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Nucleic Acids Research, 2000, Vol. 28, No. 8 1743-1750
© 2000 Oxford University Press

NMR studies on functional structures of the AU-rich element-binding domains of Hu antigen C

Makoto Inoue1,2, Yutaka Muto1, Hiroshi Sakamoto3 and Shigeyuki Yokoyama1,2,*

1Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo,7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, 2RIKEN Genomic Sciences Center, Hirosawa, Wako-shi, Saitama 351-0198, Japan and 3Department of Biology, Faculty of Science, Kobe University, Rokkodai, Nada-ku, Kobe 657-8501, Japan

Hu antigen C (HuC) has three RNA-binding domains (RBDs). The N-terminal two, RBD1 and RBD2, are linked in tandem and bind to the AU-rich elements (AREs) in the 3'-untranslated region of particular mRNAs. The solution structures of HuC RBD1 and RBD2 were determined by NMR methods. The HuC RBD1 and RBD2 structures are quite similar to those of Sxl RBD1 and RBD2, respectively. The individual RBDs of HuC, RBD1 and RBD2 in isolation can interact rather weakly with the minimal ARE motif, AUUUA, while the didomain fragment, RBD1–RBD2, of HuC binds more tightly to a longer ARE RNA, UAUUUAUUUU. Chemical shift perturbations by the longer RNA on HuC RBD1–RBD2 were mapped on and around the two ß-sheets and on the C-terminal region of RBD1. The HuC RBD1–RBD2 residues that exhibited significant chemical shift perturbations coincide with those conserved in Sxl RBD1–RBD2. These data indicate that the RNA-binding characteristics of the HuC and Sxl didomain fragments are similar, even though the target RNAs and the biological functions of the proteins are different.

* To whom correspondence should be addressed at: Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. Tel: +81 3 5841 4392; Fax: +81 3 5841 8057; Email: yokoyama@biochem.s.u-tokyo.ac.jp


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