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Overexpression of a heterologous sam gene encoding S-adenosylmethionine synthetase in flax (Linum usitatissimum) cells: Consequences on methylation of lignin precursors and pectins.
Lamblin, Frédéric; Saladin, Gaëlle; Dehorter, Bertrand; Cronier, David; Grenier, Emmanuel; Lacoux, Jérôme; Bruyant, Philippe; Lainé, Eric; Chabbert, Brigitte; Girault, Fabienne; Monties, Bernard; Morvan, Claudine; David, Hélène; David, Alain.
Afiliação
  • Lamblin F; Laboratoire de Biotechnologie et Physiologie Végétales, Faculté des Sciences, Université de Picardie Jules Verne, 33 rue Saint-Leu, F-80039 Amiens cedex, France Equipe Parois et Polymères Pariétaux, SCUEOR ESA CNRS 6037, F-76821 Mt Saint Aignan cedex, France Laboratoire de Physiologie des Parois Végétales, UPRES 2702, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq cedex, France Equipe Biochimie des Macromolécules Végétales, UPBP, INRA, BP 286, F-51686 Reims cedex, Fr
Physiol Plant ; 112(2): 223-232, 2001 Jun.
Article em En | MEDLINE | ID: mdl-11454228
ABSTRACT
The Arabidopsis thaliana sam1 gene encoding S-adenosylmethionine synthetase (EC 2.5.1.6) was transferred to flax (Linum usitatissimum) cells via Agrobacterium tumefaciens. This enzyme catalyses the conversion of methionine to S-adenosylmethionine (SAM), the major methyl group donor in living cells. The aim of this work was to study the consequences of an increased SAM-synthetase (SAM-S) activity in transgenic cell lines on both the production of mono- and dimethoxylated lignin monomers and the degree of methylesterification of pectins. Hypocotyls were cocultivated with Agrobacterium tumefaciens strain GV3101 (pGV2260) harbouring the pO35SSAM binary vector carrying the sam1 gene under the control of the 35S promoter and the nptII gene for selection of putative transformed cells. Most of the transgenic cell lines exhibited a significant (up to 3.2-fold) increase in SAM-S activity compared to the controls. The results showed that for the cell lines analysed this transformation had no effect on caffeic acid O-methyltransferase (COMT, EC 2.1.1.68) in vitro activity, degree of methoxylation of lignin precursors or lignin deposition, pectin methyltransferase (PMT, EC 2.1.1) in vitro activity, but led to an increase of pectin methylesterification in friable and fast-growing transgenic cell lines.
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Base de dados: MEDLINE Idioma: En Revista: Physiol Plant Ano de publicação: 2001 Tipo de documento: Article País de afiliação: França
Buscar no Google
Base de dados: MEDLINE Idioma: En Revista: Physiol Plant Ano de publicação: 2001 Tipo de documento: Article País de afiliação: França