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

Author

Listed:
  • Ben Montpetit

    (University of California
    University of California)

  • Nathan D. Thomsen

    (University of California
    University of California
    Present addresses: Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, USA (N.D.T.); Department of Pharmacology, State University of New York at Stony Brook, Stony Brook, New York 11794, USA (M.A.S.).)

  • Kara J. Helmke

    (University of California
    University of California)

  • Markus A. Seeliger

    (University of California
    University of California
    Present addresses: Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, USA (N.D.T.); Department of Pharmacology, State University of New York at Stony Brook, Stony Brook, New York 11794, USA (M.A.S.).)

  • James M. Berger

    (University of California
    University of California)

  • Karsten Weis

    (University of California
    University of California)

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.

Suggested Citation

  • Ben Montpetit & Nathan D. Thomsen & Kara J. Helmke & Markus A. Seeliger & James M. Berger & Karsten Weis, 2011. "A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export," Nature, Nature, vol. 472(7342), pages 238-242, April.
    • Handle: RePEc:nat:nature:v:472:y:2011:i:7342:d:10.1038_nature09862
    DOI: 10.1038/nature09862
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