Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1979594 | Current Opinion in Structural Biology | 2006 | 8 Pages |
Abstract
The group I intron has served as a model for RNA catalysis since its discovery 25 years ago. Four recently determined high-resolution crystal structures complement extensive biochemical studies on this system. Structures of the Azoarcus, Tetrahymena and bacteriophage Twort group I introns mimic different states of the splicing or ribozyme reaction pathway and provide information on splice site selection and metal ion catalysis. The 5â²-splice site is selected by formation of a conserved G·U wobble pair between the 5â²-exon terminus and the intron. The 3â²-splice site is identified through stacking of three base triples, in which the middle triple contains the conserved terminal nucleotide of the intron, ΩG. The structures support a two-metal-ion mechanism for group I intron splicing that might have corollaries to group II intron and pre-mRNA splicing by the spliceosome.
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Authors
Mary R Stahley, Scott A Strobel,