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RNA helicase A (RHA) is a multifunctional protein that regulates gene expression. RHA has two double-stranded RNA-binding domains (dsRBDs) that serve as modules for highly structured RNA binding and protein-protein interactions. Using the dsRBDs, RHA binds to cellular and viral mRNAs, exports them from the nucleus, and regulates splicing as well as translational initiation. The RHA dsRBDs also reportedly mediate interactions with small RNAs and other dsRBD-containing proteins, and altogether form a processing complex involved in RNA silencing pathways. In addition, the RHA dsRBDs bridge RNA polymerase II with several transcription factors. Here we report the H, C, and N chemical shift assignments of the dsRBDs of RHA. The resonance assignments obtained in this work will contribute to the elucidation of the interactions between RHA and transcriptional or post-transcriptional gene regulators. [ABSTRACT FROM AUTHOR]