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.

Confirmation of Flixweed (Descurainia sophia) Resistance to Tribenuron-Methyl Using Three Different Assay Methods

Weed Science ◽  
2010 ◽  
Vol 58 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Xian Xu ◽  
Gui Qi Wang ◽  
Si Long Chen ◽  
Cui Qin Fan ◽  
Bing Hua Li
Keyword(s):  
Enzyme Assay ◽  
Close Association ◽  
Resistance Mechanism ◽  
Petri Dish ◽  
Acetolactate Synthase ◽  
Resistance Level ◽  
Whole Plant ◽  
Plant Bioassay ◽  
Assay Methods ◽  
Tribenuron Methyl

Research was conducted to establish a method to investigate the resistance level of flixweed to tribenuron-methyl and the evolved biochemical resistance mechanism. Four resistant biotypes were collected from wheat fields in Mazhuangcun, Jiacun, Dishangcun, and Bafangcun in the Hebei province of China where tribenuron-methyl had been continuously used for more than 10 yr. Two susceptible biotypes were collected from wheat fields where tribenuron-methyl was never applied. Different biotypes were assessed by petri-dish bioassay, whole-plant bioassay, and acetolactate synthase (ALS) assay. Comparisons of data indicated a similarity between methods and that experiments demonstrated that petri-dish bioassay was a feasible method to identify flixweed resistant to tribenuron-methyl. Data indicated differences among the flixweed biotypes when assessed by the petri-dish bioassay, whole-plant bioassay, or ALS enzyme assay, and a close association was obtained for the three bioassay methods. ALS resistance varied by biotypes with Mazhuangcun > Jiacun > Dishangcun > Bafangcun. Target-site enzyme assay data indicated that the resistant biotype's enhanced ALS activity was the biochemical mechanism that induced flixweed's evolved resistance to tribenuron-methyl. The concentrations of tribenuron-methyl causing 50% inhibition of ALS activity of the four resistant biotypes were 1,359, 513, 184, and 164 nM; in the susceptible biotypes these concentrations were 64 and 65 nM. Resistance indexes were 21, 8, 3, and 3 for Mazhuangcun, Jiacun, Dishangcun, and Bafangcun biotypes, respectively.

scholarly journals Genetic Variability of Acetolactate Synthase (ALS) Sequence in Centaurea cyanus Plants Resistant and Susceptible to Tribenuron-Methyl

Agronomy ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 2311
Author(s):  
Barbara Wrzesińska ◽  
Tadeusz Praczyk
Keyword(s):  
Amino Acid ◽  
Genetic Variability ◽  
Amino Acid Sequence ◽  
Herbicide Resistance ◽  
Resistance Mechanism ◽  
Acetolactate Synthase ◽  
Sequence Information ◽  
Sequence Variability ◽  
Centaurea Cyanus ◽  
Tribenuron Methyl

Centaurea cyanus, belonging to the Asteraceae family, is an arable weed species encountered mainly in fields with cereals, sugar beet, and maize. The high genetic variability of C. cyanus has been recently reported; however, little is known about its sequence variability in the context of its herbicide resistance. C. cyanus resistance was found mainly against acetolactate synthase (ALS) inhibitors, but no ALS sequence information concerning the herbicide resistance mechanism has been published yet. The aim of this study was to determine the ALS sequences for biotypes susceptible and resistant to tribenuron-methyl in order to identify mutations that may be associated with the resistance emergence. DNA isolation from susceptible and resistant plants was followed by PCR amplification and ALS sequencing. As a result, different lengths of DNA products were obtained. Moreover, both nucleotide and amino acid sequence analysis revealed high sequence variability within one plant as well as between plants from the same biotype. In a few resistant plants, four changes in the amino acid sequence were identified in comparison to those in the susceptible ones. However, these preliminary studies require further investigation toward confirming the significance of these mutations in herbicide resistance development. This study provides preliminary information contributing to the research on the C. cyanus target-site resistance mechanism.

scholarly journals Identification of separate domains in the adenovirus E1A gene for immortalization activity and the activation of virus early genes.

