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In this article we could contribute to the understanding of RNA remodelling processes by ATP-dependent DExH-type helicases. For a particular RNA helicase, called MLE, we could show that an auxiliary double-stranded RNA binding domain (dsRBD) autoregulates the double-stranded RNA unwinding process by binding to the helicase core. This conformational change is essential to allow RNA entering the core of the helicase. These findings are based on seven cryo-EM structures, Dr. Jagtap could determine. Mutation of the interface between the dRBD and the helicase core rendered the helicase inactive with lethal consequences for the male fruit fly. The latter was shown by our collaborators in the Peter Becker lab at the LMU. This work has implications for drug development against the human ortholog of MLE, DHX9. This RNA helicase has been recognised for its therapeutic potential in cancer, autoimmune diseases and viral infection.