First published online May 21, 2004; 10.1104/pp.104.039347
Plant Physiology 135:828-839 (2004)
© 2004 American Society of Plant Biologists
BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES
Glucosinolate and Amino Acid Biosynthesis in Arabidopsis1
Ben Field,
Guillermo Cardon,
Maria Traka,
Johan Botterman,
Guy Vancanneyt and
Richard Mithen*
Department of Metabolic Biology, John Innes Centre, Norwich NR4 7UH (B.F.); BayerCrop Science N.V., B–9000 Gent, Belgium (G.C., J.B., G.V.); and Nutrition Division, Institute of Food Research, Norwich NR4 7UA, United Kingdom (M.T., R.M.)
Enzymes that catalyze the condensation of acetyl coenzyme A and 2-oxo acids are likely to be important in two distinct metabolic pathways in Arabidopsis. These are the synthesis of isopropylmalate, an intermediate of Leu biosynthesis in primary metabolism, and the synthesis of methylthioalkylmalates, intermediates of Met elongation in the synthesis of aliphatic glucosinolates (GSLs), in secondary metabolism. Four Arabidopsis genes in the ecotype Columbia potentially encode proteins that could catalyze these reactions. MAM1 and MAML are adjacent genes on chromosome 5 at the Gsl-elong locus, while MAML-3 and MAML-4 are at opposite ends of chr 1. The isopropylmalate synthase activity of each member of the MAM-like gene family was investigated by heterologous expression in an isopropylmalate synthase-null Escherichia coli mutant. Only the expression of MAML-3 restored the ability of the mutant to grow in the absence of Leu. A MAML knockout line (KO) lacked long-chain aliphatic GSLs, which were restored when the KO was transformed with a functional MAML gene. Variation in expression of MAML did not alter the total levels of Met-derived GSLs, but just the ratio of chain lengths. MAML overexpression in Columbia led to an increase in long-chain GSLs, and an increase in 3C GSLs. Moreover, plants overexpressing MAML contained at least two novel amino acids. One of these was positively identified via MS/MS as homo-Leu, while the other, with identical mass and fragmentation patterns, was likely to be homo-Ile. A MAML-4 KO did not exhibit any changes in GSL profile, but had perturbed soluble amino acid content.
1 This work was supported by the John Innes Foundation (BF), by the BBSRC, and by UK Bayer Crop Science.
Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.039347.
* Corresponding author; e-mail richard.mithen{at}bbsrc.ac.uk; fax 44–1603–507–723.
Received January 20, 2004;
returned for revision March 1, 2004;
accepted March 1, 2004.
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