Journal
ANNUAL REVIEW OF BIOPHYSICS, VOL 41
Volume 41, Issue -, Pages 247-267Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-biophys-050511-102243
Keywords
ATPase; helicase; molecular motor; kinetics; thermodynamics; mechanism
Categories
Funding
- NIGMS NIH HHS [R01 GM071688, GM097348, R01 GM097348] Funding Source: Medline
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RNA helicase enzymes catalyze the in vivo folding and conformational rearrangement 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.
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