doi: 10.1016/s0092-8674(02)00771-7.
A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
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- PMID: 12086675
- DOI: 10.1016/s0092-8674(02)00771-7
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A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
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Abstract
The Neurospora crassa CYT-18 protein, the mitochondrial tyrosyl-tRNA synthetase, functions in splicing group I introns by inducing formation of the catalytically active RNA structure. Here, we identified a DEAD-box protein (CYT-19) that functions in concert with CYT-18 to promote group I intron splicing in vivo and vitro. CYT-19 does not bind specifically to group I intron RNAs and instead functions as an ATP-dependent RNA chaperone to destabilize nonnative RNA structures that constitute kinetic traps in the CYT-18-assisted RNA-folding pathway. Our results demonstrate that a DExH/D-box protein has a specific, physiologically relevant chaperone function in the folding of a natural RNA substrate.
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