Molecular Biology Reports

, Volume 39, Issue 3, pp 3235–3243

Characterization and subcellular localization of geranylgeranyl diphosphate synthase from Catharanthus roseus

Authors

  • Insaf Thabet
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
    • Département des Sciences Biologiques, Laboratoire de Biotechnologie et Physiologie VégétaleFaculté des Sciences de Tunis
  • Grégory Guirimand
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
  • Anthony Guihur
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
  • Arnaud Lanoue
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
  • Vincent Courdavault
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
  • Nicolas Papon
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
  • Sadok Bouzid
    • Département des Sciences Biologiques, Laboratoire de Biotechnologie et Physiologie VégétaleFaculté des Sciences de Tunis
  • Nathalie Giglioli-Guivarc’h
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
  • Andrew J. Simkin
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
    • EA2106, Biomolécules et Biotechnologies végétalesUniversité François-Rabelais
Article

DOI: 10.1007/s11033-011-1091-9

Cite this article as:
Thabet, I., Guirimand, G., Guihur, A. et al. Mol Biol Rep (2012) 39: 3235. doi:10.1007/s11033-011-1091-9

Abstract

The enzyme geranylgeranyl diphosphate synthase (GGPS: EC 2.5.1.1, EC 2.5.1.10, EC 2.5.1.29) catalyses the formation of geranylgeranyl diphosphate (GGPP) from isopentenyl diphosphate and dimethylallyl diphosphate via three successive condensation reactions. A full-length nucleotide sequence of GGPS (named CrGGPS) was cloned from the medicinal plant Catharanthus roseus. The deduced polypeptide has 383 amino acids with a calculated mass of 41.6 kDa and possesses prenyltransferase signatures characteristic of plant type II GGPS. The enzyme was characterized by functional complementation in carotenoid accumulating strains of Escherichia coli. When cultures of Catharanthus cell lines were treated with methyljasmonate, no specific increase in transcript levels were observed. In plants, GGPS are encoded by a small multigene family and the isoforms have been shown to be localized in three different subcellular compartments: chloroplast, endoplasmic reticulum and mitochondria. We investigated the subcellular distribution of CrGGPS through transient transformations of C. roseus cells with a yellow fluorescent protein-fused construct. Our results clearly indicate that CrGGPS is located to plastids within stroma and stromules.

Keywords

Geranylgeranyl diphosphate synthaseIsoprenoidChloroplastStromuleCatharanthus roseus

Copyright information

© Springer Science+Business Media B.V. 2011