scholarly journals Interaction of acetyl-CoA carboxylase enzyme inhibiting herbicides with auxin herbicides on ryegrass

2021 ◽  
Vol 51 (4) ◽  
Author(s):  
Rubens Antonio Polito ◽  
Larissa Pasqualotto ◽  
Rafael Dysarz ◽  
Rafaela Cinelli ◽  
Tamara Heck ◽  
...  
Keyword(s):  
Weed Control ◽  
Coenzyme A ◽  
Lolium Multiflorum ◽  
Antagonistic Effect ◽  
Acetyl Coa Carboxylase ◽  
Herbicide Application ◽  
Acetyl Coa ◽  
Antagonistic Interaction ◽  
Auxin Herbicides

ABSTRACT: This study aimed to evaluate the antagonistic effect of the mixture ofacetyl coenzyme-A carboxylase (ACCase) enzyme inhibiting herbicides and auxin herbicides in Lolium multiflorum and to determine mechanisms to mitigate this possible effect. The first experiments were conducted by associating the herbicide clethodim (108 g a.i. ha−1), quizalofop-p-ethyl (54 g a.i. ha−1), and clethodim + quizalofop-p-ethyl (108+54 g a.i. ha−1) with 2,4-D (1005 g a.e. ha−1) or triclopyr (720 g a.e. ha−1), in addition to the sole application of the respective graminicides. Another experiment included clethodim (54; 81; 108; 162; 216 g a.i. ha−1), quizalofop-p-ethyl (27; 40.5; 54; 81; 108 g a.i. ha−1), and clethodim + quizalofop-p-ethyl (54+27; 81+40.5; 108+54; 162+81; 216+108 g a.i. ha−1) mixed with 2,4-D (1005 g a.e. ha−1), or triclopyr (720 g a.e. ha−1), in addition to the control treatments without herbicide application. In the second experiment, herbicides clethodim (108 g a.i. ha−1), quizalofop-p-ethyl (54 g a.i. ha−1), and clethodim + quizalofop-p-ethyl (108+54 g a.i. ha−1) in combination with the herbicides 2,4-D (1005 g a.e. ha−1) or triclopyr (720 g a.e. ha−1)had malathion (1000 g a.i. ha−1) or glyphosate (720 g a.e. ha−1) mixed, in addition to the sole applications of the graminicides. The herbicide clethodim + quizalofop-p-ethyl did not present an antagonistic interaction with the auxin herbicides, and obtained 85% weed control. To obtain control similar to the sole application of this graminicide, the dose of the herbicide clethodim needs to be increased by 20%. However, the mixture of the herbicide quizalofop-p-ethyl with 2,4-D and triclopyr affects the ryegrass control. The use of strategies that increase the absorption of ACCase herbicides or the inhibition of P450 enzymes are ways to mitigate the antagonistic effect caused by the association of the two auxin herbicides.

Evaluation of weed control in acetyl coA carboxylase-resistant rice with mixtures of quizalofop and auxinic herbicides

2019 ◽  
Vol 34 (4) ◽  
pp. 498-505
Author(s):  
Tameka L. Sanders ◽  
Jason A. Bond ◽  
Benjamin H. Lawrence ◽  
Bobby R. Golden ◽  
Thomas W. Allen ◽  
...  
Keyword(s):  
Weed Control ◽  
Rice Yield ◽  
Field Studies ◽  
Growth Stages ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Herbicide Treatments ◽  
Herbicide Mixture ◽  
Sequential Treatments ◽  
And Control

