Identification and functional analysis of bifunctional ent-kaurene synthase from the moss Physcomitrella patens

被引：176
作者：
Hayashi, Ken-ichiro
Kawaide, Hiroshi
Notomi, Miho
Sakigi, Yuka
Matsuo, Akihiko
Nozaki, Hiroshi
机构：
[1] Okayama Univ Sci, Dept Biochem, Okayama 7000005, Japan
[2] Tokyo Univ Agr & Technol, Inst Symbiot Sci & Technol, Div Agrisci & Biosci, Fuchu, Tokyo 1838509, Japan
[3] Kure Univ, Fac Social Informat Sci, Div Environm Biochem, Kure, Hiroshima 72407, Japan
来源：
FEBS LETTERS | 2006年 / 580卷 / 26期
基金：
日本学术振兴会;
关键词：
ent-kaurene synthase; moss; gibberellin; biosynthesis; Physcomitrella patens;
D O I：
10.1016/j.febslet.2006.10.018
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
ent-Kaurene is the key intermediate in biosynthesis of gibberellins; (GAs), plant hormones. In higher plants, ent-kaurene is svnthesized successively by copalyl diphosphate synthase (CPS) and ent-kaurene synthase (KS) from geranylgeranyl diphosphate (GGDP). On the other hand, fungal ent-kaurene synthases are bifunctional cyclases with both CPS and KS activity in a single polypeptide. The moss Physcomitrella patens is a model organism for the study of genetics and development in an early land plant. We identified ent-kaurene synthase (PpCPS/KS) from P. patens and analyzed its function. PpCPS/KS cDNA encodes a 101-kDa polypeptide, and shows high similarity with CPSs and abietadiene synthase from higher plants. PpCPS/KS is a bifunctional cyclase and, like fungal CPS/KS, directly synthesizes the ent-kaurene skeleton from GGDP. PpCPS/KS has two aspartate-rich DVDD and DDYFD motifs observed in CPS and KS, respectively. The mutational analysis of two conserved motifs in PpCPS/KS indicated that the DVDD motif is responsible for CPS activity (GGDP to CDP) and the DDYFD motif for KS activity (CDP to ent-kaurene and ent-16 alpha-hydroxy-kaurene). (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码：6175 / 6181
页数：7
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