Access

Article

Nature 398, 579-585 (15 April 1999) | doi:10.1038/19242; Received 20 November 1998; Accepted 10 March 1999

Open Innovation Challenges

  • Methods to Analyze Consumer Emotions

    • Deadline: Jan 17 2010
    • Reward: $10,000 USD

    The Seeker is looking for methods to analyze consumer emotions. This Challenge requires only a writ...

  • Single-cell Analysis Platform

    • Deadline: Dec 02 2009
    • Reward: $5,000 USD

    This Challenge is looking for novel approaches to analyzing changes at a single-cell level. This is...

naturejobs

More science jobs
Post a job for free

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

Noriko Handa1, Osamu Nureki1,2, Kazuki Kurimoto1, Insil Kim1, Hiroshi Sakamoto3, Yoshiro Shimura4,5, Yutaka Muto1 & Shigeyuki Yokoyama1,2

  1. Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
  2. Genomic Sciences Center and Cellular Signaling Laboratory, The Institute of Physical and Chemical Research (RIKEN), 2-1 Hirosawa, Wako, Saitama 351-0106, Japan
  3. Department of Biology, Faculty of Science, Kobe University, 1-1 Rokkodaicho, Nada-ku, Kobe 657-0013, Japan
  4. Department of Biophysics, Faculty of Science, Kyoto University, Oiwake-cho, Kitashirakawa, Sakyo-ku, Kyoto 606-8224, Japan
  5. Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan

Correspondence to: Shigeyuki Yokoyama1,2 Correspondence and requests for materials should be addressed to S.Y.
(e-mail: Email: yokoyama@y-sun.biochem.s.u-tokyo.ac.jp).The coordinates for the Sxldot RNA complex have been deposited in the Brook haven Protein Data Bank, accession code 1B7F.

Top

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 beta-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.