Looking back on the birth of DEAD-box RNA helicases

Patrick Linder, Frances Fuller-Pace

    Research output: Contribution to journalArticlepeer-review

    60 Citations (Scopus)

    Abstract

    DEAD-box proteins represent the largest family of RNA helicases, present in all three kingdoms of life. They are involved in a variety of processes involving RNA metabolism and in some instances also in processes that use guide RNAs. Since their first descriptions in the late 1980s, the perception of their molecular activities has dramatically changed. At the time when only eight proteins with 9 conserved motifs constituted the DEAD-box protein family, it was the biochemical characterization of mammalian eIF4A that first suggested a local unwinding activity. This was confirmed in vitro using partially double stranded RNA substrates with the unexpected result of a bidirectional unwinding activity. A real change of paradigm from the classical helicase activity to localized RNA unwinding occurred with the publication of the vasa•RNA structure with a bend in the RNA substrate and the insightful work from several laboratories demonstrating local unwinding without translocation. Finally, elegant work on the exon-junction complex revealed how DEAD-box proteins can bind to RNA to serve as clamps to function as nucleation centers to form RNP complexes. This article is part of a Special Issue entitled: The Biology of RNA helicases - Modulation for life.
    Original languageEnglish
    Pages (from-to)750-755
    Number of pages6
    JournalBiochimica et Biophysica Acta - Gene Regulatory Mechanisms
    Volume1829
    Issue number8
    Early online date29 Mar 2013
    DOIs
    Publication statusPublished - Aug 2013

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