@article {377,
	title = {A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing.},
	journal = {Cell},
	volume = {109},
	number = {6},
	year = {2002},
	month = {2002 Jun 14},
	pages = {769-79},
	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.},
	keywords = {Adenosine Triphosphatases, Adenosine Triphosphate, Alternative Splicing, Base Sequence, Blotting, Northern, Cloning, Molecular, Dose-Response Relationship, Drug, Fungal Proteins, Immunoblotting, Introns, Kinetics, Models, Genetic, Molecular Sequence Data, Mutation, Neurospora crassa, Nucleic Acid Conformation, Open Reading Frames, Phenotype, RNA, Substrate Specificity, Temperature, Time Factors},
	issn = {0092-8674},
	author = {Mohr, Sabine and Stryker, John M and Lambowitz, Alan M}
}
