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Abstract
Understanding the regulation of the characteristic life cycle of Toxoplasma gondii is key to drug development. The Skp1-cullin1-F-box protein (SCF) complex plays a major role in the regulation of the eukaryotic cell cycle. A novel O2-dependent hydroxylation/glycosylation pathway modifies the adaptor protein Skp1 in Toxoplasma, but not any host proteins. In an unrelated protist, Dictyostelium, evidence indicates that the pathway only modifies Skp1 and enhances the association between Skp1 and F-box proteins (FBPs) to promote SCF activity. This study investigated if the Toxoplasma Skp1 modifications influenced the association between Skp1 and its interactors. Toxoplasma FbxO1 was identified as the most abundant Skp1-interacting FBP. Domain analysis revealed that Toxoplasma FbxO1 was conserved in apicomplexans and potentially N-myristoylated, supportive of its dynamic localization in cells. The Toxoplasma Skp1-FbxO1 association was found to be robust, however, no significant effect of the Toxoplasma Skp1 modifications on the association between Skp1 and FbxO1 was found.