Molecular Basis of Resistance to Herbicides Inhibiting Acetolactate Synthase in Two Rigid Ryegrass (Lolium rigidum) Populations from Australia

Weed Science ◽  
2012 ◽  
Vol 60 (2) ◽  
pp. 172-178 ◽  
Author(s):  
Shiv S. Kaundun ◽  
Richard P. Dale ◽  
Géraldine C. Bailly
Keyword(s):  
Molecular Basis ◽  
Molecular Mechanisms ◽  
Codon Position ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Weed Species ◽  
Site Mutation ◽  
Sulfometuron Methyl ◽  
Whole Plant ◽  
Field Samples

Acetolactate Synthase- (ALS) inhibiting herbicides are important components for the control of ryegrass species infesting cereal-cropping systems worldwide. Although resistance to ALS herbicides in ryegrasses has evolved more than 25 yr ago, few studies have been dedicated to elucidate the molecular mechanisms involved. To this end, we have investigated the molecular basis of chlorsulfuron, sulfometuron-methyl, and imazapyr resistance in AUS5 and AUS23, two ryegrass populations from Australia. Comparison between whole-plant herbicide assays and DNA sequencing results showed that resistance to the nonmetabolizable herbicide sulfometuron-methyl was associated with four different proline mutations at ALS codon position 197 (P197) in AUS23. In addition to three P197 amino acid changes impacting on the efficacies of the two sulfonylurea herbicides, the tryptophan to leucine target-site mutation at ALS codon position 574 (W574L) was present in AUS5, conferring resistance to both sulfometuron-methyl and imazapyr. The samples were also characterized by non target-site-based resistance impacting on the metabolizable herbicide chlorsulfuron only. Interestingly, compound mutant heterozygotes threonine/serine at ALS position 197, and plants with double mutations at positions 197 and 574 were detected, thus reflecting the ability of this outcrossing species to accumulate mutant alleles. Whole-plant dose-response assays conducted on predetermined wild-type and mutant genotypes originating from the same populations allowed for a more precise estimation of the dominant and very high levels of resistance associated with the proline to serine target-site mutation at ALS codon position 197 (P197S) and W574L mutations. The two highly efficient polymerase chain reaction- (PCR) based derived cleaved amplified polymorphic sequence (dCAPS) markers developed here will allow for quick confirmation of 197 and 574 ALS target-site resistance in ryegrass species field samples and also contribute to identify populations characterized by other likely resistance mechanisms in this important weed species.

Acetolactate Synthase (ALS) Target-Site Mutations in ALS Inhibitor-Resistant Russian Thistle (Salsola tragus)

Weed Science ◽  
2010 ◽  
Vol 58 (3) ◽  
pp. 244-251 ◽  
Author(s):  
Suzanne I. Warwick ◽  
Connie A. Sauder ◽  
Hugh J. Beckie
Keyword(s):  
Molecular Basis ◽  
Genome Structure ◽  
Acetolactate Synthase ◽  
Molecular Techniques ◽  
Target Site ◽  
Weed Species ◽  
Single Nucleotide ◽  
Herbicide Resistant ◽  
Inhibitor Resistance ◽  
Als Inhibitor

ALS inhibitor-resistant biotypes are the fastest growing class of herbicide-resistant (HR) weeds. A Canadian ALS inhibitor-resistant biotype of Russian thistle was first reported in 1989. The molecular basis for ALS-inhibitor resistance is unknown for Canadian populations of this polyploid weed species, and was determined in this study for one Alberta and two Saskatchewan HR Russian thistle populations. HR plants survived spray application of the ALS-inhibitor mixture thifensulfuron : tribenuron in the greenhouse. All three HR Russian thistle populations were heterogeneous and contained both HR and herbicide-susceptible (HS) individuals. The molecular basis for resistance was determined by sequencing theALSgene and/or conducting a TaqMan genotyping assay for single nucleotide polymorphism (SNP) for the Trp574Leu mutation. Two target-site mutations were observed: Trp574Leu in all three biotypes (554 individuals) and Pro197Gln in one biotype (one individual), suggesting multiple-founding events for Russian thistle HR populations in western Canada. Segregation patterns among F1 and F2 progeny arrays of HR lines sprayed under greenhouse conditions varied; some segregated (i.e., had HR and HS progeny), whereas other lines were exclusively HR. In contrast, no segregation of molecular types, i.e., Trp574, Trp/Leu574and Leu574, as would be expected with heterozygosity at a single locus Trp/Leu574, was observed. Such lack of segregation is consistent with the polyploid genome structure of Russian thistle and the presence of two copies of theALSgene. The presence of more than oneALSgene confounded the ability of the molecular techniques to accurately identify “true” heterozygotes in this study.

