Crystal Structure of a Group I Ribozyme Domain: Principles of RNA Packing

  • Jamie H. Cate
    J. H. Cate, K. Zhou, and J. A. Doudna are in the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA;
  • Anne R. Gooding
    A. R. Gooding, E. Podell, B. L. Golden, C. E. Kundrot, and T. R. Cech are in the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA;
  • Elaine Podell
    A. R. Gooding, E. Podell, B. L. Golden, C. E. Kundrot, and T. R. Cech are in the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA;
  • Kaihong Zhou
    J. H. Cate, K. Zhou, and J. A. Doudna are in the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA;
  • Barbara L. Golden
    A. R. Gooding, E. Podell, B. L. Golden, C. E. Kundrot, and T. R. Cech are in the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA;
  • Craig E. Kundrot
    A. R. Gooding, E. Podell, B. L. Golden, C. E. Kundrot, and T. R. Cech are in the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA;
  • Thomas R. Cech
    A. R. Gooding, E. Podell, B. L. Golden, C. E. Kundrot, and T. R. Cech are in the Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA;
  • Jennifer A. Doudna
    J. H. Cate, K. Zhou, and J. A. Doudna are in the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA;

抄録

<jats:p> Group I self-splicing introns catalyze their own excision from precursor RNAs by way of a two-step transesterification reaction. The catalytic core of these ribozymes is formed by two structural domains. The 2.8-angstrom crystal structure of one of these, the P4-P6 domain of the <jats:italic>Tetrahymena thermophila</jats:italic> intron, is described. In the 160-nucleotide domain, a sharp bend allows stacked helices of the conserved core to pack alongside helices of an adjacent region. Two specific long-range interactions clamp the two halves of the domain together: a two-Mg <jats:sup>2+</jats:sup> -coordinated adenosine-rich corkscrew plugs into the minor groove of a helix, and a GAAA hairpin loop binds to a conserved 11-nucleotide internal loop. Metal- and ribose-mediated backbone contacts further stabilize the close side-by-side helical packing. The structure indicates the extent of RNA packing required for the function of large ribozymes, the spliceosome, and the ribosome. </jats:p>

収録刊行物

  • Science

    Science 273 (5282), 1678-1685, 1996-09-20

    American Association for the Advancement of Science (AAAS)

被引用文献 (11)*注記

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