scholarly journals The problem of plants resistance to herbicides – inhibitors of acetolactate synthase

2019 ◽  
Vol 24 ◽  
pp. 296-301
Author(s):  
Zh. Z. Guralchuk ◽  
Ye. Yu. Morderer
Keyword(s):  
Amino Acid ◽  
Flavin Adenine Dinucleotide ◽  
Acetolactate Synthase ◽  
Structural Features ◽  
Genetic Mutations ◽  
Thiamine Diphosphate ◽  
Mechanisms Of Resistance ◽  
Resistance To Herbicides ◽  
Als Inhibitors ◽  
Emergence Of Resistance

Aim. The purpose of the work is to analyze the available literature data associated with the emergence of resistance to herbicides ALS inhibitors. Results. Target resistance to herbicides ALS inhibitors is a consequence of genetic mutations due to the replacement of one amino acid with another in the enzyme polypeptide. The article deals with data on the action of herbicides ALS inhibitors on the functioning of the enzyme and its modification in the presence of mutations that predispose the resistance to herbicides ALS inhibitors. Brief description of the structural features of the binding of various classes of herbicides inhibitors ALS with the target enzyme and the modification of the cofactors (thiamine diphosphate and flavin adenine dinucleotide) is presented. Conclusions. Studies of recent decades have led to an increase in knowledge about the action characteristics of herbicides belonging to different classes of ALS inhibitors and the causes of resistance. The obtained results are the basis for better understanding of the mechanisms of resistance to herbicides and the development of ways to overcome them. Keywords: herbicides, acetolactate synthase, resistance, gene mutation.

The Evidence for Reduced Glyphosate Efficacy on Acetolactate Synthase–Inhibiting Herbicide-Resistant Yellow Nutsedge (Cyperus esculentus)

Weed Science ◽  
2016 ◽  
Vol 64 (3) ◽  
pp. 389-398
Author(s):  
Parsa Tehranchian ◽  
Jason K. Norsworthy ◽  
Matheus Palhano ◽  
Nicholas E. Korres ◽  
Scott McElroy ◽  
...  
Keyword(s):  
Amino Acid ◽  
Production Systems ◽  
Acetolactate Synthase ◽  
Dry Weight ◽  
Cross Resistance ◽  
Purple Nutsedge ◽  
Yellow Nutsedge ◽  
Epsps Gene ◽  
Treated Leaf ◽  
Als Inhibitors

A yellow nutsedge biotype (Res) from an Arkansas rice field has evolved resistance to acetolactate synthase (ALS)-inhibiting herbicides. TheResbiotype previously exhibited cross-resistance to ALS inhibitors from four chemical families (imidazolinone, pyrimidinyl benzoate, sulfonylurea, and triazolopyrimidine). Experiments were conducted to evaluate alternative herbicides (i.e., glyphosate, bentazon, propanil, quinclorac, and 2,4-D) currently labeled in Arkansas rice–soybean production systems. Based on the percentage of aboveground dry weight reduction, control of the yellow nutsedge biotypes with the labeled rate of bentazon, propanil, quinclorac, and 2,4-D was < 44%. Glyphosate (867 g ae ha−1) resulted in 68 and > 94% control of theResand susceptible yellow nutsedge biotypes, respectively, at 28 d after treatment. Dose-response studies were conducted to estimate the efficacy of glyphosate on theResbiotype, three susceptible yellow nutsedge biotypes, and purple nutsedge. Based on the dry weights, theResbiotype was ≥ 5- and ≥ 1.3-fold less responsive to glyphosate compared to the susceptible biotypes and purple nutsedge, respectively. Differences in absorption and translocation of radiolabeled glyphosate were observed among the yellow nutsedge biotypes and purple nutsedge. The susceptible biotype had less14C-glyphosate radioactivity in the tissues above the treated leaf and greater radioactivity in tissues below the treated leaf compared to theResbiotype and purple nutsedge. Reduced translocation of glyphosate in tissues below the treated leaf of theResbiotype could be a reason for the lower glyphosate efficacy in theResbiotype. No amino acid substitution that would correspond to glyphosate resistance was found in the 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) gene of theResbiotype. However, an amino acid (serine) addition was detected in the EPSPS gene of theResbiotype; albeit, it is not believed that this addition contributes to lower efficacy of glyphosate in this biotype.