AbstractRice with enhanced tolerance to herbicides that inhibit acetyl coA carboxylase (ACCase) allows POST application of quizalofop, an ACCase-inhibiting herbicide. Two concurrent field studies were conducted in 2017 and 2018 near Stoneville, MS, to evaluate control of grass (Grass Study) and broadleaf (Broadleaf Study) weeds with sequential applications of quizalofop alone and in mixtures with auxinic herbicides applied in the first or second application. Sequential treatments of quizalofop were applied at 119 g ai ha−1 alone and in mixtures with labeled rates of auxinic herbicides to rice at the two- to three-leaf (EPOST) or four-leaf to one-tiller (LPOST) growth stages. In the Grass Study, no differences in rice injury or control of volunteer rice (‘CL151’ and ‘Rex’) were detected 14 and 28 d after last application (DA-LPOST). Barnyardgrass control at 14 and 28 DA-LPOST with quizalofop applied alone or with auxinic herbicides EPOST was ≥93% for all auxinic herbicide treatments except penoxsulam plus triclopyr. Barnyardgrass control was ≥96% with quizalofop applied alone and with auxinic herbicides LPOST. In the Broadleaf Study, quizalofop plus florpyrauxifen-benzyl controlled more Palmer amaranth 14 DA-LPOST than other mixtures with auxinic herbicides, and control with this treatment was greater EPOST compared with LPOST. Hemp sesbania control 14 DA-LPOST was ≤90% with quizalofop plus quinclorac LPOST, orthosulfamuron plus quinclorac LPOST, and triclopyr EPOST or LPOST. All mixtures except quinclorac and orthosulfamuron plus quinclorac LPOST controlled ivyleaf morningglory ≥91% 14 DA-LPOST. Florpyrauxifen-benzyl or triclopyr were required for volunteer soybean control >63% 14 DA-LPOST. To optimize barnyardgrass control and rice yield, penoxsulam plus triclopyr and orthosulfamuron plus quinclorac should not be mixed with quizalofop. Quizalofop mixtures with auxinic herbicides are safe and effective for controlling barnyardgrass, volunteer rice, and broadleaf weeds in ACCase-resistant rice, and the choice of herbicide mixture could be adjusted based on weed spectrum in the treated field.

scholarly journals Genome Sequence of Serratia marcescens MSU97, a Plant-Associated Bacterium That Makes Multiple Antibiotics

2017 ◽  
Vol 5 (9) ◽  
Author(s):  
Miguel A. Matilla ◽  
Zulema Udaondo ◽  
Tino Krell ◽  
George P. C. Salmond
Keyword(s):  
Serratia Marcescens ◽  
Genome Sequence ◽  
Coenzyme A ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Content Type ◽  
Acetyl Coenzyme ◽  
Multiple Antibiotics

ABSTRACT Serratia marcescens MSU97 was isolated from the Guayana region of Venezuela due to its ability to suppress plant-pathogenic oomycetes. Here, we report the genome sequence of MSU97, which produces various antibiotics, including the bacterial acetyl-coenzyme A (acetyl-CoA) carboxylase inhibitor andrimid, the chlorinated macrolide oocydin A, and the red linear tripyrrole antibiotic prodigiosin.

scholarly journals Impact of a Novel W2027L Mutation and Non-Target Site Resistance on Acetyl-CoA Carboxylase-Inhibiting Herbicides in a French Lolium multiflorum Population

Genes ◽  
2021 ◽  
Vol 12 (11) ◽  
pp. 1838
Author(s):  
Shiv Shankhar Kaundun ◽  
Joe Downes ◽  
Lucy Victoria Jackson ◽  
Sarah-Jane Hutchings ◽  
Eddie Mcindoe
Keyword(s):  
Lolium Multiflorum ◽  
Restriction Enzymes ◽  
Target Site ◽  
Cereal Crops ◽  
Acetyl Coa Carboxylase ◽  
Wild Type ◽  
Resistance Mutations ◽  
Acetyl Coa ◽  
Pcr Product ◽  
Target Site Resistance

