ATP utilization and RNA conformational rearrangement by DEAD-box proteins

Arnon Henn, Michael J. Bradley, Enrique M. De La Cruz

Research output: Contribution to journalReview articlepeer-review


RNA helicase enzymes catalyze the in vivo folding and conformational re-arrangement of RNA. DEAD-box proteins (DBPs) make up the largest family of RNA helicases and are found across all phyla. DBPs are molecular motor proteins that utilize chemical energy in cycles of ATP binding, hydrolysis, and product release to perform mechanical work resulting in reorganization of cellular RNAs. DBPs contain a highly conserved motor domain helicase core. Auxiliary domains, enzymatic adaptations, and regulatory partner proteins contribute to the diversity of DBP function throughout RNA metabolism. In this review we focus on the current understanding of the DBP ATP utilization mechanism in rearranging and unwinding RNA structures. We discuss DBP structural properties, kinetic pathways, and thermodynamic features of nucleotide-dependent interactions with RNA. We highlight recent advances in the DBP field derived from biochemical and molecular biophysical investigations aimed at developing a quantitative mechanistic understanding of DBP molecular motor function.

Original languageEnglish
Pages (from-to)247-267
Number of pages21
JournalAnnual Review of Biophysics
Issue number1
StatePublished - 9 Jun 2012


  • ATPase
  • Helicase
  • Kinetics
  • Mechanism
  • Molecular motor
  • Thermodynamics

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Bioengineering
  • Biochemistry
  • Cell Biology


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