Target site–based penoxsulam resistance in barnyardgrass (Echinochloa crus-galli) from China

Weed Science ◽  
2019 ◽  
Vol 67 (3) ◽  
pp. 281-287 ◽  
Author(s):  
Jiapeng Fang ◽  
Tingting Liu ◽  
Yuhua Zhang ◽  
Jun Li ◽  
Liyao Dong
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Cross Resistance ◽  
Predicted Amino Acid Sequence ◽  
Sequence Analyses ◽  
Als Inhibitors ◽  
Higher Sensitivity

AbstractBarnyardgrass [Echinochloa crus-galli (L.) P. Beauv.] is acknowledged to be the most troublesome weed in rice fields in Anhui and Jiangsu provinces of China. It cannot be effectively controlled using certain acetolactate synthase (ALS)-inhibiting herbicides, including penoxsulam. Echinochloa crus-galli samples with suspected resistance to penoxsulam were collected to identify the target site–based mechanism underlying this resistance. Populations AXXZ-2 and JNRG-2 showed 33- and 7.3-fold resistance to penoxsulam, respectively, compared with the susceptible JLGY-3 population. Cross-resistance to other ALS inhibitors was reported in AXXZ-2 but not in JNRG-2, and occasionally showed higher sensitivity than JLGY-3. In vitro ALS activity assays revealed that penoxsulam concentrations required to inhibit 50% of ALS activity were 11 and 5.2 times greater in AXXZ-2 and JNRG-2, respectively, than in JLGY-3. DNA and predicted amino acid sequence analyses of ALS revealed Ala-205-Val and Ala-122-Gly substitutions in AXXZ-2 and JNRG-2, respectively. Our results indicate that these substitutions in ALS are at least partially responsible for resistance to penoxsulam.

scholarly journals Distribution of Herbicide Resistances and Molecular Mechanisms Conferring Resistance in Missouri Waterhemp (Amaranthus rudisSauer) Populations

Weed Science ◽  
2015 ◽  
Vol 63 (1) ◽  
pp. 336-345 ◽  
Author(s):  
John L. Schultz ◽  
Laura A. Chatham ◽  
Chance W. Riggins ◽  
Patrick J. Tranel ◽  
Kevin W. Bradley
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Molecular Mechanisms ◽  
Dna Analysis ◽  
D1 Protein ◽  
Acetolactate Synthase ◽  
Glyphosate Resistance ◽  
Mechanisms Of Action ◽  
Resistance To Herbicides ◽  
Inhibitor Resistance

