A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export

Ben Montpetit, Nathan D. Thomsen, Kara J. Helmke, Markus A. Seeliger, James M. Berger () and Karsten Weis ()
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Ben Montpetit: University of California
Nathan D. Thomsen: University of California
Kara J. Helmke: University of California
Markus A. Seeliger: University of California
James M. Berger: University of California
Karsten Weis: University of California

Nature, 2011, vol. 472, issue 7342, 238-242

Abstract: Mechanisms of mRNA export As mRNA-protein complexes are exported from the nucleus to the cytoplasm, they pass through the nuclear pore complex (NPC). Dbp5, an RNA helicase associated with the NPC through the Nup159 subunit, remodels such mRNA-protein complexes. Montpetit et al. present the structure of Dbp5 bound to Gle1 and the small-molecule activator InsP6, with and without Nup159 and RNA. Similarities to the structure of the translation initiation complex, eIF4G–eIF4A suggests that Gle1InsP6 activates Dbp5 by relieving an autoinhibitory mechanism, by promoting release of RNA, and (with Nup159) by stabilizing a conformation that cannot bind RNA.

Date: 2011
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DOI: 10.1038/nature09862

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