Study on gibberellin perception

点击翻译按钮获取中文摘要

We analyzed the 3D structure of rice GA receptor (OsGID1) bound with GA. The overall structure shows an α/β-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 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 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.