarithmic phase to the non-dividing (highly infectious) stationary phase, showed high levels of Li Pol ß at the infective phase of the parasite. The data suggest a role of Li Pol ß in base excision repair in L.infantum, a parasite usually affected by oxygen stress environments into the macrophage host cells.

* To whom the correspondence should be addressed. Tel: +34 91 5611800; Fax: +34 91 5627518; Email: vlarraga{at}cib.csic.es


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