An RNA Switch at the 5′ Splice Site Requires ATP and the DEAD Box Protein Prp28p
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چکیده
منابع مشابه
An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p.
Pre-mRNA splicing requires dramatic RNA rearrangements hypothesized to be catalyzed by ATP-dependent RNA unwindases of the DExD/H box family. In a rearrangement critical for the fidelity of 5' splice site recognition, a base-pairing interaction between the 5' splice site and U1 snRNA must be switched for a mutually exclusive interaction between the 5' splice site and U6 snRNA. By lengthening th...
متن کاملAn RNA Switch at the 59 Splice Site Requires ATP and the DEAD Box Protein Prp28p
site cleavage, the spliceosome rearranges to permit exon ligation (Umen and Guthrie, 1995b), the mRNA and lariat products are released (Company et al. Pre-mRNA splicing requires dramatic RNA rearrange-Since this pathway is conserved from yeast to mammals, ments hypothesized to be catalyzed by ATP-depen-it likely reflects fundamental requirements for intron rec-dent RNA unwindases of the DExD/H ...
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Fidelity and efficiency of pre-mRNA splicing are critical for generating functional mRNAs, but how such accuracy in 5' splice site (SS) selection is attained is not fully clear. Through a series of yeast genetic screens, we isolated alleles of prp28 that improve splicing of suboptimal 5'SS substrates, demonstrating that WT-Prp28p proofreads, and consequently rejects, poor 5'SS. Prp28p is though...
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The yeast PRP28 g ene has been implicated in nuclear precursor messenger RNA (pre-mRNA) splicing, a two-step reaction involved in a multitude of RNA structural alterations. Prp28p, the gene product of PRP28 , is a member of the evolutionarily conserved DEAD-box proteins (DBPs). Members of DBPs are involved in a variety of RNA-related biochemical processes, presumably by their putative RNA helic...
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DbpA is a putative Escherichia coli ATP dependent RNA helicase belonging to the family of DEAD box proteins. It hydrolyzes ATP in the presence of 23S ribosomal RNA and 93 bases in the peptidyl transferase center of 23S rRNA are sufficient to trigger 100% of the ATPase activity of DbpA. In the present study we characterized the ATPase and RNA unwinding activities of DbpA in more detail. We repor...
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ژورنال
عنوان ژورنال: Molecular Cell
سال: 1999
ISSN: 1097-2765
DOI: 10.1016/s1097-2765(00)80174-4