scholarly journals Target site as the main mechanism of resistance to imazamox in a Euphorbia heterophylla biotype

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Antonia M. Rojano-Delgado ◽  
João M. Portugal ◽  
Candelario Palma-Bautista ◽  
Ricardo Alcántara-de la Cruz ◽  
Joel Torra ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Root Exudation ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Southern Brazil ◽  
Fresh Weight ◽  
Weed Species ◽  
Site Mutation ◽  
Principal Mechanism ◽  
Continuous Use

Abstract Euphorbia heterophylla is a weed species that invades extensive crop areas in subtropical regions of Brazil. This species was previously controlled by imazamox, but the continuous use of this herbicide has selected for resistant biotypes. Two biotypes of E. heterophylla from southern Brazil, one resistant (R) and one susceptible (S) to imazamox, were compared. The resistance of the R biotype was confirmed by dose-response assays since it required 1250.2 g ai ha−1 to reduce the fresh weight by 50% versus 7.4 g ai ha−1 for the S biotype. The acetolactate synthase (ALS) enzyme activity was studied using ALS-inhibiting herbicides from five different chemical families. The R biotype required the highest concentrations to reduce this enzyme activity by 50%. A Ser653Asn mutation was found in the ALS gene of the R biotype. The experiments carried out showed that imazamox absorption and metabolism were not involved in resistance. However, greater 14C-imazamox root exudation was found in the R biotype (~70% of the total absorbed imazamox). Target site mutation in the ALS gene is the principal mechanism that explains the imazamox resistance of the R biotype, but root exudation seems to also contribute to the resistance of this biotype.

scholarly journals Molecular Basis of Evolved Resistance to Glyphosate and Acetolactate Synthase-Inhibitor Herbicides in Kochia (Kochia scoparia) Accessions from Montana

Weed Science ◽  
2015 ◽  
Vol 63 (4) ◽  
pp. 758-769 ◽  
Author(s):  
Vipan Kumar ◽  
Prashant Jha ◽  
Darci Giacomini ◽  
Eric P. Westra ◽  
Philip Westra
Keyword(s):  
Molecular Mechanisms ◽  
Conservation Tillage ◽  
Cropping Systems ◽  
Rapid Evolution ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Northern Great Plains ◽  
Site Mutation ◽  
Als Inhibitor

The rapid evolution and spread of glyphosate-resistant (GR) kochia in the Northern Great Plains is an increasing threat to GR cropping systems and conservation tillage practices common in this region. GR kochia accessions with 4.6- to 11-fold levels of resistance to glyphosate have recently been reported in Montana. Those GR kochia accessions were also suspected to be resistant to acetolactate synthase (ALS) inhibitors, i.e., multiple herbicide-resistant (MHR) kochia. In this research, the level of resistance to the ALS-inhibitor herbicides (sulfonylureas) and the molecular mechanisms conferring resistance to glyphosate and ALS-inhibitor herbicides in MHR kochia was investigated. On the basis of whole-plant dose–response assays, MHR kochia accessions (GIL01, JOP01, and CHES01) were 9.3- to 30-fold more resistant to premixed thifensulfuron methyl + tribenuron methyl + metsulfuron methyl than the susceptible (SUS) accession. In an in vivo leaf-disk shikimate assay, MHR plants accumulated less shikimate than the SUS plants at a discriminate dose of 100 μM glyphosate. Sequencing of the conserved region ofEPSPSrevealed no target-site mutation at Thr102or Pro106residue. MHR kochia accessions had increased relativeEPSPSgene copies (~ 4 to 10) compared with the SUS accession (single copy). Furthermore, MHR kochia accumulated higher EPSPS protein compared with the SUS plants. Resistance to the ALS-inhibitor herbicides was conferred by Pro197amino acid substitution (proline to glutamine).EPSPSgene amplification and a single target-site mutation at Pro197inALSgene confer resistance to glyphosate and ALS-inhibitor herbicides, respectively, in MHR kochia accessions from Montana. This is the first confirmation of occurrence of MHR kochia in Montana.

