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Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein

Author

Listed:
  • Noriko Handa

    (Graduate School of Science, University of Tokyo)

  • Osamu Nureki

    (Graduate School of Science, University of Tokyo
    Genomic Sciences Center and Cellular Signaling Laboratory, The Institute of Physical and Chemical Research (RIKEN))

  • Kazuki Kurimoto

    (Graduate School of Science, University of Tokyo)

  • Insil Kim

    (Graduate School of Science, University of Tokyo)

  • Hiroshi Sakamoto

    (Faculty of Science, Kobe University)

  • Yoshiro Shimura

    (Faculty of Science, Kyoto University
    Biomolecular Engineering Research Institute)

  • Yutaka Muto

    (Graduate School of Science, University of Tokyo)

  • Shigeyuki Yokoyama

    (Graduate School of Science, University of Tokyo
    Genomic Sciences Center and Cellular Signaling Laboratory, The Institute of Physical and Chemical Research (RIKEN))

Abstract

The Sex-lethal (Sxl) protein of Drosophila melanogaster regulates alternative splicing of the transformer (tra) messenger RNA precursor by binding to the tra polypyrimidine tract during the sex-determination process. The crystal structure has now been determined at 2.6 Å resolution of the complex formed between two tandemly arranged RNA-binding domains of the Sxl protein and a 12-nucleotide, single-stranded RNA derived from the tra polypyrimidine tract. The two RNA-binding domains have their β-sheet platforms facing each other to form a V-shaped cleft. The RNA is characteristically extended and bound in this cleft, where the UGUUUUUUU sequence is specifically recognized by the protein. This structure offers the first insight, to our knowledge, into how a protein binds specifically to a cognate RNA without any intramolecular base-pairing.

Suggested Citation

  • Noriko Handa & Osamu Nureki & Kazuki Kurimoto & Insil Kim & Hiroshi Sakamoto & Yoshiro Shimura & Yutaka Muto & Shigeyuki Yokoyama, 1999. "Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein," Nature, Nature, vol. 398(6728), pages 579-585, April.
    • Handle: RePEc:nat:nature:v:398:y:1999:i:6728:d:10.1038_19242
    DOI: 10.1038/19242
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    Cited by:

    1. Malgorzata M. Duszczyk & Harry Wischnewski & Tamara Kazeeva & Rajika Arora & Fionna E. Loughlin & Christine Schroetter & Ugo Pradère & Jonathan Hall & Constance Ciaudo & Frédéric H.-T. Allain, 2022. "The solution structure of Dead End bound to AU-rich RNA reveals an unusual mode of tandem RRM-RNA recognition required for mRNA regulation," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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