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The subcellular localization of periwinkle farnesyl diphosphate synthase provides insight into the role of peroxisome in isoprenoid biosynthesis
Authors:Thabet Insaf  Guirimand Grégory  Courdavault Vincent  Papon Nicolas  Godet Stéphanie  Dutilleul Christelle  Bouzid Sadok  Giglioli-Guivarc'h Nathalie  Clastre Marc  Simkin Andrew J
Institution:a Université François-Rabelais de Tours, EA2106, Biomolécules et Biotechnologies Végétales, 31 Avenue Monge, 37200 Tours, France
b Laboratoire de Biotechnologie et Physiologie Végétale, Faculté des Sciences de Tunis, Département des Sciences Biologiques, 2092 El-Manar II, Tunis, Tunisia
Abstract:Farnesyl diphosphate (FPP) synthase (FPS: EC.2.5.1.1, EC.2.5.1.10) catalyzes the formation of FPP from isopentenyl diphosphate and dimethylallyl diphosphate via two successive condensation reactions. A cDNA designated CrFPS, encoding a protein showing high similarities with trans-type short FPS isoforms, was isolated from the Madagascar periwinkle (Catharanthus roseus). This cDNA was shown to functionally complement the lethal FPS deletion mutant in the yeast Saccharomyces cerevisiae. At the subcellular level, while short FPS isoforms are usually described as cytosolic proteins, we showed, using transient transformations of C. roseus cells with yellow fluorescent protein-fused constructs, that CrFPS is targeted to peroxisomes. This finding is discussed in relation to the subcellular distribution of FPS isoforms in plants and animals and opens new perspectives towards the understanding of isoprenoid biosynthesis.
Keywords:DMAPP  dimethylallyl diphosphate  FOA  5-fluoroorotic acid  FPP  farnesyl diphosphate  FPS  farnesyl diphosphate synthase  IPP  isopentenyl diphosphate  MVA  mevalonic acid  PTS  peroxisomal targeting signal  YFP  yellow fluorescent protein
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