Investigating the resistance levels and mechanisms to penoxsulam and cyhalofop-butyl in barnyardgrass (Echinochloa crus-galli) from Ningxia province, China

Weed Science ◽  
2021 ◽  
pp. 1-25
Author(s):  
Qian Yang ◽  
Xia Yang ◽  
Zichang Zhang ◽  
Jieping Wang ◽  
Weiguo Fu ◽  
...  
Keyword(s):  
Herbicide Resistance ◽  
Molecular Mechanisms ◽  
Acetolactate Synthase ◽  
Rice Fields ◽  
Target Site ◽  
Herbicide Resistant ◽  
Susceptible Populations ◽  
High Level ◽  
Als Inhibitor ◽  
Encoding Genes

Abstract Barnyardgrass (Echinochloa crus-galli) is a noxious grass weed which infests rice fields and causes huge crop yield losses. In this study, we collected twelve E. crus-galli populations from rice fields of Ningxia province in China and investigated the resistance levels to acetolactate synthase (ALS) inhibitor penoxsulam and acetyl-CoA carboxylase (ACCase) inhibitor cyhalofop-butyl. The results showed that eight populations exhibited resistance to penoxsulam and four populations evolved resistance to cyhalofop-butyl. Moreover, all of the four cyhalofop-butyl-resistant populations (NX3, NX4, NX6 and NX7) displayed multiple-herbicide-resistance (MHR) to both penoxsulam and cyhalofop-butyl. The alternative herbicides bispyribac-sodium, metamifop and fenoxaprop-P-ethyl cannot effectively control the MHR plants. To characterize the molecular mechanisms of resistance, we amplified and sequenced the target-site encoding genes in resistant and susceptible populations. Partial sequences of three ALS genes and six ACCase genes were examined. A Trp-574-Leu mutation was detected in EcALS1 and EcALS3 in two high-level (65.84- and 59.30-fold) penoxsulam-resistant populations NX2 and NX10, respectively. In addition, one copy (EcACC4) of ACCase genes encodes a truncated aberrant protein due to a frameshift mutation in E. crus-galli populations. None of amino acid substitutions that are known to confer herbicide resistance were detected in ALS and ACCase genes of MHR populations. Our study reveals the widespread of multiple-herbicide resistant E. crus-galli populations at Ningxia province of China that exhibit resistance to several ALS and ACCase inhibitors. Non-target-site based mechanisms are likely to be involved in E. crus-galli resistance to the herbicides, at least in four MHR populations.

Translation of In Vitro Activity to In Vivo Activity: Lessons from the Triazolopyrimidine Sulfonanilides

Weed Science ◽  
1996 ◽  
Vol 44 (3) ◽  
pp. 757-762 ◽  
Author(s):  
B. Clifford Gerwick ◽  
Csaba T. Cseke ◽  
Gerry Deboer ◽  
William A. Kleschick ◽  
Paul R. Schmitzer
Keyword(s):  
Acetolactate Synthase ◽  
Metabolic Stability ◽  
Plant Structure ◽  
Weed Species ◽  
Whole Plant ◽  
Stability Data ◽  
Activity Models ◽  
Two Parameter

Eight triazolopyrimidine sulfonanilides were tested for metabolic stability in a number of crop and weed species. These data, along with in vitro determinations of activity (I50) against acetolactate synthase, successfully described the in vivo activity of these compounds in a two-parameter model. Whole plant activity increased with increasing compound stability and decreasing I50 (r2 =.78, N = 36). The difficulty in obtaining metabolic stability data during a structure optimization program prompted a study with substituent parameters in models of in vivo activity. Models describing whole plant activity in jimsonweed were developed using a series of 5-methyl triazolopyrimidine sulfonanilides that differed only in ortho and meta substituents on the aniline ring. The I50 term and clogP were most important to jimsonweed activity. Hence, in vitro activity (I50) may be a useful component of whole plant structure activity models to aid in identification of barriers to in vivo performance.

