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Structural Insights into Group II Intron Catalysis and Branch-Site Selection

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Science  15 Mar 2002:
Vol. 295, Issue 5562, pp. 2084-2088
DOI: 10.1126/science.1069268

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Abstract

Group II self-splicing introns catalyze autoexcision from precursor RNA transcripts by a mechanism strikingly similar to that of the spliceosome, an RNA-protein assembly responsible for splicing together the protein-coding parts of most eukaryotic pre-mRNAs. Splicing in both cases initiates via nucleophilic attack at the 5′ splice site by the 2′ OH of a conserved intron adenosine residue, creating a branched (lariat) intermediate. Here, we describe the crystal structure at 3.0 Å resolution of a 70-nucleotide RNA containing the catalytically essential domains 5 and 6 of the yeast ai5γ group II self-splicing intron, revealing an unexpected two-nucleotide bulged structure around the branch-point adenosine in domain 6.

  • * To whom correspondence should be addressed. E-mail: jennifer.doudna{at}yale.edu

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