A survey of soybean fields containing waterhemp was conducted just prior to harvest in 2012 to determine the scope and extent of herbicide resistance and multiple herbicide resistances among a sample of Missouri waterhemp populations. Resistance was confirmed to glyphosate and to acetolactate synthase (ALS), protoporphyrinogen oxidase (PPO), photosystem II (PSII), and 4-hydroxyphenylpyruvate dioxygenase (HPPD) inhibitors, but not to 2,4-D. Of the 187 populations tested, 186 exhibited resistance to chlorimuron. The proportions of populations with atrazine or glyphosate resistance were similar, with 30 and 29% of the populations surviving the 3× rates. Lactofen resistance was observed in 5% of the populations, whereas mesotrione resistance was only found in 1.6% of the populations. All populations tested were susceptible to 2,4-D at the 3× rate. At least 52% of the waterhemp populations tested exhibited resistance to herbicides from two mechanism of action. Resistance to atrazine plus chlorimuron as well as glyphosate plus chlorimuron was present in 29% of the populations. Three-way resistance, primarily comprised of resistance to atrazine plus chlorimuron plus glyphosate, was present in 11% of the populations. Resistance to herbicides from four mechanisms of action was found in 2% of the populations, and one population exhibited resistance to herbicides from five mechanisms of action. DNA analysis of a subsample of plants revealed that previously documented mechanisms of resistance in waterhemp, including the ΔG210 deletion conferring PPO-inhibitor resistance, the Trp574Leu amino acid substitution conferring ALS-inhibitor resistance, and elevated 5-enolypyruvyl-shikimate-3-phosphate synthase copy number and the Pro106Ser amino acid substitution resulting in glyphosate resistance, explained survival in many, but not all, instances. Atrazine resistance was not explained by the Ser264Gly D1 protein substitution. Overall, results from these experiments indicate that Missouri soybean fields contain waterhemp populations with resistance to glyphosate, ALS-, PPO-, PSII-, and HPPD-inhibiting herbicides, which are some of the most common mechanisms of action currently utilized for the control of this species in corn and soybean production systems. Additionally, these results indicate that slightly more than half of the populations tested exhibit resistance to more than one herbicide mechanisms of action. Managing the current resistance levels in existing populations is of utmost importance. The use of multiple, effective herbicide modes of action, both preemergence and postemergence, and the integration of optimum cultural and mechanical control practices will be vital in the management of Missouri waterhemp populations in the future.

scholarly journals Multiple mutations in the EPSPS and ALS genes of Amaranthus hybridus underlie resistance to glyphosate and ALS inhibitors

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Maria J. García ◽  
Candelario Palma-Bautista ◽  
José G. Vazquez-Garcia ◽  
Antonia M. Rojano-Delgado ◽  
María D. Osuna ◽  
...  
Keyword(s):  
Amino Acid ◽  
Target Genes ◽  
Acetolactate Synthase ◽  
Resistance Mechanisms ◽  
Activity Level ◽  
Cross Resistance ◽  
Weed Species ◽  
Amaranthus Hybridus ◽  
Als Inhibitors ◽  
Moderate Resistance

Abstract Amaranthus hybridus is one of the main weed species in Córdoba, Argentina. Until recently, this weed was effectively controlled with recurrent use of glyphosate. However, a population exhibiting multiple resistance (MR2) to glyphosate and imazamox appeared in a glyphosate resistant (GR) soybean field, with levels of resistance up to 93 and 38-fold higher to glyphosate and imazamox, respectively compared to the susceptible (S) population. In addition to imidazolinones, MR2 plants showed high resistance levels to sulfonylamino-carbonyl (thio) benzoates and moderate resistance to sulfonylureas and triazolopyrimidines. Multiple amino acid substitutions were found in both target genes, acetolactate synthase (ALS) and 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), responsible for conferring high herbicides resistance levels in this A. hybridus population. In the case of EPSPS, the triple amino acid substitution TAP-IVS was found. In addition, MR2 plants also showed increased EPSPS gene expression compared to susceptible plants. A Ser653Asn substitution was found in the ALS sequence of MR2, explaining the pattern of cross-resistance to the ALS-inhibitor herbicide families found at the ALS enzyme activity level. No other mutations were found in other conserved domains of the ALS gene. This is the first report worldwide of the target site resistance mechanisms to glyphosate and ALS inhibitors in multiple herbicide resistance Amaranthus hybridus.