Acetolactate Synthase Gene Proline (197) Mutations Confer Tribenuron-Methyl Resistance in Flixweed (Descurainia sophia) Populations from China

Weed Science ◽  
2011 ◽  
Vol 59 (3) ◽  
pp. 376-379 ◽  
Author(s):  
Hai Lan Cui ◽  
Chao Xian Zhang ◽  
Shou Hui Wei ◽  
Hong Jun Zhang ◽  
Xiang Ju Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Molecular Basis ◽  
Resistance Mechanism ◽  
Point Mutations ◽  
Acetolactate Synthase ◽  
Amino Acid Position ◽  
Resistance Level ◽  
Coding Sequence ◽  
Whole Plant ◽  
Tribenuron Methyl

The molecular basis of resistance to tribenuron-methyl, an acetolactate synthase (ALS)–inhibiting herbicide was investigated in four resistant (R) and three susceptible (S) flixweed populations. The resistance level in the R populations was assessed in whole-plant pot experiments in a greenhouse, and resistance indices ranged from 723 to 1422. The ALS genes of the three S populations and four R populations were cloned and sequenced, and the full coding sequence of the ALS gene of flixweed was 2,004 bp. The sequences of the ALS genes of the three S populations collected from Shaanxi, Gansu, and Tianjin were identical. Comparison of the ALS gene sequences of the S and R populations withArabidopsisrevealed that proline at position 197 of the ALS gene was substituted by leucine in R population SSX-2, by alanine in R population SSX-3, and by serine in R populations TJ-2 and GS-2. In another study of two R flixweed populations from Hebei and Shaanxi, resistance was also related to mutation at position 197 of the ALS gene. Both studies confirmed tribenuron-methyl resistance in flixweed in China, with the resistance mechanism being conferred by specific ALS point mutations at amino acid position 197.

scholarly journals Multiple-Herbicide Resistance in a 2,4-D–Resistant Waterhemp (Amaranthus tuberculatus) Population from Nebraska

Weed Science ◽  
2017 ◽  
Vol 65 (6) ◽  
pp. 743-754 ◽  
Author(s):  
Roberto J. Crespo ◽  
Ana B. Wingeyer ◽  
Greg R. Kruger ◽  
Chance W. Riggins ◽  
Patrick J. Tranel ◽  
...  
Keyword(s):  
D1 Protein ◽  
Acetolactate Synthase ◽  
Mechanisms Of Action ◽  
Target Site ◽  
Site Mutation ◽  
Auxin Receptor ◽  
Application Rates ◽  
Chlorimuron Ethyl ◽  
Als Inhibitors ◽  
Susceptible Populations

A 2,4-D-resistant tall waterhemp population (FS) from Nebraska was evaluated for resistance to other TIR1 auxin receptor herbicides and to herbicides having alternative mechanisms of action using greenhouse bioassays and genetic markers. Atrazine, imazethapyr, lactofen, mesotrione, glufosinate, and glyphosate were applied in a single-dose bioassay, and tissue was collected from marked plants for genetic analysis. The FS population was not injured by atrazine or by imazethapyr. Approximately 50% of the plants survived lactofen and were actively growing 28 d after treatment. The population was susceptible to mesotrione, glufosinate, and glyphosate. Ametryn, chlorimuron-ethyl, 2,4-D, aminocyclopyraclor, aminopyralid, and picloram were applied in dose–response studies. The FS population was sensitive to ametryn, and the Ser-264-Gly substitution in the D1 protein was not detected, suggesting the lack of response to atrazine is not due to a target-site mutation. The FS population exhibited less than 50% injury to chlorimuron-ethyl at application rates 20 times the labeled use rate. The Ser-653-Asn acetolactate synthase (ALS) substitution, which confers resistance to imidazolinone herbicides, was present in the FS population. However, this does not explain the lack of response to the sulfonylurea herbicide, chlorimuron-ethyl. Sequencing of a portion of thePPX2Lgene did not show the ΔG210 mutation that confers resistance to protoporphyrinogen oxidase–inhibiting herbicides, suggesting that other factors were responsible for waterhemp survival after lactofen application. The FS population was confirmed to be at least 30-fold resistant to 2,4-D relative to the susceptible populations. In addition, it was at least 3-fold less sensitive to aminopyralid and picloram, two other TIR1 auxin receptor herbicides, than the 2,4-D-susceptible populations were. These data indicated that the FS population contains both target and non–target site mechanisms conferring resistance to herbicides spanning at least three mechanisms of action: TIR1 auxin receptors, ALS inhibitors, and photosystem II inhibitors.

