Mutations in the acetolactate synthase genes of sulfonylurea‐resistant biotypes of <i>Lindernia</i> spp.

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<jats:p>Acetolactate synthase (ALS) is a key enzyme in the biosynthetic pathway of branched‐chain amino acids. A mutation of the ALS gene causing amino acid substitution at the position of proline in Domain A makes ALS less sensitive to sulfonylureas, which are ALS‐inhibiting herbicides. We cloned partial ALS genes from four <jats:italic>Lindernia</jats:italic> plants, <jats:italic>L</jats:italic>. <jats:italic>dubia</jats:italic> var. <jats:italic>dubia</jats:italic>, <jats:italic>L</jats:italic>. <jats:italic>dubia</jats:italic> var. <jats:italic>major</jats:italic>, <jats:italic>L</jats:italic>. <jats:italic>micrantha</jats:italic> and <jats:italic>L</jats:italic>. <jats:italic>procumbens</jats:italic>, for which biotypes resistant to sulfonylureas have been found in paddy fields. The clones were classified into two groups in each <jats:italic>Lindernia</jats:italic> plant: <jats:italic>Als1</jats:italic> and <jats:italic>Als2</jats:italic>. Sequencing of the clones and alignment of deduced amino acid sequences with previously reported ALS of other species suggested that the cloned region contains an intron in both <jats:italic>Als1</jats:italic> and <jats:italic>Als2</jats:italic>. Comparison of <jats:italic>Als1</jats:italic> between resistant and susceptible biotypes showed that the proline of Domain A was replaced by alanine, serine or glutamine in all resistant biotypes of <jats:italic>Lindernia</jats:italic> plants, while it was conserved in all susceptible biotypes. This amino acid substitution in ALS encoded by <jats:italic>Als1</jats:italic> is involved in the resistant mechanism of ALS to sulfonylurea in the four <jats:italic>Lindernia</jats:italic> plants.</jats:p>

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