Entity

Time filter

Source Type


Mahjoub A.,Laboratoire Of Botanique | Mahjoub A.,Tunisie Unite Of Genetique Et Of Bio Ressources | Abdellaoui R.,Laboratoire Of Biotechnologie Et Physiologie Vegetale | Naceur M.B.,Laboratoire Of Biotechnologie Et Physiologie Vegetale | Brahim N.B.,Laboratoire Of Botanique
Acta Botanica Gallica | Year: 2010

Genetic diversity of three durum wheat cultivars (Triticum durum Desf.) and thirteen Aegilops geniculata Roth accessions belonging to different regions of Tunisia (in North and Central) was evaluated using random amplified polymorphic DNA (RAPD) markers. Nineteen arbitrary universal primers were used for the amplification of random DNA sequences. Data were analysed with the SIMQUAL program using the NTSYS-pc. Phylogenetic diagram was drowning using the UPGMA algorithm. Results indicate an important inter-specific polymorphism between Aegilops and durum wheat. Ae. geniculata accessions revealed a high level of polymorphism (71.27%) than wheat cultivars (39.76%). Two main groups were represented by cluster and principal component analyses. The first group is formed by Ae. geniculata accessions and the second is constituted only by durum wheat cultivars. Consequently, RAPD markers separate clearly Ae. geniculata accessions and durum wheat cultivars. Source


Simkin A.J.,CNRS Biomolecule and Plant Biotechnology Laboratory | Guirimand G.,CNRS Biomolecule and Plant Biotechnology Laboratory | Papon N.,CNRS Biomolecule and Plant Biotechnology Laboratory | Courdavault V.,CNRS Biomolecule and Plant Biotechnology Laboratory | And 6 more authors.
Planta | Year: 2011

In plants, the mevalonic acid (MVA) pathway provides precursors for the formation of triterpenes, sesquiterpenes, phytosterols and primary metabolites important for cell integrity. Here, we have cloned the cDNA encoding enzymes catalysing the final three steps of the MVA pathway from Madagascar periwinkle (Catharanthus roseus), mevalonate kinase (MVK), 5-phosphomevalonate kinase (PMK) and mevalonate 5-diphosphate decarboxylase (MVD). These cDNA were shown to functionally complement MVA pathway deletion mutants in the yeast Saccharomyces cerevisiae. Transient transformations of C. roseus cells with yellow fluorescent protein (YFP)-fused constructs reveal that PMK and MVD are localised to the peroxisomes, while MVK was cytosolic. These compartmentalisation results were confirmed using the Arabidopsis thaliana MVK, PMK and MVD sequences fused to YFP. Based on these observations and the arguments raised here we conclude that the final steps of the plant MVA pathway are localised to the peroxisome. © 2011 Springer-Verlag. Source


Thabet I.,University of Tours | Thabet I.,Laboratoire Of Biotechnologie Et Physiologie Vegetale | Guirimand G.,University of Tours | Guihur A.,University of Tours | And 7 more authors.
Molecular Biology Reports | Year: 2011

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. © 2011 Springer Science+Business Media B.V. Source


Thabet I.,University of Tours | Thabet I.,Laboratoire Of Biotechnologie Et Physiologie Vegetale | Gregory Guirimand G.,University of Tours | Guihur A.,University of Tours | And 8 more authors.
Molecular Biology Reports | Year: 2012

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.© Springer Science+Business Media B.V. 2011. Source

Discover hidden collaborations