| Literature DB >> 16697179 |
Mary R Stahley1, Scott A Strobel.
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 5'-splice site is selected by formation of a conserved G.U wobble pair between the 5'-exon terminus and the intron. The 3'-splice site is identified through stacking of three base triples, in which the middle triple contains the conserved terminal nucleotide of the intron, OmegaG. 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.Entities:
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Year: 2006 PMID: 16697179 DOI: 10.1016/j.sbi.2006.04.005
Source DB: PubMed Journal: Curr Opin Struct Biol ISSN: 0959-440X Impact factor: 6.809