Changes In Oxylipin Synthesis After Phytophthora Infestans Infection Of Potato Leaves Do Not Correlate With Resistance

in Plant Physiology and Biochemistry (2008), 46(8-9), 823-831

Characterization of potato tuber ageing using physiological markers and proteomic data based on DIGE proteome analysis and antioxidant activities assessment

Poster (2006, December 18)

Changes in redox status and oxylipin profiles during source-potato tuber ageing.

Poster (2006)

Optimisation de la transformation génétique de la pomme de terre par Agrobacterium tumefaciens. Utilisation de la résistance à l'hygromycine comme marqueur sélectif.

in Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE] (2003), 7

Lipoxygenase Pathway And Membrane Permeability And Composition During Storage Of Potato Tubers (Solanum Tuberosum L. Cv Bintje And Desiree) In Different Conditions

in Plant Biology (2002), 4(1),

Evolution of membrane permeability and composition during storage of potato tubers (Solanum tuberosum L. cv Bintje and Désirée) in different conditions and in relation with lipoxygenase activity

Poster (2001, November 19)

Study of lipoxygenase activity during storage of potato tubers (Solanum tuberosum L.) in relation with membrane integrity.

Poster (2001, June 06)

Molecular cloning and characterization of a soluble inorganic pyrophosphatase in potato.

in Plant Physiology (1995), 109(3), 853-60

A cDNA clone encoding a soluble inorganic pyrophosphatase (EC 3.6.1.1) of potato (Solanum tuberosum L.) was isolated by screening a developing tuber library with a heterologous probe. The central domain ... [more ▼]

A cDNA clone encoding a soluble inorganic pyrophosphatase (EC 3.6.1.1) of potato (Solanum tuberosum L.) was isolated by screening a developing tuber library with a heterologous probe. The central domain of the encoded polypeptide is nearly identical at the sequence level with its Arabidopsis homolog (J.J. Kieber and E.R. Signer [1991] Plant Mol Biol 16: 345-348). Computer-assisted analysis of the potato, Arabidopsis, and Escherichia coli soluble pyrophosphatases indicated a remarkably conserved organization of the hydrophobic protein domains. The enzymatic function of the potato protein could be deduced from the presence of amino acid residues highly conserved in soluble pyrophosphatases and was confirmed by its capacity to complement a thermosensitive pyrophosphatase mutation in E. coli. The potato polypeptide was purified from complemented bacterial cells and its pyrophosphatase activity was shown to be strictly dependent on Mg2+ and strongly inhibited by Ca2+. The subcellular location of the potato pyrophosphatase is unknown. Structure analysis of the N-terminal protein domain failed to recognize typical transit peptides and the calculated molecular mass of the polypeptide (24 kD) is significantly inferior to the values reported for the plastidic (alkaline) or mitochondrial pyrophosphatases in plants (28-42 kD). Two unlinked loci could be mapped by restriction fragment length polymorphism analysis in the potato genome using the full-length cDNA as probe. [less ▲]