Acetolactate synthase inhibitor-resistant stinkweed (Thlaspi arvense L.) in Alberta

2007 ◽  
Vol 87 (4) ◽  
pp. 965-972 ◽  
Author(s):  
H. J. Beckie ◽  
L. M. Hall ◽  
F. J. Tardif ◽  
G. Séguin-Swartz
Keyword(s):  
Herbicide Resistance ◽  
Dominant Gene ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Cross Resistance ◽  
Resistance Pattern ◽  
Site Mutation ◽  
Thlaspi Arvense ◽  
Synthase Inhibitor ◽  
Als Inhibitor

Two stinkweed populations from southern and central Alberta were not controlled by acetolactate synthase (ALS)-inhibiting herbicides in 2000. This study reports on their cross-resistance to ALS-inhibiting herbicides, molecular basis of resistance, and inheritance of resistance. Both putative herbicide-resistant biotypes responded similarly to increasing doses of the herbicides. The biotypes were highly resistant to ethametsulfuron and exhibited a low level of resistance to metsulfuron and imazethapyr. However, both biotypes were not resistant to florasulam, a triazolopyrimidine ALS inhibitor, or sulfometuron, a non-selective sulfonylurea ALS inhibitor. The cross-resistance pattern was consistent with the confirmed target-site mutation. Sequence analysis of the ALS gene detected a Pro197Leu mutation in both biotypes. Similar to many other ALS inhibitor-resistant weed biotypes, resistance was conferred by a single dominant gene. This study confirms the first global occurrence of herbicide resistance in this species. Key words: ALS-inhibitor resistance, ALS sequence, herbicide resistance, target-site mutation

Molecular Basis of Resistance to Tribenuron in Water Starwort (Myosoton aquaticum) Populations from China

Weed Science ◽  
2013 ◽  
Vol 61 (3) ◽  
pp. 390-395 ◽  
Author(s):  
Weitang Liu ◽  
Yaling Bi ◽  
Lingxu Li ◽  
Guohui Yuan ◽  
Jinxin Wang
Keyword(s):  
Molecular Basis ◽  
Inhibitory Concentration ◽  
Acetolactate Synthase ◽  
Susceptible Population ◽  
Documented Case ◽  
Whole Plant ◽  
Winter Annual ◽  
High Level ◽  
Plant Bioassays

Populations of water starwort, a winter annual or biennial weed in the pink family (Caryophyllaceae), can no longer be controlled by tribenuron following successive use of this herbicide over several years. Whole-plant bioassays have established that the resistant water starwort populations JS17, JS08, JS16, and JS07 showed high-level (from 203-fold to 565-fold) resistance to tribenuron. In vitro acetolactate synthase (ALS) assays revealed that resistance was due to reduced sensitivity of the ALS enzyme to tribenuron. The half-maximal inhibitory concentration (I50) values for JS17, JS08, JS16, and JS07 were 72, 71, 70, and 76 times greater, respectively, than were those of the susceptible population JS24. This altered ALS sensitivity in the resistant populations was due to a mutation in the ALS gene resulting in a Pro197to Ser substitution (JS17, JS08, and JS16) and a Pro197to Leu substitution (JS07). This study established the first documented case, to our knowledge, of evolved tribenuron resistance in water starwort and concluded that the molecular basis of resistance is due, at least in part, to a target-site modification at Pro197in the ALS gene.

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.

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