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Characterization of the recombination activities of the Entamoeba histolytica Rad51 recombinase
Journal article   Open access   Peer reviewed

Characterization of the recombination activities of the Entamoeba histolytica Rad51 recombinase

Andrew A. Kelso, Steven D. Goodson, Suchitra Chavan, Amanda F. Say, Audrey Turchick, Deepti Sharma, LeAnna L. Ledford, Erin Ratterman, Kristin Leskoske, Ada V. King, …
Molecular and biochemical parasitology, v 210(01-Feb)
Nov 2016
DOI: https://doi.org/10.1016/j.molbiopara.2016.09.001
PMID: 27678398
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://doi.org/10.1016/j.molbiopara.2016.09.001View
Accepted (AM)Open Access (Publisher-Specific),  Open

Abstract

DNA repair Entamoeba histolytica Homologous recombination RAD51 Recombinase inhibitors
[Display omitted] The protozoan parasite responsible for human amoebiasis is Entamoeba histolytica. An important facet of the life cycle of E. histolytica involves the conversion of the mature trophozoite to a cyst. This transition is thought to involve homologous recombination (HR), which is dependent upon the Rad51 recombinase. Here, a biochemical characterization of highly purified ehRad51 protein is presented. The ehRad51 protein preferentially binds ssDNA, forms a presynaptic filament and possesses ATP hydrolysis activity that is stimulated by the presence of DNA. Evidence is provided that ehRad51 catalyzes robust DNA strand exchange over at least 5.4 kilobase pairs. Although the homologous DNA pairing activity of ehRad51 is weak, it is strongly enhanced by the presence of two HR accessory cofactors, calcium and Hop2-Mnd1. The biochemical system described herein was used to demonstrate the potential for targeting ehRad51 with two small molecule inhibitors of human RAD51. We show that 4,4′-diisothiocyanostilbene-2,2′-disulfonic acid (DIDS) inhibited ehRad51 by interfering with DNA binding and attenuated encystation in Entamoeba invadens, while B02 had no effect on ehRad51 strand exchange activity. These results provide insight into the underlying mechanism of homology-directed DNA repair in E. histolytica.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Parasitology
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