Herbicides that inhibit acetyl-CoA carboxylase (ACCase) are among the few remaining options for the post-emergence control of Lolium species in small grain cereal crops. Here, we determined the mechanism of resistance to ACCase herbicides in a Lolium multiflorum population (HGR) from France. A combined biological and molecular approach detected a novel W2027L ACCase mutation that affects aryloxyphenoxypropionate (FOP) but not cyclohexanedione (DIM) or phenylpyraxoline (DEN) subclasses of ACCase herbicides. Both the wild-type tryptophan and mutant leucine 2027-ACCase alleles could be positively detected in a single DNA-based-derived polymorphic amplified cleaved sequence (dPACS) assay that contained the targeted PCR product and a cocktail of two discriminating restriction enzymes. Additionally, we identified three well-characterised I1781L, I2041T, and D2078G ACCase target site resistance mutations as well as non-target site resistance in HGR. The non-target site component endowed high levels of resistance to FOP herbicides whilst partially impacting on the efficacy of pinoxaden and cycloxydim. This study adequately assessed the contribution of the W2027L mutation and non-target site mechanism in conferring resistance to ACCase herbicides in HGR. It also highlights the versatility and robustness of the dPACS method to simultaneously identify different resistance-causing alleles at a single ACCase codon.

Transcriptional regulation of acetyl coenzyme A carboxylase gene expression by tumor necrosis factor in 30A-5 preadipocytes

1989 ◽  
Vol 9 (3) ◽  
pp. 974-982
Author(s):  
M E Pape ◽  
K H Kim
Keyword(s):  
Tumor Necrosis Factor ◽  
Rna Polymerase ◽  
Tumor Necrosis ◽  
Transcriptional Control ◽  
Coenzyme A ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Mrna Accumulation ◽  
Acetyl Coenzyme A ◽  
Necrosis Factor

Acetyl coenzyme A (acetyl-CoA) carboxylase activity, amount, and mRNA levels increase during the differentiation of 30A-5 preadipocytes to adipocytes. Tumor necrosis factor (TNF) completely prevents this differentiation, with concomitant inhibition of acetyl-CoA carboxylase mRNA accumulation. To investigate the mechanisms by which TNF prevents acetyl-CoA carboxylase mRNA accumulation, we determined the effect of TNF on the transcription rate of the carboxylase gene and the half-life of carboxylase mRNA. Nuclear runoff transcription assays revealed no differences in the number of RNA polymerase molecules actively engaged in transcription of the acetyl-CoA carboxylase gene in preadipocytes, adipocytes, TNF-treated preadipocytes, or at any time during the course of differentiation. However, changes in adipsin, glycerophosphate dehydrogenase, and actin mRNAs, whose levels are also differentiation dependent, can be accounted for in part by changes in the number of polymerase complexes on their respective genes. To determine whether TNF caused a decrease in the stability of carboxylase RNA transcripts, we measured the rate of decay of prelabeled acetyl-CoA carboxylase mRNA. Control and TNF-treated cells showed no difference between the apparent half-lives of acetyl-CoA carboxylase mRNAs (9 h). However, the rate of acetyl-CoA carboxylase mRNA synthesis in vivo was decreased three- to fourfold in the presence of TNF. These data demonstrate that TNF prevents accumulation of acetyl-CoA carboxylase mRNA during preadipocyte differentiation by decreasing the rate of acetyl-CoA carboxylase gene transcription. However, transcriptional control is not due to a change in the number of RNA polymerase complexes actively engaged in carboxylase transcript elongation which could be measured by a number runoff assay. Instead, transcriptional control may be related to the rate at which RNA polymerase traverses the acetyl-CoA carboxylase gene.

scholarly journals Presence of Acetyl Coenzyme A (CoA) Carboxylase and Propionyl-CoA Carboxylase in Autotrophic Crenarchaeota and Indication for Operation of a 3-Hydroxypropionate Cycle in Autotrophic Carbon Fixation

1999 ◽  
Vol 181 (4) ◽  
pp. 1088-1098 ◽  
Author(s):  
Castor Menendez ◽  
Zsuzsa Bauer ◽  
Harald Huber ◽  
Nasser Gad’on ◽  
Karl-Otto Stetter ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Carbon Fixation ◽  
Coenzyme A ◽  
Autotrophic Growth ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Carboxylase Activity ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

