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质体乙酰辅酶A羧化酶羧基转移酶结构域中的单一位点突变赋予了对禾本科特异性除草剂的抗性。

Single-site mutations in the carboxyltransferase domain of plastid acetyl-CoA carboxylase confer resistance to grass-specific herbicides.

作者信息

Liu Wenjie, Harrison Dion K, Chalupska Dominika, Gornicki Piotr, O'donnell Chris C, Adkins Steve W, Haselkorn Robert, Williams Richard R

机构信息

Agricultural Molecular Biotechnology Laboratory, School of Agronomy and Horticulture, University of Queensland, Gatton 4343, Queensland, Australia.

出版信息

Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3627-32. doi: 10.1073/pnas.0611572104. Epub 2007 Feb 20.

DOI:10.1073/pnas.0611572104
PMID:17360693
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1802000/
Abstract

Grass weed populations resistant to aryloxyphenoxypropionate (APP) and cyclohexanedione herbicides that inhibit acetyl-CoA carboxylase (ACCase; EC 6.4.1.2) represent a major problem for sustainable agriculture. We investigated the molecular basis of resistance to ACCase-inhibiting herbicides for nine wild oat (Avena sterilis ssp. ludoviciana Durieu) populations from the northern grain-growing region of Australia. Five amino acid substitutions in plastid ACCase were correlated with herbicide resistance: Ile-1,781-Leu, Trp-1,999-Cys, Trp-2,027-Cys, Ile-2,041-Asn, and Asp-2,078-Gly (numbered according to the Alopecurus myosuroides plastid ACCase). An allele-specific PCR test was designed to determine the prevalence of these five mutations in wild oat populations suspected of harboring ACCase-related resistance with the result that, in most but not all cases, plant resistance was correlated with one (and only one) of the five mutations. We then showed, using a yeast gene-replacement system, that these single-site mutations also confer herbicide resistance to wheat plastid ACCase: Ile-1,781-Leu and Asp-2,078-Gly confer resistance to APPs and cyclohexanediones, Trp-2,027-Cys and Ile-2,041-Asn confer resistance to APPs, and Trp-1,999-Cys confers resistance only to fenoxaprop. These mutations are very likely to confer resistance to any grass weed species under selection imposed by the extensive agricultural use of the herbicides.

摘要

对抑制乙酰辅酶A羧化酶(ACCase;EC 6.4.1.2)的芳氧苯氧丙酸酯(APP)和环己二酮类除草剂产生抗性的禾本科杂草种群,是可持续农业面临的一个主要问题。我们研究了来自澳大利亚北部谷物种植区的9个野燕麦(Avena sterilis ssp. ludoviciana Durieu)种群对ACCase抑制性除草剂的抗性分子基础。质体ACCase中的5个氨基酸替换与除草剂抗性相关:Ile-1,781-Leu、Trp-1,999-Cys、Trp-2,027-Cys、Ile-2,041-Asn和Asp-2,078-Gly(根据黑麦草质体ACCase编号)。设计了一种等位基因特异性PCR检测方法,以确定这些5种突变在疑似具有ACCase相关抗性的野燕麦种群中的流行情况,结果是,在大多数但并非所有情况下,植物抗性与这5种突变中的一种(且仅一种)相关。然后,我们使用酵母基因替换系统表明,这些单点突变也赋予了小麦质体ACCase除草剂抗性:Ile-1,781-Leu和Asp-2,078-Gly赋予对APPs和环己二酮类除草剂的抗性,Trp-2,027-Cys和Ile-2,041-Asn赋予对APPs的抗性,而Trp-1,999-Cys仅赋予对精恶唑禾草灵的抗性。在除草剂广泛农业使用所施加的选择压力下,这些突变很可能赋予任何禾本科杂草物种抗性。

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The molecular bases for resistance to acetyl co-enzyme A carboxylase (ACCase) inhibiting herbicides in two target-based resistant biotypes of annual ryegrass (Lolium rigidum).一年生黑麦草(多花黑麦草)两种基于靶点的抗性生物型对乙酰辅酶A羧化酶(ACCase)抑制性除草剂抗性的分子基础。
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Molecular bases for sensitivity to acetyl-coenzyme A carboxylase inhibitors in black-grass.黑麦草对乙酰辅酶A羧化酶抑制剂敏感性的分子基础
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Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop.稀禾啶和二氯喹啉酸对乙酰辅酶A羧化酶羧基转移酶结构域抑制作用的分子基础
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An isoleucine residue within the carboxyl-transferase domain of multidomain acetyl-coenzyme A carboxylase is a major determinant of sensitivity to aryloxyphenoxypropionate but not to cyclohexanedione inhibitors.多结构域乙酰辅酶A羧化酶的羧基转移酶结构域内的异亮氨酸残基是对芳氧基苯氧基丙酸酯敏感性的主要决定因素,但对环己二酮抑制剂不敏感。
Plant Physiol. 2003 Jul;132(3):1716-23. doi: 10.1104/pp.103.021139.
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Expression of cytosolic and plastid acetyl-coenzyme A carboxylase genes in young wheat plants.小麦幼苗中胞质和质体乙酰辅酶A羧化酶基因的表达
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PCR-based detection of resistance to acetyl-CoA carboxylase-inhibiting herbicides in black-grass (Alopecurus myosuroides Huds) and ryegrass (Lolium rigidum gaud).基于聚合酶链式反应检测黑麦草(Alopecurus myosuroides Huds)和硬直黑麦草(Lolium rigidum gaud)对乙酰辅酶A羧化酶抑制型除草剂的抗性
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