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Isopentenyl diphosphate isomerase (IDI) is a key enzyme of the isoprenoid pathway, catalyzing the interconversion of isopentenyl diphosphate and dimethylallyl diphosphate, the universal precursors of all isoprenoids. In plants, several subcellular compartments, including cytosol/ER, peroxisomes, mitochondria and plastids, are involved in isoprenoid biosynthesis. Here, we report on the unique triple targeting of two Catharanthus roseus IDI isoforms encoded by a single gene (CrIDI1). The triple localization of CrIDI1 in mitochondria, plastids and peroxisomes is explained by alternative transcription initiation of CrIDI1, by the specificity of a bifunctional N-terminal mitochondria/plastid transit peptide and by the presence of a C-terminal peroxisomal targeting signal. Moreover, bimolecular fluorescence complementation assays revealed self-interactions suggesting that the IDI likely acts as a multimer in vivo.


Grégory Guirimand, Anthony Guihur, Michael A Phillips, Audrey Oudin, Gaëlle Glévarec, Samira Mahroug, Céline Melin, Nicolas Papon, Marc Clastre, Nathalie Giglioli-Guivarc'h, Benoit St-Pierre, Manuel Rodríguez-Concepción, Vincent Burlat, Vincent Courdavault. Triple subcellular targeting of isopentenyl diphosphate isomerases encoded by a single gene. Plant signaling & behavior. 2012 Nov;7(11):1495-7

PMID: 22951398

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