The guanosine binding mechanism of the Tetrahymena group I intron.

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

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1 Citation (Scopus)


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.

Original languageEnglish
Pages (from-to)191-192
Number of pages2
JournalNucleic acids symposium series
Issue number42
Publication statusPublished - 1999
Externally publishedYes

ASJC Scopus subject areas

  • General Medicine


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