Abstract
Summary Wheat ( Triticum aestivum L. var. Chinese Spring) cell suspension cultures resistant to growth inhibition by a lysine analog S-(2-aminoethyl)-L-cysteine (AEC) were selected by a stepwise selection method. Resistance was stable even when the selected cells were cultured in the absence of AEC for 12 months. Wild-type and AEC-resistant cell lines contained comparable amounts of free lysine and other aspartate family amino acids throughout the 30-day culture period. The activities of two key enzymes in lysine biosynthesis, aspartate kinase and dihydrodipicolinate synthase, were similar in both cell lines. Aspartate kinase from AEC-resistant cells was slightly less sensitive to inhibition by lysine or AEC than the kinase from wild-type cells; whereas, dihydrodipicolinate synthases from both cell lines were inhibited equally by lysine or AEC. Uptake of 14 C-lysine from the transport medium was greatly reduced in the AEC-resistant cells. Apparently the reduced uptake of AEC is the main mechanism by which resistance to AEC is conferred in our resistant cells.
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