From unwinding to clamping — the DEAD box RNA helicase family View Full Text


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Article Info

DATE

2011-07-22

AUTHORS

Patrick Linder, Eckhard Jankowsky

ABSTRACT

Key PointsRNA helicases of the DEAD box family are important players in RNA metabolism in most living organisms. Despite high conservation between DEAD box proteins, they participate in many different processes.Recent structural and functional analyses have changed our perception of these fascinating enzymes. They clamp the RNA substrate in an ATP-dependent manner, which can lead to the formation of an RNA-binding complex or to local unwinding of double-stranded RNA. Whereas ATP-binding is necessary and sufficient for RNA binding or unwinding, ATP hydrolysis is required for the release and recycling of the enzyme.The binding to the RNA substrate, or the unwinding of a duplex RNA and the hydrolysis of ATP and release of phosphate, must be tightly regulated by other proteins and small molecules. Therefore, DEAD box RNA helicases act in complexes that are sometimes very large.Three processes that beautifully exemplify these different concepts are the formation of the exon junction complex, the export of mRNA and translation initiation.In the exon junction complex, eukaryotic initiation factor 4AIII (eIF4AIII) is bound to the mRNA and the hydrolysis of ATP and release of phosphate are controlled by partner proteins.The export of mRNA through the nuclear complex involves many proteins. This process is assisted by DEAD box protein 5 (Dbp5) in yeast (DDX19 and DDX25 in vertebrates), which is required for the recycling of export factors and the release of the mRNA into the cytoplasm. Its activity is controlled by nuclear pore complex proteins and the small metabolite inositol hexakisphosphate.eIF4A, which was the first DEAD box protein to be characterized, is required for translation initiation. Its activity is stimulated by the interaction with eIF4G, which is a large scaffolding protein of the cap-binding complex, and inhibited by the tumour suppressor protein programmed cell death 4 (PDCD4), the small RNA BC1 or the small natural products pateamine A or hippuristanol. More... »

PAGES

505-516

References to SciGraph publications

  • 2010-10-13. Single-molecule analysis of Mss116-mediated group II intron folding in NATURE
  • 2011-03-27. A conserved mechanism of DEAD-box ATPase activation by nucleoporins and IP6 in mRNA export in NATURE
  • 2006-10-29. The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2007-10. Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone in NATURE
  • 2004-03-21. eIF4AIII binds spliced mRNA in the exon junction complex and is essential for nonsense-mediated decay in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2004-10. Molecular mechanisms of translational control in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • 2009-02-15. The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2005-09-18. The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2006-06-18. Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export in NATURE CELL BIOLOGY
  • 2011-03-23. mRNA helicases: the tacticians of translational control in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • 2006-06-18. Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export in NATURE CELL BIOLOGY
  • 1989-01. Birth of the D-E-A-D box in NATURE
  • 2010-09-05. The exon junction complex differentially marks spliced junctions in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2004-02. An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay in NATURE
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    http://scigraph.springernature.com/pub.10.1038/nrm3154

    DOI

    http://dx.doi.org/10.1038/nrm3154

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1052580278

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/21779027


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