DEAD‐box proteins as RNA helicases and chaperones
- 20 September 2010
- Vol. 2 (1), 135-152
- https://doi.org/10.1002/wrna.50
Abstract
DEAD‐box proteins are ubiquitous in RNA‐mediated processes and function by coupling cycles of ATP binding and hydrolysis to changes in affinity for single‐stranded RNA. Many DEAD‐box proteins use this basic mechanism as the foundation for a version of RNA helicase activity, efficiently separating the strands of short RNA duplexes in a process that involves little or no translocation. This activity, coupled with mechanisms to direct different DEAD‐box proteins to their physiological substrates, allows them to promote RNA folding steps and rearrangements and to accelerate remodeling of RNA–protein complexes. This review will describe the properties of DEAD‐box proteins as RNA helicases and the current understanding of how the energy from ATPase activity is used to drive the separation of RNA duplex strands. It will then describe how the basic biochemical properties allow some DEAD‐box proteins to function as chaperones by promoting RNA folding reactions, with a focus on the self‐splicing group I and group II intron RNAs. WIREs RNA 2011 2 135–152 DOI: 10.1002/wrna.50 This article is categorized under: RNA Structure and Dynamics > RNA Structure, Dynamics, and Chemistry RNA-Based Catalysis > Miscellaneous RNA‐Catalyzed Reactions RNA Interactions with Proteins and Other Molecules > Protein–RNA RecognitionThis publication has 116 references indexed in Scilit:
- SF1 and SF2 helicases: family mattersCurrent Opinion in Structural Biology, 2010
- Protein-Facilitated Folding of Group II Intron RibozymesJournal of Molecular Biology, 2010
- Structure of the Yeast DEAD Box Protein Mss116p Reveals Two Wedges that Crimp RNAMolecular Cell, 2009
- Unwinding by Local Strand Separation Is Critical for the Function of DEAD-Box Proteins as RNA ChaperonesJournal of Molecular Biology, 2009
- A Conformational Rearrangement in the Spliceosome Sets the Stage for Prp22-Dependent mRNA ReleaseMolecular Cell, 2008
- The ATPase Cycle Mechanism of the DEAD-box rRNA Helicase, DbpAJournal of Molecular Biology, 2008
- Function of the C-terminal Domain of the DEAD-box Protein Mss116p Analyzed in Vivo and in VitroJournal of Molecular Biology, 2008
- Do DEAD-Box Proteins Promote Group II Intron Splicing without Unwinding RNA?Molecular Cell, 2007
- Probing the Mechanisms of DEAD-Box Proteins as General RNA Chaperones: The C-Terminal Domain of CYT-19 Mediates General Recognition of RNABiochemistry, 2007
- Involvement of DEAD-box Proteins in Group I and Group II Intron Splicing. Biochemical Characterization of Mss116p, ATP Hydrolysis-dependent and -independent Mechanisms, and General RNA Chaperone ActivityJournal of Molecular Biology, 2007