Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa

Article Abstract:

DEAD-box RNA helicases, which regulate various processes involving RNA, have two RecA-like domains as a catalytic core to alter higher order RNA structures. Mutational analyses indicate that the interdomain interactions couple ATP hydrolysis to RNA unwinding, probably through fine positioning of the duplex relative to the wedge helix, and this mechanism, which differs from those for canonical translocating helicases, may enable the targeted modulation of intricate RNA structures.

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Bent out of shape: RNA unwinding by the DEAD-box helicase Vasa

Article Abstract:

RNA helicases of the DEAD-box family are involved in essentially all RNA-dependent cellular processes. The structure of the DEAD-box protein Vasa in the presence of RNA and a nonhydrolyzable ATP analog is solved and important insights into how this family of helicases unwinds RNA is provided, presenting an elegant combination of structural, biochemical, and functional data on Drosophila Vasa.

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A new paradigm for translational control: Inhibition via 5'-3' mRNA tethering by Biocoid and the elF4E cognate 4EHP

Article Abstract:

The d4EHP, an eIF4E-related cap binding protein, specifically interacts with Biocoid to suppress caudal translation. The cap-dependent translational control that is not mediated by canonical eIF4E defines a new paradigm for translational inhibiytion involving tethering of the mRNA 5'and 3' ends.

Embryology, Experimental, Embryological research, Messenger RNA, Binding proteins

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