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- Title
Identification and functional analysis of bifunctional ent-kaurene synthase from the moss Physcomitrella patens
- Authors
Hayashi, Ken-ichiro; Kawaide, Hiroshi; Notomi, Miho; Sakigi, Yuka; Matsuo, Akihiko; Nozaki, Hiroshi
- Abstract
Abstract: ent-Kaurene is the key intermediate in biosynthesis of gibberellins (GAs), plant hormones. In higher plants, ent-kaurene is synthesized 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-16α-hydroxykaurene).
- Subjects
HEREDITY; HORMONES; DEVELOPMENTAL biology; BIOCHEMISTRY
- Publication
FEBS Letters, 2006, Vol 580, Issue 26, p6175
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2006.10.018