Mutations in the acetolactate synthase genes of sulfonylurea-resistant biotypes of Lindernia spp.
Mutations in the acetolactate synthase genes of sulfonylurea-resistant biotypes of Lindernia spp.
复制标题
林德尼亚属磺酰脲类抗性生物型的乙酰乳酸合酶基因突变。
DOI:
10.1046/j.1445-6664.2001.00054.x
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发表时间:
2002
影响因子:
1.4
通讯作者:
Hiroaki Watanabe
中科院分区:
文献类型:
--
作者:
A. Uchino;Hiroaki Watanabe
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 Lindernia plants, L. dubia var. dubia, L. dubia var. major, L. micrantha and L. procumbens, for which biotypes resistant to sulfonylureas have been found in paddy fields. The clones were classified into two groups in each Lindernia plant: Als1 and Als2. 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 Als1 and Als2. Comparison of Als1 between resistant and susceptible biotypes showed that the proline of Domain A was replaced by alanine, serine or glutamine in all resistant biotypes of Lindernia plants, while it was conserved in all susceptible biotypes. This amino acid substitution in ALS encoded by Als1 is involved in the resistant mechanism of ALS to sulfonylurea in the four Lindernia plants.