Structural basis for gibberellin recognition by its receptor GID1

DOI
  • Shimada Asako
    Bioscience and Biotechnology Center, Nagoya University
  • Ueguchi-Tanaka Miyako
    Bioscience and Biotechnology Center, Nagoya University
  • Nakatsu Toru
    Graduate School of Pharmaceutical Sciences, Kyoto University RIKEN Harima Institute at SPring-8
  • Nakajima Masatoshi
    Department of Applied Biological Chemistry, The University of Tokyo
  • Naoe Youichi
    Graduate School of Pharmaceutical Sciences, Kyoto University
  • Ohmiya Hiroko
    Bioscience and Biotechnology Center, Nagoya University
  • Kato Hiroaki
    Graduate School of Pharmaceutical Sciences, Kyoto University RIKEN Harima Institute at SPring-8
  • Matsuoka Makoto
    Bioscience and Biotechnology Center, Nagoya University

Bibliographic Information

Other Title
  • ジベレリン受容体の立体構造を基にした分子進化と基質特異性の解析

Abstract

A nuclear Gibberellin (GA) receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), has a primary structure similar to that of the hormone-sensitive lipases (HSLs). Here we analyze the crystal structure of rice GID1 (OsGID1) bound with GA4 and GA3 at 1.9 Å resolution. The overall structure of both complexes shows an alpha/beta-hydrolase fold similar to that of HSLs. The GA-binding pocket corresponds to the substrate-binding site of HSLs. On the basis of the OsGID1 structure, we mutagenized important residues for GA binding. The replacement of Ile 133 with Leu or Val, residues corresponding to those of the lycophyte GID1s, caused an increase in the binding affinity for GA34, a 2β-hydroxylated GA4. These observations indicate that GID1 originated from HSL and has been further modified to have higher affinity and more strict selectivity for bioactive GAs by adapting the amino acids involved in GA binding in the course of plant evolution.

Journal

Details 詳細情報について

  • CRID
    1390282680606994304
  • NII Article ID
    130006990929
  • DOI
    10.14841/jspp.2009.0.0250.0
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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