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The DEXD/H-box RNA Helicase DDX19 Is Regulated by an α-Helical Switch*S⃞

By Ruairi Collins, Tobias Karlberg, Lari Lehtiö, Patrick Schütz, Susanne van den Berg, Lars-Göran Dahlgren, Martin Hammarström, Johan Weigelt and Herwig Schüler


DEXD/H-box RNA helicases couple ATP hydrolysis to RNA remodeling by an unknown mechanism. We used x-ray crystallography and biochemical analysis of the human DEXD/H-box protein DDX19 to investigate its regulatory mechanism. The crystal structures of DDX19, in its RNA-bound prehydrolysis and free posthydrolysis state, reveal an α-helix that inserts between the conserved domains of the free protein to negatively regulate ATPase activity. This finding was corroborated by biochemical data that confirm an autoregulatory function of the N-terminal region of the protein. This is the first study describing crystal structures of a DEXD/H-box protein in its open and closed cleft conformations

Topics: Accelerated Publication
Publisher: American Society for Biochemistry and Molecular Biology
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Provided by: PubMed Central
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