Allelic mutations in acetyl-coenzyme A carboxylase confer herbicide tolerance in maize

Marshall, Lorelei C.; Somers, David A.; Dotray, P. D.; Gengenbach, B. G.; Wyse, Donald L.; Gronwald, John W.

doi:10.1007/bf00226531

Cited by 40 publications

(22 citation statements)

References 15 publications

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“…These isozymes have significant difference in herbicide resistance (18). The studies of ACCase mutants with different sensitivities to herbicides suggested the presence of three, and possibly five, alleles of maize ACCase structural genes (29). These findings show that the isozymes of the eukaryote form are in different cell compartments in Proc.…”

Section: Resultsmentioning

confidence: 77%

Compartmentalization of two forms of acetyl-CoA carboxylase in plants and the origin of their tolerance toward herbicides.

Konishi

Sasaki

1994

Proc. Natl. Acad. Sci. U.S.A.

227

175

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Acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) catalyzes the synthesis of malonyl-CoA, the first intermediate in fatty acid synthesis. We studied the llization of two forms, the prokaryote and the eukaryote forms, of ACCase in pea leaves by comparing the blotin polypeptides of the two ACCases in protein extract from leaves and plastids.We found that the two forms of ACCase were in diferent cell compartments of pea leaves; the prokaryote form was in the plastids, and the eukaryote form was elsewhere, probably in the cytosol. This result suested the existence of two sites of malonyl-CoA thes. The Gramineae, such as rice and wheat, which lack the accD gene encoding one of the subunits ofthe prokaryote form ofACCase in their chloroplast genomes, did not have the prokaryote form of the enzyme but had the eukaryote form. The selectlve grass herbicides of the diphenoxyproponic acid type and the cyclohexanedione type, in vitro, inhibited plastidic ACCase of the eukaryote form from wheat but did not inhibit that of the prokaryote form from pea, suggeting that the origin of the tolerance of intact pea plant toward these herbicides is partly in the insensitivity of the prokaryote form of the enzyme. The origin of the susceptibility of the Gramineae plants toward these herbicides seems to lie in the presence of the herbicide-sensitive eukaryote form and the absence ofthe insenitive prokaryote form due to the lack of the accD gene in plastid.Acetyl-CoA carboxylase (ACCase; EC 6.4.1.2) catalyzes the ATP-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The reaction is the first committed step in the synthesis of fatty acid, providing the essential substrate for fatty acid synthesis. There are two forms of ACCase: a prokaryote form consisting of three protein components biotin carboxylase, carboxyltransferase, and biotin carboxylase carrier protein (1)-and a eukaryote form consisting of three functional domains on a single polypeptide (2-7). It has been believed that, in plants, plastids are the major site of fatty acid synthesis (8) and that only the eukaryote form ofthe enzyme in plastids participates in the synthesis (9, 10). Early studies reported the existence of the prokaryote form in the spinach chloroplast (11), but this finding has been dismissed because the prokaryote form has not yet been purified and the purified ACCases from various plants are all eukaryote form consisting of a subunit size of -200 kDa (5-7), like that of the mammal enzyme (2). ACCase gene encoding the 230-kDa polypeptide has been isolated from a photosynthetic eukaryote alga (12). This large polypeptide is probably nuclearencoded because this sequence is not found in the complete sequence ofchloroplast genomes (13-15). However, recently we have obtained evidence ofthe existence of the prokaryote form in pea chloroplasts by identifying one of the subunits of carboxyltransferase, the chloroplast-encoded accD protein (16). This finding supports the early studies and indicates the existence of two forms of ACCase in pea plants (16,17). ...

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Section: Resultsmentioning

confidence: 77%

Compartmentalization of two forms of acetyl-CoA carboxylase in plants and the origin of their tolerance toward herbicides.

Konishi

Sasaki

1994

Proc. Natl. Acad. Sci. U.S.A.

227

175

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“…Similar relationships between whole-plant responses and enzyme activity have been reported for resistant and susceptible Festuca spp. (Stoltenberg et al, 1989) and resistant corn lines derived from tissue culture (Parker et al, 1990;Marshall et al, 1992). This provides strong evidence in support of a single site of action at the enzyme level.…”

Section: Membrane Response and Herbicide Phytotoxicitymentioning

confidence: 63%

Membrane Response to Diclofop Acid Is pH Dependent and Is Regulated by the Protonated Form of the Herbicide in Roots of Pea and Resistant and Susceptible Rigid Ryegrass

DiTomaso

1993

Plant Physiol.

