Solution structure of an RNA fragment with the P7/P9.0 region and the 3′-terminal guanosine of the Tetrahymena group I intron

Aya Kitamura, Yutaka Muto, Satoru Watanabe, Insil Kim, Takuhiro Ito, Yoichi Nishiya, Kensaku Sakamoto, Takashi Ohtsuki, Gota Kawai, Kimitsuna Watanabe, Kazumi Hosono, Hiroshi Takaku, Etsuko Katoh, Toshimasa Yamazaki, Tan Inoue, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


In the second step of the two consecutive transesterifications of the self-splicing reaction of the group I intron, the conserved guanosine at the 3′ terminus of the intron (ωG) binds to the guanosine-binding site (GBS) in the intron. In the present study, we designed a 22-nt model RNA (GBS/ωG) including the GBS and ωG from the Tetrahymena group I intron, and determined the solution structure by NMR methods. In this structure, ωG is recognized by the formation of a base triple with the G264·C311 base pair, and this recognition is stabilized by the stacking interaction between ωG and C262. The bulged structure at A263 causes a large helical twist angle (40 ± 8°) between the G264·C311 and C262·G312 base pairs. We named this type of binding pocket with a bulge and a large twist, formed on the major groove, a "Bulge-and-Twist" (BT) pocket. With another twist angle between the C262·G312 and G413·C313 base pairs (45 ± 10°), the axis of GBS/ωG is kinked at the GBS region. This kinked axis superimposes well on that of the corresponding region in the structure model built on a 5.0 Å resolution electron density map (Golden et al., Science, 1998, 282:345-358). This compact structure of the GBS is also consistent with previous biochemical studies on group I introns. The BT pockets are also found in the arginine-binding site of the HIV-TAR RNA, and within the 16S rRNA and the 23S rRNA.

Original languageEnglish
Pages (from-to)440-451
Number of pages12
Issue number4
Publication statusPublished - 2002
Externally publishedYes


  • NMR
  • RNA structure
  • Ribozyme
  • Self-splicing

ASJC Scopus subject areas

  • Molecular Biology


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