Structural and Biochemical Characterization of Dinitroaniline-Resistant <i>Eleusine</i>

Vaughan, Keith; Vaughan, Martin A.

doi:10.1021/bk-1990-0421.ch025

Cited by 30 publications

(15 citation statements)

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“…Microtubules may be formed in vitro using the isolated tubulin protein. Tubulin from the susceptible biotypes could form microtubules, but the process was disrupted by oryzalin 38. However, tubulin protein from the resistant biotype formed microtubules even in the presence of oryzalin, indicating an intrinsic difference in the tubulin protein that allowed it to polymerize even in the presence of the dinitroaniline herbicides 38.…”

Section: Dinitroaniline Herbicide Resistancementioning

confidence: 99%

“…Tubulin from the susceptible biotypes could form microtubules, but the process was disrupted by oryzalin 38. However, tubulin protein from the resistant biotype formed microtubules even in the presence of oryzalin, indicating an intrinsic difference in the tubulin protein that allowed it to polymerize even in the presence of the dinitroaniline herbicides 38. Molecular characterization of the tubulin genes in goosegrass revealed that a single amino acid change conferred resistance 39…”

Section: Dinitroaniline Herbicide Resistancementioning

confidence: 99%

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Herbicide resistance work in the United States Department of Agriculture—Agricultural Research Service

Vaughn¹

2003

Pest Management Science

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Herbicide-resistant weed biotypes are an increasing problem in agriculture, with reports of resistance to almost every herbicide class at some place in the world, and the total number of resistant biotypes at over 250. Agricultural Research Service (ARS) scientists have been key players in this area since the first substantiated occurrence of these resistant biotypes in the 1970s. The most significant of their contributions is the complete unraveling of the mechanism of triazine resistance by Arntzen and colleagues, then with ARS at the University of Illinois. These studies established a high benchmark for research in this area and are a model for all studies in this area. Other ARS scientists have investigated a large number of weed biotypes with resistance to a wide range of herbicide classes and mechanisms of resistance. Collectively, these studies have been used to generate herbicide resistance-management schemes for growers, based upon the herbicide site and the potential for resistance development.

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Section: Dinitroaniline Herbicide Resistancementioning

confidence: 99%

Section: Dinitroaniline Herbicide Resistancementioning

confidence: 99%

Herbicide resistance work in the United States Department of Agriculture—Agricultural Research Service

Vaughn¹

2003

Pest Management Science

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“…The resistant goosegrass biotype was shown to be sensitive to the microtubule-depolymerizing drug colchicine and supersensitive to other classes of microtubule disrupters, e.g. griseofulvin (Vaughn et al, 1987), and to the microtubule-stabilizing drug Taxol (Vaughn and Vaughn, 1990). These data show similarities to the observations made on the phenotypes of three tubulin mutants in Chlamydomonas reinhardtii isolated on the basis of resistance to colchicine (Bolduc et al, 1988;Lee and Huang, 1990;Schibler and Huang, 1991) or to the phosphorothioamidate herbicide amiprophosmethyl (James et al, 1993).…”

mentioning

confidence: 99%

“…Vol. 105,1994 likely in the resistant goosegrass biotype, is the result of an increased stability of microtubules in the cells compared to wild type rather than an alteration in a specific drug-binding site, detoxification of the drugs, or defective drug uptake (Vaughn and Vaughn, 1990;Schibler and Huang, 1991;James et al, 1993).…”

mentioning

confidence: 99%

Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor Site(s)

Ellis¹,

Taylor²,

Hussey³

1994

Plant Physiol.

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Dinitroaniline and phosphorothioamidate herbicides disrupt microtubule assembly from tubulin protein dimers and thereby halt microtubule-based processes such as mitosis in plant cells. Despite the contrasting chemical properties of dinitroaniline and phosphorothioamidate herbicides, a three-dimensional molecular analysis revealed remarkable electrostatic similarity between these two classes of herbicide. From these data it is proposed that dinitroaniline and phosphorothioamidate herbicides share common binding site(s) in the plant cell.

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“…Tubulin is composed of an at and a subunit. The a subunit is different in the herbicide-resistant goosegrass biotype (25). Nothing is known of the nature of the binding site of these herbicides on tubulin, and little has been published on the structure-activity relationships of herbicides that act at this site.…”

Section: Cell Divisionmentioning

confidence: 99%

Overview of Herbicide Mechanisms of Action

Duke¹

1990

Environmental Health Perspectives

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Commercial herbicides exhibit many different mechanisms of action. Several enzymes involved in biosynthesis of amino acids are sites of action for herbicides. A large number of different herbicide classes inhibit photosynthesis by binding to the quinone-binding protein, D-1, to prevent photosynthetic electron transfer. Several different types of herbicides apparently cause accumulation of photodynamic porphyrins by inhibiting protoporphyrinogen oxidase. Bipyridyliums and heteropentalenes cause the production of superoxide radicals by energy diversion from photosystem I of photosynthesis. Lipid synthesis is the site of action of a broad array of herbicides used in controlling monocot weeds. Herbicides of several classes apparently act by inhibiting mitosis through direct interaction with tubulin. Several other molecular sites of herbicide action are known. Despite a growing body of knowledge, the exact molecular sites of action of many herbicides are unknown. Some herbicides are known to have more than one site of action. Virtually all knowledge of herbicide structure-activity relationships is semiempirical. In addition to site of action structure-activity relationships, herbicide structure and chemical properties also strongly influence absorption, translocation, bioactivation, and environmental stability. Considering how little is known about all the potential sites of herbicide action, it is unlikely that during the next decade more than a relatively small number of site-specific herbicide structure-activity relationships will be developed.

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Structural and Biochemical Characterization of Dinitroaniline-Resistant Eleusine

Cited by 30 publications

References 0 publications

Herbicide resistance work in the United States Department of Agriculture—Agricultural Research Service

Herbicide resistance work in the United States Department of Agriculture—Agricultural Research Service

Molecular Modeling Indicates that Two Chemically Distinct Classes of Anti-Mitotic Herbicide Bind to the Same Receptor Site(s)

Overview of Herbicide Mechanisms of Action

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