| pubmed-article:19393667 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19393667 | lifeskim:mentions | umls-concept:C0237868 | lld:lifeskim |
| pubmed-article:19393667 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:19393667 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:19393667 | lifeskim:mentions | umls-concept:C0205276 | lld:lifeskim |
| pubmed-article:19393667 | lifeskim:mentions | umls-concept:C0036679 | lld:lifeskim |
| pubmed-article:19393667 | lifeskim:mentions | umls-concept:C1704973 | lld:lifeskim |
| pubmed-article:19393667 | lifeskim:mentions | umls-concept:C2247938 | lld:lifeskim |
| pubmed-article:19393667 | lifeskim:mentions | umls-concept:C1511545 | lld:lifeskim |
| pubmed-article:19393667 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:19393667 | pubmed:dateCreated | 2009-6-1 | lld:pubmed |
| pubmed-article:19393667 | pubmed:abstractText | The DEAD-box proteins CYT-19 in Neurospora crassa and Mss116p in Saccharomyces cerevisiae are broadly acting RNA chaperones that function in mitochondria to stimulate group I and group II intron splicing and to activate mRNA translation. Previous studies showed that the S. cerevisiae cytosolic/nuclear DEAD-box protein Ded1p could stimulate group II intron splicing in vitro. Here, we show that Ded1p complements mitochondrial translation and group I and group II intron splicing defects in mss116Delta strains, stimulates the in vitro splicing of group I and group II introns, and functions indistinguishably from CYT-19 to resolve different nonnative secondary and/or tertiary structures in the Tetrahymena thermophila large subunit rRNA-DeltaP5abc group I intron. The Escherichia coli DEAD-box protein SrmB also stimulates group I and group II intron splicing in vitro, while the E. coli DEAD-box protein DbpA and the vaccinia virus DExH-box protein NPH-II gave little, if any, group I or group II intron splicing stimulation in vitro or in vivo. The four DEAD-box proteins that stimulate group I and group II intron splicing unwind RNA duplexes by local strand separation and have little or no specificity, as judged by RNA-binding assays and stimulation of their ATPase activity by diverse RNAs. In contrast, DbpA binds group I and group II intron RNAs nonspecifically, but its ATPase activity is activated specifically by a helical segment of E. coli 23S rRNA, and NPH-II unwinds RNAs by directional translocation. The ability of DEAD-box proteins to stimulate group I and group II intron splicing correlates primarily with their RNA-unwinding activity, which, for the protein preparations used here, was greatest for Mss116p, followed by Ded1p, CYT-19, and SrmB. Furthermore, this correlation holds for all group I and group II intron RNAs tested, implying a fundamentally similar mechanism for both types of introns. Our results support the hypothesis that DEAD-box proteins have an inherent ability to function as RNA chaperones by virtue of their distinctive RNA-unwinding mechanism, which enables refolding of localized RNA regions or structures without globally disrupting RNA structure. | lld:pubmed |
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| pubmed-article:19393667 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19393667 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19393667 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19393667 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19393667 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19393667 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:19393667 | pubmed:issn | 1089-8638 | lld:pubmed |
| pubmed-article:19393667 | pubmed:author | pubmed-author:JiangYueY | lld:pubmed |
| pubmed-article:19393667 | pubmed:author | pubmed-author:JankowskyEckh... | lld:pubmed |
| pubmed-article:19393667 | pubmed:author | pubmed-author:LambowitzAlan... | lld:pubmed |
| pubmed-article:19393667 | pubmed:author | pubmed-author:MohrSabineS | lld:pubmed |
| pubmed-article:19393667 | pubmed:author | pubmed-author:Del... | lld:pubmed |
| pubmed-article:19393667 | pubmed:author | pubmed-author:JiaHuijueH | lld:pubmed |
| pubmed-article:19393667 | pubmed:issnType | Electronic | lld:pubmed |