Molecular Basis of Resistance to ALS-Inhibitor Herbicides in Greater Beggarticks

Weed Science ◽  
2009 ◽  
Vol 57 (5) ◽  
pp. 474-481 ◽  
Author(s):  
Fabiane P. Lamego ◽  
Dirk Charlson ◽  
Carla A. Delatorre ◽  
Nilda R. Burgos ◽  
Ribas A. Vidal
Keyword(s):  
Amino Acid ◽  
Molecular Basis ◽  
Single Point ◽  
Acetolactate Synthase ◽  
Amino Acid Sequences ◽  
Single Point Mutation ◽  
Weed Species ◽  
Herbicide Resistant ◽  
Als Inhibitors ◽  
Als Inhibitor

Soybean is a major crop cultivated in Brazil, and acetolactate synthase (ALS)-inhibiting herbicides are widely used to control weeds in this crop. The continuous use of these ALS-inhibiting herbicides has led to the evolution of herbicide-resistant weeds worldwide. Greater beggarticks is a polyploid species and one of the most troublesome weeds in soybean production since the discovery of ALS-resistant biotypes in 1996. To confirm and characterize the resistance of greater beggarticks to ALS inhibitors, whole-plant bioassays and enzyme experiments were conducted. To investigate the molecular basis of resistance in greater beggarticks theALSgene was sequenced and compared between susceptible and resistant biotypes. Our results confirmed that greater beggarticks is resistant to ALS inhibitors and also indicated it possesses at least three isoforms of theALSgene. Analysis of the nucleotide and deduced amino acid sequences among the isoforms and between the biotypes indicated that a single point mutation, G–T, in oneALSisoform from the resistant biotype resulted in an amino acid substitution, Trp574Leu. Two additional substitutions were observed, Phe116Leu and Phe149Ser, in a second isoform of the resistant biotype, which were not yet reported in any other herbicide-resistantALSgene; thus, their role in conferring herbicide resistance is not yet ascertained. This is the first report ofALSmutations in an important, herbicide-resistant weed species from Brazil.

Resistance in Canadian biotypes of wild mustard (Sinapis arvensis) to acetolactate synthase inhibiting herbicides

Weed Science ◽  
2005 ◽  
Vol 53 (5) ◽  
pp. 631-639 ◽  
Author(s):  
Suzanne I. Warwick ◽  
Connie Sauder ◽  
Hugh J. Beckie
Keyword(s):  
Amino Acid ◽  
Single Gene ◽  
Acetolactate Synthase ◽  
Western Canada ◽  
Nucleotide Polymorphisms ◽  
Weed Species ◽  
Susceptible Population ◽  
Wild Mustard ◽  
Als Inhibitors ◽  
Als Inhibitor

Multiple cases of ALS inhibitor-resistant weed biotypes are reported for many species, including wild mustard. The physiological extent and molecular basis of resistance to ALS inhibitors was compared in four biotypes of wild mustard from western Canada: a sulfonylurea (SU)-resistant (R) biotype from Manitoba detected in 1992; an SU (ethametsulfuron)-R biotype from Alberta detected in 1993 (metabolism-based resistance); an SU-R biotype from Manitoba detected in 2002; and a SU- and imidazolinone (IMI)-R biotype from Saskatchewan detected in 2002. Herbicide dose-response experiments confirmed that the two Manitoba biotypes were resistant to the SU herbicides ethametsulfuron and tribenuron : thifensulfuron mixture, whereas the Saskatchewan biotype was resistant to both SU herbicides and to imazethapyr, an IMI herbicide. Sequence analysis of theALSgene detected target site mutations in three of the four R biotypes, with amino acid substitutions Pro197(CCT) to Ser (TCT) [Domain A of the gene] in the two SU-R Manitoba biotypes and Trp574(TGG) to Leu (TTG) [Domain B] in the Saskatchewan biotype. The Alberta SU-R biotype had the sameALSnucleotide and amino acid sequence as the susceptible population at these two positions. Two heterozygous individuals [Trp574(Tt/gG)] were detected in the Saskatchewan biotype, and genetic segregation for nucleotide bases and resistance phenotype was consistent with single gene control. Nucleotide variation in neutral regions of theALSgene varied with biotype, with no variation in the two Manitoba biotypes, two variants in the Saskatchewan biotype, and 16 neutral nucleotide polymorphisms (0.9%) in the Alberta biotype. The occurrence of at least three different ALS inhibitor-R biotypes in this important weed species is likely to impact negatively on the use of ALS inhibitors, such as the IMIs, and serves as a warning for strict implementation of herbicide rotations to prevent or delay the evolution and spread of such populations.

