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DDX3X is a human DEAD-box RNA helicase implicated in many cancers and inviral progression. In addition to the RecA-like catalytic core, DDX3X containsN- and C-terminal domains. Here, we investigate the substrate and proteinrequirements to support the ATPase activity of a DDX3X construct lacking 80residues from its C-terminal domain. Our data confirmed previous results thatfor an RNA molecule to support the ATPase activity of DDX3X it must contain asingle-stranded-double-stranded region. We investigated protein and RNAstructural reasons for this requirement. First, the RNA substrates consistingonly of a double-helix were unable to support DDX3X binding. A single-strandedRNA substrate supported DDX3X binding, while an RNA substrate consisting of asingle-stranded-double-stranded region not only supported the binding of DDX3Xto RNA, but also promoted DDX3X trimer formation. Thus, thesingle-stranded-double-stranded RNA region is needed for DDX3X trimerformation, and trimer formation is required for ATPase activity. Interestingly,the dependence of ATP hydrolysis on the protein concentration suggests that theDDX3X trimer hydrolyzes only two molecules of ATP. Lastly, a DNA substrate thatcontains single-stranded-double-stranded regions does not support the ATPaseactivity of DDX3X.

Action mechanism of DDX3X: An RNA helicase implicated in cancer propagation and viral infection