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pubmed-article:15618406pubmed:abstractTextGroup I and II introns self-splice in vitro, but require proteins for efficient splicing in vivo, to stabilize the catalytically active RNA structure. Recent studies showed that the splicing of some Neurospora crassa mitochondrial group I introns additionally requires a DEAD-box protein, CYT-19, which acts as an RNA chaperone to resolve nonnative structures formed during RNA folding. Here we show that, in Saccharomyces cerevisiae mitochondria, a related DEAD-box protein, Mss116p, is required for the efficient splicing of all group I and II introns, some RNA end-processing reactions, and translation of a subset of mRNAs, and that all these defects can be partially or completely suppressed by the expression of CYT-19. Results for the aI2 group II intron indicate that Mss116p is needed after binding the intron-encoded maturase, likely for the disruption of stable but inactive RNA structures. Our results suggest that both group I and II introns are prone to kinetic traps in RNA folding in vivo and that the splicing of both types of introns may require DEAD-box proteins that function as RNA chaperones.lld:pubmed
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pubmed-article:15618406pubmed:authorpubmed-author:JiangYueYlld:pubmed
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pubmed-article:15618406pubmed:articleTitleThe splicing of yeast mitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function.lld:pubmed
pubmed-article:15618406pubmed:affiliationDepartment of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9148, USA.lld:pubmed
pubmed-article:15618406pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15618406pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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