scholarly journals ALS Gene Mutations in Apera Spica-Venti Confer Broad-Range Resistance to Herbicides

2011 ◽  
Vol 51 (3) ◽  
pp. 261-267 ◽  
Author(s):  
Michał Krysiak ◽  
Stanisław Gawroński ◽  
Kazimierz Adamczewski ◽  
Roman Kierzek
Keyword(s):  
Gene Mutations ◽  
Pcr Amplification ◽  
Acetolactate Synthase ◽  
Nucleotide Polymorphisms ◽  
Molecular Tests ◽  
Whole Plant ◽  
Plant Bioassay ◽  
Resistance To Herbicides ◽  
Als Inhibitors ◽  
High Level

ALS Gene Mutations in Apera Spica-Venti Confer Broad-Range Resistance to Herbicides Several biotypes of wind bentgrass in Poland have been identified as being resistant to acetolactate synthase (ALS) inhibitors. We screened these weeds with chlorsulfuron and performed a whole-plant bioassay with a range of doses based on these four herbicides: chlorsulfuron, sulfosulfuron, propoxycarbazone-sodium and mesosulfuron-methyl + iodosulfuron-methyl-sodium mixture. Ten biotypes, diverse in their levels of resistance, were submitted for molecular tests. PCR amplification and sequencing of als domains demonstrated numerous single nucleotide polymorphisms. Nine biotypes showed non-synonymous substitutions in codon Pro197, changing it to Ser or Thr. Mutation in Pro197 conferred a high level of resistance to the tested herbicides. Analysis of four biotypes also revealed a substitution in the Ala122 codon, changing it to Val. In one biotype this substitution was not accompanied by Pro197 mutation and this biotype was resistant to chlorsulfuron and mesosulfuron + iodosulfuron, but not to sulfosulfuron or propoxycarbazone-sodium. Correspondence between mutations and levels of resistan ce to ALS inhibitors may support management of resistant weeds with the existing palette of herbicides.

Molecular basis of multiple resistance to herbicides inhibiting acetyl-CoA carboxylase and acetolactate synthase in American sloughgrass (Beckmannia syzigachne) from China

2016 ◽  
Vol 67 (11) ◽  
pp. 1208 ◽  
Author(s):  
Lang Pan ◽  
Haitao Gao ◽  
Han Wu ◽  
Liyao Dong
Keyword(s):  
Acetolactate Synthase ◽  
Alternative Methods ◽  
Multiple Resistance ◽  
Homozygous Mutation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Wheat Field ◽  
Sequence Method ◽  
Resistance To Herbicides ◽  
Als Inhibitors

American sloughgrass (Beckmannia syzigachne Steud.) is a problematic grass that is widely distributed in wheat and oilseed rape fields in China. The herbicides fenoxaprop-P-ethyl and mesosulfuron-methyl failed to control B. syzigachne JCWJ-R populations collected from a wheat field in Jiangsu Province. Dose-response experiments showed that JCWJ-R was resistant to the acetyl-CoA carboxylase (ACCase) inhibitors fenoxaprop-P-ethyl (33.8-fold), haloxyfop-R-methyl (12.7-fold), clethodim (7.8-fold) and pinoxaden (11.6-fold), and to the acetolactate synthase (ALS) inhibitors mesosulfuron-methyl (15.9-fold), pyroxsulam (17.6-fold), flucarbazone-Na (10.7-fold) and imazethapyr (7-fold). Resistance to ALS inhibitors was due to a Pro-197-Ser mutation in the ALS gene and resistance to ACCase inhibitors was due to an Ile-1781-Leu mutation in the ACCase gene. A derived cleaved amplified polymorphic sequence method was developed to detect the ALS mutation in B. syzigachne. This was combined with a previously established method to detect Ile-1781-Leu, and the mutation frequency and homozygous mutation rates in the JCWJ-R population were determined. The evolution of multiple resistance to ACCase and ALS inhibitors in this B. syzigachne population indicated that alternative methods should be developed to control resistant weeds.

