Study of divinyl ether synthase in potato tubers (Solanum tuberosum L.)

Poster (2001, April 18)

Potato tubers exhibit both homolytic and heterolytic hydroperoxide fatty acid cleaving activities

Poster (2000, July 23)

Identification de cultivars de palmier dattier (Phoenix dactylifera L.) par l'amplification aléatoire d'ADN (RAPD)

in Cahiers Agricultures (2000), 9(2), 103-107

Breeding for "low-gossypol seed and high-gossypol plants" in upland cotton. Analysis of tri-species hybrids and backcross progenies using AFLPs and mapped RFLPs.

in Theoretical and Applied Genetics (1999), 99(7-8),

Use of randomly amplified polymorphic DNA (RAPD) markers to assist wide hybridization in cotton

in Biotechnology in Agriculture and Forestry (1998)

Development of an interspecific breeding programme in cotton assisted by RAPD markers

in Cotton biotechnology (1995)

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 ▲]

Expression Of Intron-Encoded Maturase-Like Polypeptides In Potato Chloroplasts

in Current Genetics (1994), 25(2),