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The subcellular localization of periwinkle farnesyl diphosphate synthase provides insight into the role of peroxisome in isoprenoid biosynthesis

Thabet, Insaf, Guirimand, Grégory, Courdavault, Vincent, Papon, Nicolas, Godet, Stéphanie, Dutilleul, Christelle, Bouzid, Sadok, Giglioli-Guivarc’h, Nathalie, Clastre, Marc, Simkin, Andrew J. and others. (2011) The subcellular localization of periwinkle farnesyl diphosphate synthase provides insight into the role of peroxisome in isoprenoid biosynthesis. Journal of Plant Physiology, 168 (17). pp. 2110-2116. ISSN 0176-1617. (doi:10.1016/j.jplph.2011.06.017) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:93881)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL:
https://doi.org/10.1016/j.jplph.2011.06.017

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.

Item Type: Article
DOI/Identification number: 10.1016/j.jplph.2011.06.017
Uncontrolled keywords: Catharanthus roseus; Farnesyl diphosphate synthase; Isoprenoid; Peroxisome; Prenyltransferase
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Andrew Simkin
Date Deposited: 05 May 2022 18:51 UTC
Last Modified: 06 May 2022 09:46 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/93881 (The current URI for this page, for reference purposes)

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