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- W1982449314 abstract "After mutagenesis, M2 seedlings of Arabidopsis thaliana were grown on a selective medium containing toxic concentrations of lysine and threonine. One of the LT-resistant mutants (RLT 40) was studied at the biochemical and genetical levels. A six-fold increase in free threonine content was found in 8-day-old mutant plantlets compared with the wild type. The total amino acid content of the mutant was also remarkably increased, essentially due to increased levels of aspartate, threonine, methionine, isoleucine and lysine. As one of the possible reasons for the LT-resistance resides in a change of the regulatory properties of the first enzyme of the aspartate pathway, aspartate kinase (EC 2.7.2.4), the feedback-inhibition pattern of aspartate kinase was examined in the mutant and the wild type. In Arabidopsis, after ion-exchange chromatography of whole plant extracts, three peaks of activity were detected corresponding respectively to a threonine-sensitive isoform, to a lysine-sensitive form and a form insensitive to both inhibitors. The threonine accumulation in RLT 40 could be related to a partial insensitivity of the lysinesensitive form of aspartate kinase. Genetical analysis showed that the resistance gene behaved as a dominant, monogenic nuclear trait. Linkage analysis, performed with a multiple marker line, indicated that the mutation is located on chromosome 2, 36.0 cM from the er locus and 19.8 cM from the py locus on chromosome 2. This partially lysine-insensitive mutant of aspartate kinase offers ways to a map-based approach for cloning the gene coding for the corresponding isoform in plants." @default.
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- W1982449314 date "1995-06-01" @default.
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- W1982449314 title "Threonine Accumulation in a Mutant of Arabidopsis thaliana (L.) Heynh. with an Altered Aspartate Kinase" @default.
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- W1982449314 doi "https://doi.org/10.1016/s0176-1617(11)82049-3" @default.
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