scholarly journals Herbicide Resistance in Phalaris Species: A Review

Plants ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 2248
Author(s):  
Javid Gherekhloo ◽  
Saeid Hassanpour-bourkheili ◽  
Parvin Hejazirad ◽  
Sajedeh Golmohammadzadeh ◽  
Jose G. Vazquez-Garcia ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Herbicide Resistance ◽  
Acetolactate Synthase ◽  
Fitness Cost ◽  
Acetyl Coa Carboxylase ◽  
Mechanisms Of Resistance ◽  
Ps Ii ◽  
Herbicide Resistant ◽  
Evolution Of Resistance ◽  
Resistance To Herbicides

Weeds, such as Phalaris spp., can drastically reduce the yield of crops, and the evolution of resistance to herbicides has further exacerbated this issue. Thus far, 23 cases of herbicide resistance in 11 countries have been reported in Phalaris spp., including Phalaris minor Retz., Phalaris paradoxa L., and Phalaris brachystachys L., for photosystem II (PS-II), acetyl-CoA carboxylase (ACCase), and acetolactate synthase (ALS)-inhibiting herbicides. This paper will first review the cases of herbicide resistance reported in P. minor, P. paradoxa, and P. brachystachys. Then, the mechanisms of resistance in Phalaris spp. are discussed in detail. Finally, the fitness cost of herbicide resistance and the literature on the management of herbicide-resistant weeds from these species are reviewed.

scholarly journals Activity of Antioxidant Enzymes in Euphorbia heterophylla Biotypes and their Relation to Cross Resistance to ALS and Protox Inhibitors

2018 ◽  
Vol 36 ◽  
Author(s):  
E. XAVIER ◽  
M.M. TREZZI ◽  
M.C. OLIVEIRA ◽  
R.A. VIDAL ◽  
A.P. BRUSAMARELLO
Keyword(s):  
Antioxidant Enzymes ◽  
Acetolactate Synthase ◽  
Cross Resistance ◽  
Multiple Resistance ◽  
Protoporphyrinogen Oxidase ◽  
Resistance Factors ◽  
Resistance To Herbicides ◽  
Als Inhibitors ◽  
The One ◽  
Chemical Groups

ABSTRACT: The characteristics of multiple resistance in Euphorbia heterophylla biotypes to herbicides that are inhibitors of ALS (Acetolactate synthase) and PPO (Protoporphyrinogen oxidase) and their responsible mechanisms are still not completely elucidated. The objectives of this study were to identify cross-resistance to herbicides from different chemical groups of ALS inhibitors (imidazolinones, sulfonylureas, pyrimidyl benzoates and sulfonanilides) and also PPO inhibitors (diphenylethers, phthalamides, oxadiazoles, triazolinones and pyrimidinediones) in E. heterophylla biotypes with multiple resistance to these herbicides; to analyze whether the antioxidant enzymes superoxide dismutase (SOD) and peroxidase (POD) constitute mechanisms that are responsible for the resistance to PPO inhibitors. Initially, the response to doses of herbicides from these different chemical groups was determined, using doses below and above the one recommended for the species. The control of E. heterophylla was determined, estimating the required doses for a 50 and 80% control reduction and calculating the resistance factors. The constitutive and induced activities of the SOD and POD enzymes were also determined. The results confirmed cross-resistance for all chemical groups of ALS and PPO inhibitors in the Bom Sucesso do Sul and Vitorino biotypes. The constitutive and induced activities of the SOD and POD enzymes were superior in plants from the E. heterophylla biotypes Vitorino and Bom Sucesso do Sul, contributing to their resistance to PPO inhibiting herbicides.

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