Función de la DNA polimerasa lambda en reparación de DNA y tumorogénesis

TL;DRAbstract

This Doctoral Thesis reports the purification of Leishmania infantum DNA polymerase beta (LiPols), as well as its characterization as a DNA repair enzyme, with a metal preference for Mn2+ over Mg2+. LiPols prefers gapped-DNA substrates having a 5?-P end, in agreement with its role in DNA repair reactions. Purified LiPols also displayed a 5?-deoxyribose-5-phosphate (dRP) lyase activity, consistent with a selimination mechanism. The concerted action of dRP lyase and DNA polymerization activities of LiPols on a uracil-containing DNA suggests its participation in ?singlenucleotide? base excision repair (BER). Analysis of LiPols DNA polymerization activity at different stages of the L. infantum infective cycle supports a role for LiPols in parasite DNA repair, counteracting the oxidative damage occurring inside the macrophage. DNA polymerase lambda (Pol?), a recently described Family X DNA polymerase, has been also studied in this work regarding its in vivo role in DNA repair and tolerance

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