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Published Online February 21, 2002
Science
DOI: 10.1126/science.1069268
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Reports
Submitted on December 21, 2001
Accepted on February 4, 2002
Structural Insights into Group II Intron Catalysis and Branch-Site Selection
Lan Zhang 1
Jennifer A. Doudna 2*
1 Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520.
2 Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT 06520.
* To whom correspondence should be addressed. E-mail: jennifer.doudna{at}yale.edu.
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 ai5 group II self-splicing intron, revealing an unexpected two-nucleotide bulged structure around the branch-point adenosine in domain 6.
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