ABSTRACT The pathway of autotrophic CO2 fixation was studied in the phototrophic bacterium Chloroflexus aurantiacus and in the aerobic thermoacidophilic archaeon Metallosphaera sedula. In both organisms, none of the key enzymes of the reductive pentose phosphate cycle, the reductive citric acid cycle, and the reductive acetyl coenzyme A (acetyl-CoA) pathway were detectable. However, cells contained the biotin-dependent acetyl-CoA carboxylase and propionyl-CoA carboxylase as well as phosphoenolpyruvate carboxylase. The specific enzyme activities of the carboxylases were high enough to explain the autotrophic growth rate via the 3-hydroxypropionate cycle. Extracts catalyzed the CO2-, MgATP-, and NADPH-dependent conversion of acetyl-CoA to 3-hydroxypropionate via malonyl-CoA and the conversion of this intermediate to succinate via propionyl-CoA. The labelled intermediates were detected in vitro with either 14CO2 or [14C]acetyl-CoA as precursor. These reactions are part of the 3-hydroxypropionate cycle, the autotrophic pathway proposed forC. aurantiacus. The investigation was extended to the autotrophic archaea Sulfolobus metallicus andAcidianus infernus, which showed acetyl-CoA and propionyl-CoA carboxylase activities in extracts of autotrophically grown cells. Acetyl-CoA carboxylase activity is unexpected in archaea since they do not contain fatty acids in their membranes. These aerobic archaea, as well as C. aurantiacus, were screened for biotin-containing proteins by the avidin-peroxidase test. They contained large amounts of a small biotin-carrying protein, which is most likely part of the acetyl-CoA and propionyl-CoA carboxylases. Other archaea reported to use one of the other known autotrophic pathways lacked such small biotin-containing proteins. These findings suggest that the aerobic autotrophic archaea M. sedula,S. metallicus, and A. infernus use a yet-to-be-defined 3-hydroxypropionate cycle for their autotrophic growth. Acetyl-CoA carboxylase and propionyl-CoA carboxylase are proposed to be the main CO2 fixation enzymes, and phosphoenolpyruvate carboxylase may have an anaplerotic function. The results also provide further support for the occurrence of the 3-hydroxypropionate cycle in C. aurantiacus.

scholarly journals Hormonal regulation of adipose-tissue acetyl-coenzyme A carboxylase by changes in the polymeric state of the enzyme. The role of long-chain fatty acyl-coenzyme A thioesters and citrate

1974 ◽  
Vol 142 (2) ◽  
pp. 365-377 ◽  
Author(s):  
Andrew P. Halestrap ◽  
Richard M. Denton
Keyword(s):  
Enzyme Activity ◽  
Coenzyme A ◽  
Total Activity ◽  
Fatty Acyl ◽  
Acetyl Coa Carboxylase ◽  
Initial Activity ◽  
Acetyl Coa ◽  
Coa Thioesters ◽  
Fat Pads

1. Acetyl-CoA carboxylase activity was measured in extracts of rat epididymal fat-pads either on preparation of the extracts (initial activity) or after incubation of the extracts with citrate (total activity). In the presence of glucose or fructose, brief exposure of pads to insulin increased the initial activity of acetyl-CoA carboxylase; no increase occurred in the absence of substrate. Adrenaline in the presence of glucose and insulin decreased the initial activity. None of these treatments led to a substantial change in the total activity of acetyl-CoA carboxylase. A large decrease in the initial activity of acetyl-CoA carboxylase also occurred with fat-pads obtained from rats that had been starved for 36h although the total activity was little changed by this treatment. 2. Conditions of high-speed centrifugation were found which appear to permit the separation of the polymeric and protomeric forms of the enzyme in fat-pad extracts. After the exposure of the fat-pads to insulin (in the presence of glucose), the proportion of the enzyme in the polymeric form was increased, whereas exposure to adrenaline (in the presence of glucose and insulin) led to a decrease in enzyme activity. 3. These changes are consistent with a role of citrate (as activator) or fatty acyl-CoA thioesters (as inhibitors) in the regulation of the enzyme by insulin and adrenaline; no evidence that the effects of these hormones involve phosphorylation or dephosphorylation of the enzyme could be found. 4. Changes in the whole tissue concentration of citrate and fatty acyl-CoA thioesters were compared with changes in the initial activity of acetyl-CoA carboxylase under a variety of conditions of incubation. No correlation between the citrate concentration and the initial enzyme activity was evident under any condition studied. Except in fat-pads which were exposed to insulin there was little inverse correlation between the concentration in the tissue of fatty acyl-CoA thioesters and the initial activity of acetyl-CoA carboxylase. 5. It is suggested that changes in the concentration of free fatty acyl-CoA thioesters (which may not be reflected in whole tissue concentrations of these metabolites) may be important in the regulation of the activity of acetyl-CoA carboxylase. The possibility is discussed that the concentration of free fatty acyl-CoA thioesters may be controlled by binding to a specific protein with properties similar to albumin.

