Abstract
Proteins with RNA chaperone activity are ubiquitous proteins that play important roles in cellular mechanisms. They prevent RNA from misfolding by loosening misfolded structures without ATP consumption. RNA chaperone activity is studied in vitro and in vivo using oligonucleotide- or ribozyme-based assays. Due to their functional as well as structural diversity, a common chaperoning mechanism or universal motif has not yet been identified. A growing database of proteins with RNA chaperone activity has been established based on evaluation of chaperone activity via the described assays. Although the exact mechanism is not yet understood, it is more and more believed that disordered regions within proteins play an important role. This possible mechanism and which proteins were found to possess RNA chaperone activity are discussed here.
Highlights
Among all biological macromolecules, RNAs represent one of the most functionally versatile players in the cell
As proteins with RNA chaperone activity are very heterogeneous concerning their structure and their way to resolve the folding of RNA molecules, there are various RNA chaperone assays available to measure different activities
Analogous to the annealing assays, melting activity can be detected by using native gel electrophoresis or by measuring loss of fluorescence energy resonance transfer (FRET) that occurs upon dissociation of the complementary fluorophor labelled RNAs
Summary
RNAs represent one of the most functionally versatile players in the cell. RNA molecules often undergo transition states during their folding pathways before they reach the native and active structure. These transient structures can represent traps along the folding pathway from which the molecules might have a hard time to escape and which end up being long-lived intermediates. The reason for this structural versatility is the fact that RNA consists of only four different bases which are capable of forming stable helices, that are not necessarily the native structure. Biochemistry Research International chaperone activity and discuss possible mechanisms of RNA chaperoning
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