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- W2955851284 abstract "We describe a strategy for tracking Mg2+-initiated folding of 32P-labeled tRNA molecules to their native structures based on capacity for aminoacylation by the cognate aminoacyl-tRNA synthetase enzyme. The approach directly links folding to function, paralleling a common strategy used to study the folding of catalytic RNAs. Incubation of unfolded tRNA with magnesium ions, followed by addition of tRNA synthetase and further incubation, yields a rapid burst of aminoacyl-tRNA formation corresponding to the prefolded tRNA fraction. A subsequent slower increase in product formation monitors continued folding in the presence of enzyme. Further analysis reveals the presence of a parallel fraction of tRNA that folds more rapidly than the majority of the population. Application of the approach to study the influence of post-transcriptional modifications in folding of E. coli tRNA1 Gln reveals that the modified bases increase the folding rate but do not affect either the equilibrium between properly folded and misfolded states or the apparent folding pathway. This assay allows the use of 32P-labeled tRNA in integrated studies combining folding, post-transcriptional processing and aminoacylation reactions. The assay also allows tracking folding of mitochondrial tRNAs, the native structures of many of which are poorly characterized." @default.
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- W2955851284 date "2012-04-01" @default.
- W2955851284 modified "2023-10-16" @default.
- W2955851284 title "Kinetics of tRNA Folding Monitored by Aminoacylation" @default.
- W2955851284 doi "https://doi.org/10.1096/fasebj.26.1_supplement.945.2" @default.
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