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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
Author(s) -
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
Publication year - 2001
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.2001.1120211.x
Subject(s) - linum , lignin , biochemistry , agrobacterium tumefaciens , methylation , arabidopsis thaliana , agrobacterium , transformation (genetics) , genetically modified crops , cell wall , chemistry , cell culture , biology , microbiology and biotechnology , gene , transgene , mutant , botany , genetics
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.