Structural basis for gibberellin recognition by its receptor GID1

被引:267
作者
Shimada, Asako [2 ]
Ueguchi-Tanaka, Miyako [2 ]
Nakatsu, Toru [1 ,3 ]
Nakajima, Masatoshi [4 ]
Naoe, Youichi [1 ]
Ohmiya, Hiroko [2 ]
Kato, Hiroaki [1 ,3 ]
Matsuoka, Makoto [2 ]
机构
[1] Kyoto Univ, Dept Biol Struct, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan
[2] Nagoya Univ, Biosci & Biotechnol Ctr, Nagoya, Aichi 4648601, Japan
[3] RIKEN, Harima Inst SPring 8, Mikazuki, Hyogo 6795148, Japan
[4] Univ Tokyo, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1138657, Japan
基金
日本学术振兴会;
关键词
D O I
10.1038/nature07546
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Gibberellins ( GAs) are phytohormones essential for many developmental processes in plants(1). A nuclear GA receptor, GIBBERELLIN INSENSITIVEDWARF1 ( GID1), has a primary structure similar to that of the hormone- sensitive lipases (HSLs)(2,3). Here we analyse the crystal structure of Oryza sativa GID1 (OsGID1) bound with GA(4) and GA(3) at 1.9 angstrom resolution. The overall structure of both complexes shows an alpha/beta-hydrolase fold similar to that of HSLs except for an amino- terminal lid. 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 and examined their binding activities. Almost all of them showed very little or no activity, confirming that the residues revealed by structural analysis are important for GA binding. The replacement of Ile 133 with Leu or Val - residues corresponding to those of the lycophyte Selaginella moellendorffii GID1s - caused an increase in the binding affinity for GA(34), a 2 beta-hydroxylated GA(4). These observations indicate that GID1 originated from HSL and was 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.
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收藏
页码:520 / U44
页数:5
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