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Originally published in Science Express on 21 February 2002
Science 15 March 2002:
Vol. 295. no. 5562, pp. 2084 - 2088
DOI: 10.1126/science.1069268
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Reports
Structural Insights into Group II Intron Catalysis and Branch-Site Selection
Lan Zhang,1
Jennifer A. Doudna12*
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.
1 Department of Molecular Biophysics and
Biochemistry and
2 Howard Hughes Medical Institute,
Yale University, New Haven, CT 06520, USA.
*
To whom correspondence should be addressed. E-mail:
jennifer.doudna{at}yale.edu
Read the Full Text
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