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Electrophysiological studies in roots of pea (Pisum sativum 1.) and rigid ryegrass (Lolium rigidum Caud.) seedlings were conducted to elucidate the mechanism involved in the membrane response to the herbicide diclofop. In pea, a dicotyledonous plant insensitive to diclofop, membrane depolarization at varying pH values and herbicide concentrations increased at higher concentrations of the protonated form of diclofop acid (pK, 3.57). In unbuffered nutrient solution (pH 5.71, diclofop acid (50 PM) depolarized the membrane potential (E,) in roots of both resistant and susceptible biotypes of rigid ryegrass, whereas recovery of E, occurred only in the resistant biotype following removal of the herbicide. This differential response was correlated with an increase (450%) in the rate of acidification of the externa1 solution by the susceptible biotype, and the E , differences between biotypes were eliminated in solutions buffered at pH 5.0 or 6.0. In addition, p-chloromercuribenzene-sulfonic acid did not prevent the depolarization of E , by 50 PM diclofop acid. It is concluded that the differential membrane response to diclofop acid in herbicide-resistant and -susceptible biotypes of rigid ryegrass is due to pH differences at the cell wall/plasmalemma interface. Although the membrane response is probably not involved in the primary inhibitory effect of diclofop on plant growth, it could reduce the concentration of the permeant protonated form of the herbicide and possibly could contribute to increased tolerance to diclofop and other weak acid herbicides.

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“…In a biotype of Italian rygrass (Lolium multiflorum) that was selected with an AOPP herbicide, the ACCase is resistant to AOPP but not CHD herbicides (Gronwald 1991). Maize cell cultures that were selected with sethoxydim or haloxyfop developed resistance as a consequence of mutations of the gene coding for ACCase (Marshall et al 1992), with modified forms of the enzyme encoded by different allelic mutations at the same locus. These data, together with the L. rigidum data herein, show that several modifications of ACCase, endowing resistance to CHD andor AOPP herbicides, are possible and that the pattern of cross-resistance is determined by the type of mutation.…”

Section: Inhibition Of Accase By Herbicides the Activity Ofmentioning

confidence: 99%

Occurrence of a herbicide-resistant acetyl-coenzyme A carboxylase mutant in annual ryegrass (Lolium rigidum) selected by sethoxydim

Tardif

Hokum

Powles

1993

Planta

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Abstract. The spectrum of herbicide resistance was determined in an annual ryegrass (Lolium rigidum Gaud.) biotype (SLR 3) that had been exposed to the grass herbicide sethoxydim, an inhibitor of the plastidic enzyme acetylcoenzyme A carboxylase (ACCase, EC 6.4.1.2), for three consecutive years. This biotype has an 18-fold resistance to sethoxydim and enhanced resistance to other cyclohexanedione herbicides compared with a susceptible biotype (VLR 1). The resistant biotype also has a 47-to > 300-fold cross-resistance to the aryloxyphenoxypropanoate herbicides which share ACCase as a target site. No resistance is evident to herbicide with a target site different from ACCase. The absorption of [4-14C]sethoxydim, the rate of metabolic degradation and the nature of the herbicide metabolites are similar in the resistant and susceptible biotypes. While the total activity of the herbicide target enzyme ACCase is similar in extracts from the two biotypes, the kinetics of herbicide inhibition differ. The concentrations of sethoxydim and tralkoxydim required to inhibit the activity of ACCase by 50% are 7.8 and > 9.5 times higher, respectively, in the resistant biotype. The activity of ACCase from the resistant biotype was also less sensitive to aryloxyphenoxypropanode herbicides than the susceptible biotype. The spectrum of resistance at the whole-plant level is correlated with resistance at the ACCase level and confirms that a less sensitive form of the target enzyme endows resistance in biotype SLR 3.

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Allelic mutations in acetyl-coenzyme A carboxylase confer herbicide tolerance in maize

Cited by 40 publications

References 15 publications

Compartmentalization of two forms of acetyl-CoA carboxylase in plants and the origin of their tolerance toward herbicides.

Compartmentalization of two forms of acetyl-CoA carboxylase in plants and the origin of their tolerance toward herbicides.

Membrane Response to Diclofop Acid Is pH Dependent and Is Regulated by the Protonated Form of the Herbicide in Roots of Pea and Resistant and Susceptible Rigid Ryegrass

Occurrence of a herbicide-resistant acetyl-coenzyme A carboxylase mutant in annual ryegrass (Lolium rigidum) selected by sethoxydim

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