2008年
Structural basis for gibberellin recognition by its receptor GID1
Nature
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- 巻
- 456
- 号
- 7221
- 開始ページ
- 520
- 終了ページ
- U44
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/nature07546
- 出版者・発行元
- NATURE PUBLISHING GROUP
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.
- リンク情報
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- DOI
- https://doi.org/10.1038/nature07546
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000261170500042&DestApp=WOS_CPL
- URL
- http://www.scopus.com/inward/record.url?eid=2-s2.0-57049177946&partnerID=MN8TOARS
- ID情報
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- DOI : 10.1038/nature07546
- ISSN : 0028-0836
- ORCIDのPut Code : 58433919
- SCOPUS ID : 57049177946
- Web of Science ID : WOS:000261170500042