scholarly journals Activation of immobilized acetyl-Coenzyme A carboxylase

1978 ◽  
Vol 169 (1) ◽  
pp. 255-256 ◽  
Author(s):  
A D Landman ◽  
J Lampert
Keyword(s):  
Coenzyme A ◽  
Enzymic Activity ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Sepharose 4B ◽  
Acetyl Coenzyme A Carboxylase ◽  
Covalently Bound

Partially purified acetyl-CoA carboxylase was covalently bound to a Sepharose 4B matrix. Although aggregation was thus prevented, the enzymic activity was stimulated by citrate and isocitrate.

scholarly journals A Novel W1999S Mutation and Non-Target Site Resistance Impact on Acetyl-CoA Carboxylase Inhibiting Herbicides to Varying Degrees in a UK Lolium multiflorum Population

PLoS ONE ◽  
2013 ◽  
Vol 8 (2) ◽  
pp. e58012 ◽  
Author(s):  
Shiv Shankhar Kaundun ◽  
Geraldine C. Bailly ◽  
Richard P. Dale ◽  
Sarah-Jane Hutchings ◽  
Eddie McIndoe
Keyword(s):  
Lolium Multiflorum ◽  
Target Site ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Target Site Resistance

scholarly journals Impact of a Novel W2027L Mutation And Non-Target Site Resistance On Acetyl-CoA Carboxylase Herbicides In a French Lolium Multiflorum Population

2021 ◽  
Author(s):  
Shiv Shankhar Kaundun ◽  
Joe Downes ◽  
Lucy Victoria Jackson ◽  
Sarah-Jane Hutchings ◽  
Eddie Mcindoe
Keyword(s):  
Lolium Multiflorum ◽  
Restriction Enzymes ◽  
Target Site ◽  
Cereal Crops ◽  
Acetyl Coa Carboxylase ◽  
Wild Type ◽  
Resistance Mutations ◽  
Acetyl Coa ◽  
Pcr Product ◽  
Target Site Resistance

Abstract Herbicides that inhibit acetyl-CoA carboxylase (ACCase) are among the few remaining options for the post-emergence control of Lolium species in small grain cereal crops. Here we have determined the mechanism of resistance to ACCase herbicides in a Lolium multiflorum population (HGR) from France. A combined biological and molecular approach detected a novel W2027L ACCase mutation that affects aryloxyphenoxypropionate (FOP) but not cyclohexanedione (DIM) or phenylpyraxoline (DEN) subclasses of ACCase herbicides. Both the wild type tryptophan and mutant leucine 2027-ACCase alleles could be positively detected in a single DNA-based derived Polymorphic amplified cleaved sequence (dPACS) assay that contained the targeted PCR product and a cocktail of two discriminating restriction enzymes. Additionally, we have identified three well-characterised I1781L, I2041T and D2078G target site resistance mutations as well as non-target site resistance in HGR. The non-target site component endowed high levels of resistance to FOP herbicides whilst partially impacting on the efficacy of pinoxaden and cycloxydim. This study adequately assessed the contribution of the W2027L mutation and non-target site mechanism in conferring resistance to ACCase herbicides in HGR. It also highlights the versatility and robustness of the dPACS method to simultaneously identify different resistance-causing alleles at a single ACCase codon.

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