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The guanosine binding mechanism of the Tetrahymena group I intron.
Authors:A Kitamura  Y Muto  S Watanabe  I Kim  T Ito  Y Nishiya  T Ohtsuki  G Kawai  K Watanabe  K Hosono  H Takaku  E Katoh  T Yamazaki  T Inoue  S Yokoyama
Affiliation:Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
Abstract:The Tetrahymena group I intron catalyzes self-splicing through two consecutive transesterification reactions, using a single guanosine-binding site (GBS). In this study, we constructed a model RNA that contains the GBS and a conserved guanosine nucleotide at the 3'-terminus of the intron (omegaG). We determined by NMR the solution structure of this model RNA, and revealed the guanosine binding mechanism of the group I intron. The G22 residue, corresponding to omegaG, participates in a base triple, G22 xx G3 x C12, hydrogen-bonding to the major groove edge of the Watson-Crick G3 x C12 pair. The G22 residue also interacts with A2, which is semi-conserved in all sequenced group I introns.
Keywords:
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