conformational plasticity of eukaryotic RNA‐dependent ATPases

• Published in: The FEBS journal Vol. 282; no. 5; pp. 850 - 863
• Main Authors: Ozgur, Sevim, Buchwald, Gretel, Falk, Sebastian, Chakrabarti, Sutapa, Prabu, Jesuraj Rajan, Conti, Elena
• Format: Journal Article
• Language: English
• Published: England Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies 01.03.2015; Blackwell Publishing Ltd
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; adenosine triphosphate; adenosinetriphosphatase; Biochemistry; Catalytic Domain; Cellular biology; DEAD-box RNA Helicases - chemistry; DEAD-box RNA Helicases - metabolism; DEAD‐box protein; DExH‐box protein; Enzymes; Eukaryotes; Eukaryotic Cells - enzymology; hydrolysis; metabolism; Models, Molecular; Protein Conformation; proteins; Ribonucleic acid; RNA; RNA helicase; RNA helicases; RNA Helicases - chemistry; RNA Helicases - metabolism; RNA‐dependent ATPase; RNA‐protein interaction; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; SF1; SF2; Static Electricity; translation (genetics); RNA-dependent ATPase; DEAD-box protein; RNA-protein interaction; DExH-box protein; SF2; RNA helicase; SF1
• ISSN: 1742-464X; 1742-4658
• DOI: 10.1111/febs.13198

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.