Journal
FEBS JOURNAL
Volume 282, Issue 5, Pages 850-863Publisher
WILEY-BLACKWELL
DOI: 10.1111/febs.13198
Keywords
DEAD-box protein; DExH-box protein; RNA helicase; RNA-dependent ATPase; RNA-protein interaction; SF1; SF2
Categories
Funding
- Max Planck Gesellschaft
- European Commission (ERC) [294371]
- Deutsche Forschungsgemeinschaft [DFG SFB646, SFB1035, GRK1721, FOR1680]
- Deutsche Forschungsgemeinschaft (CIPSM)
Ask authors/readers for more resources
RNA helicases are present in all domains of life and participate in almost all aspects of RNA metabolism, from transcription and processing to translation and decay. The diversity of pathways and substrates that they act on is reflected in the diversity of their individual functions, structures, and mechanisms. However, RNA helicases also share hallmark properties. At the functional level, they promote rearrangements of RNAs and RNP particles by coupling nucleic acid binding and release with ATP hydrolysis. At the molecular level, they contain two domains homologous to the bacterial RecA recombination protein. This conserved catalytic core is flanked by additional domains, which typically regulate the ATPase activity in cis. Binding to effector proteins targets or regulates the ATPase activity in trans. Structural and biochemical studies have converged on the plasticity of RNA helicases as a fundamental property that is used to control their timely activation in the cell. In this review, we focus on the conformational regulation of conserved eukaryotic RNA helicases.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available