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芳氧苯氧丙酸类(aryloxyphenoxypropionates,APPs)除草剂是一类广泛使用的乙酰辅酶A羧化酶抑制剂,可高效专一抑制禾本科杂草的乙酰辅酶A羧化酶(acetyl-coenzyme A carboxylase,ACCase)。目前已出现大量抗芳氧苯氧丙酸类除草剂的禾本科杂草,其抗性大多由叶绿体乙酰辅酶A羧化酶的羧基转移酶(carboxyltransferase,CT)功能域中的氨基酸突变引起。在所有已发现的氨基酸突变中,最引人关注的是第1 781位(对应大穗看麦娘Alopecurus myosuroides质体ACCase的氨基酸残基位置)异亮氨酸到亮氨酸的单点突变,该特定位置形成亮氨酸会导致某些杂草对APPs类除草剂产生抗性。综述了乙酰辅酶A羧化酶CT功能域的研究进展及杂草对APPs类除草剂的抗性分子机理,探讨了杂草对APPs类除草剂抗性分子机理研究中存在的问题,以期为进一步深入研究APPs类除草剂的抗性机制提供参考。
Aryloxyphenoxypropionates (APPs) herbicides are a widely used class of acetyl CoA carboxylase inhibitors that efficiently and specifically inhibit acetylcholinesterase A from grass weeds carboxylase, ACCase). At present, a large number of grass weeds resistant to aryloxyphenyphenoic acid herbicides have emerged, most of which are caused by amino acid mutations in the carboxyltransferase (CT) domain of chloroplast acetyl-CoA carboxylase. Of all the amino acid mutations that have been found, the most notable one is the single point mutation of isoleucine to leucine at position 1 781 (corresponding to the amino acid residue position of ACCase of Alopecurus myosuroides plastid) The formation of leucine at this specific site can cause certain weeds to become resistant to APPs herbicides. The research progress of the CT domain of acetyl-CoA carboxylase and the molecular mechanism of weed resistance to APPs herbicides were reviewed. The existing problems in the molecular mechanism of weed resistance to APPs herbicide were discussed. In-depth study of APPs herbicide resistance mechanisms provide a reference.