a nuclear family a dna polymerase from entamoeba histolytica bypasses thymine glycol核心家庭痢疾阿米巴绕过胸腺嘧啶醇的dna聚合酶.pdfVIP
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a nuclear family a dna polymerase from entamoeba histolytica bypasses thymine glycol核心家庭痢疾阿米巴绕过胸腺嘧啶醇的dna聚合酶
A Nuclear Family A DNA Polymerase from Entamoeba
histolytica Bypasses Thymine Glycol
1 2 1
Guillermo Pastor-Palacios , Elisa Azuara-Liceaga , Luis G. Brieba *
´ ´ ´ ´
1 Laboratorio Nacional de Genomica para la Biodiversidad, CINVESTAV, Irapuato, Mexico, 2 Posgrado en Ciencias Genomicas, Universidad Autonoma de la Ciudad de
´ ´ ´
Mexico, Mexico Distrito Federal, Mexico
Abstract
Background: Eukaryotic family A DNA polymerases are involved in mitochondrial DNA replication or translesion DNA
synthesis. Here, we present evidence that the sole family A DNA polymerase from the parasite protozoan E. histolytica
(EhDNApolA) localizes to the nucleus and that its biochemical properties indicate that this DNA polymerase may be
involved in translesion DNA synthesis.
Methodology and Results: EhDNApolA is the sole family A DNA polymerase in E. histolytica. An in silico analysis places
family A DNA polymerases from the genus Entamoeba in a separate branch of a family A DNA polymerases phylogenetic
tree. Biochemical studies of a purified recombinant EhDNApolA demonstrated that this polymerase is active in primer
elongation, is poorly processive, displays moderate strand displacement, and does not contain 39–59 exonuclease or editing
activity. Importantly, EhDNApolA bypasses thymine glycol lesions with high fidelity, and confocal microscopy demonstrates
that this polymerase is translocated into the nucleus. These data suggest a putative role of EhDNApolA in translesion DNA
synthesis in E. histolytica.
Conclusion: This is the first report of the
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