Evolution of Base Excision Repair in Entamoeba histolytica is shaped by gene loss, gene duplication, and lateral gene transfer
| Autor: | Carlos H. Trasviña-Arenas, Luis G. Brieba, Elisa Azuara-Liceaga, Sheila S. David, Luis Delaye |
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| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular DNA Repair Gene Transfer Horizontal Protein Conformation DNA repair Genes Protozoan Biochemistry DNA Glycosylases Evolution Molecular 03 medical and health sciences Entamoeba histolytica 0302 clinical medicine Gene Duplication parasitic diseases Gene duplication Humans AP site Amino Acid Sequence Molecular Biology Gene 030304 developmental biology Genetics chemistry.chemical_classification 0303 health sciences DNA ligase biology Cell Biology Base excision repair biology.organism_classification chemistry DNA glycosylase 030220 oncology & carcinogenesis |
| Zdroj: | DNA Repair. 76:76-88 |
| ISSN: | 1568-7864 |
| DOI: | 10.1016/j.dnarep.2019.02.009 |
| Popis: | During its life cycle, the protist parasite Entamoeba histolytica encounters reactive oxygen and nitrogen species that alter its genome. Base excision repair (BER) is one of the most important pathways for the repair of DNA base lesions. Analysis of the E. histolytica genome revealed the presence of most of the BER components. Surprisingly, this included a gene encoding an apurinic/apyrimidinic (AP) endonuclease that previous studies had assumed was absent. Indeed, our analysis showed that the genome of E. histolytica harbors the necessary genes needed for both short and long-patch BER sub-pathways. These genes include DNA polymerases with predicted 5'-dRP lyase and strand-displacement activities and a sole DNA ligase. A distinct feature of the E. histolytica genome is the lack of several key damage-specific BER glycosylases, such as OGG1/MutM, MDB4, Mag1, MPG, SMUG, and TDG. Our evolutionary analysis indicates that several E. histolytica DNA glycosylases were acquired by lateral gene transfer (LGT). The genes that encode for MutY, AlkD, and UDG (Family VI) are included among these cases. Endonuclease III and UNG (family I) are the only DNA glycosylases with a eukaryotic origin in E. histolytica. A gene encoding a MutT 8-oxodGTPase was also identified that was acquired by LGT. The mixed composition of BER genes as a DNA metabolic pathway shaped by LGT in E. histolytica indicates that LGT plays a major role in the evolution of this eukaryote. Sequence and structural prediction of E. histolytica DNA glycosylases, as well as MutT, suggest that the E. histolytica DNA repair proteins evolved to harbor structural modifications that may confer unique biochemical features needed for the biology of this parasite. |
| Databáze: | OpenAIRE |
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