1986 ◽  
Vol 6 (10) ◽  
pp. 3470-3480 ◽  
Author(s):  
E Moran ◽  
B Zerler ◽  
T M Harrison ◽  
M B Mathews
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Point Mutations ◽  
Apparent Molecular Weight ◽  
Amino Acid Position ◽  
Cysteine Residue ◽  
Transformation Function ◽  
Single Amino Acid ◽  
Amino Acid Substitutions ◽  
E1a Gene

The transformation and early adenovirus gene transactivation functions of the E1A region were analyzed with deletion and point mutations. Deletion of amino acids from position 86 through 120 had little effect on the lytic or transforming functions of the E1A products, while deletion of amino acids from position 121 through 150 significantly impaired both functions. The sensitivity of the transformation function to alterations in the region from amino acid position 121 to 150 was further indicated by the impairment of transforming activity resulting from single amino acid substitutions at positions 124 and 135. Interestingly, conversion of a cysteine residue at position 124 to glycine severely impaired the transformation function without affecting the early adenovirus gene activating functions. Single amino acid substitutions in a different region of the E1A gene had the converse effect. All the mutants produced polypeptides of sufficient stability to be detected by Western immunoblot analysis. The single amino acid substitutions at positions 124 and 135, although impairing the transformation functions, did not detectably alter the formation of the higher-apparent-molecular-weight forms of the E1A products.

Continuous Use of Tribenuron-Methyl Selected for Cross-Resistance to Acetolactate Synthase–inhibiting Herbicides in Wild Mustard (Sinapis arvensis)

Weed Science ◽  
2018 ◽  
Vol 66 (4) ◽  
pp. 424-432 ◽  
Author(s):  
Javid Gherekhloo ◽  
Zahra M. Hatami ◽  
Ricardo Alcántara-de la Cruz ◽  
Hamid R. Sadeghipour ◽  
Rafael De Prado
Keyword(s):  
Winter Wheat ◽  
Acetolactate Synthase ◽  
Dry Weight ◽  
Resistance Mechanisms ◽  
Cross Resistance ◽  
Resistance Level ◽  
Sinapis Arvensis ◽  
Wild Mustard ◽  
Golestan Province ◽  
Tribenuron Methyl

AbstractWild mustard (Sinapis arvensis L.) is a weed that frequently infests winter wheat (Triticum aestivum L.) fields in Golestan province, Iran. Tribenuron-methyl (TM) has been used recurrently to control this species, thus selecting for resistant S. arvensis populations. The objectives were: (1) to determine the resistance level to TM of 14 putatively resistant (PR) S. arvensis populations, collected from winter wheat fields in Golestan province, Iran, in comparison to one susceptible (S) population; and (2) to characterize the resistance mechanisms and the potential evolution of cross-resistance to other classes of acetolactate synthase (ALS)-inhibiting herbicides in three populations (AL-3, G-5, and Ag-Sr) confirmed as being resistant (R) to TM. The TM doses required to reduce the dry weight of the PR populations by 50% were between 2.2 and 16.8 times higher than those needed for S plants. The ALS enzyme activity assays revealed that the AL-3, G-5, and Ag-Sr populations evolved cross-resistance to the candidate ALS-inhibiting herbicides from the sulfonylureas (SU), triazolopyrimidines (TP), pyrimidinyl-thiobenzoates (PTB), sulfonyl-aminocarbonyl-triazolinone (SCT), and imidazolinones (IMI) classes. No differences in absorption, translocation, or metabolism of [14C]TM between R and S plants were observed, suggesting that these non-target mechanisms were not responsible for the resistance. The ALS gene of the R populations contained the Trp-574-Leu mutation, conferring cross-resistance to the SU, SCT, PTB, TP, and IMI classes. The Trp-574-Leu mutation in the ALS gene conferred cross-resistance to ALS-inhibiting herbicides in S. arvensis from winter wheat fields in Golestan province. This is the first TM resistance case confirmed in this species in Iran.

Acetolactate Synthase Resistance in a Common Waterhemp (Amaranthus rudis) Population

1997 ◽  
Vol 11 (1) ◽  
pp. 13-18 ◽  
Author(s):  
John R. R. Hinz ◽  
Micheal D. K. Owen
Keyword(s):  
Plant Material ◽  
Resistance Mechanism ◽  
Acetolactate Synthase ◽  
Grain Amaranth ◽  
Common Waterhemp ◽  
Resistant Species ◽  
Whole Plant ◽  
Amaranthus Rudis ◽  
Inhibitor Resistance ◽  
Als Inhibitor

Research was initiated to determine (a) whether a common waterhemp population was resistant to acetolactate synthase (ALS) inhibiting herbicides, (b) the percentage of the population that was ALS-inhibitor resistant, (c) the resistance mechanism, and (d) the effectiveness of a whole plant assay to detect ALS-inhibitor resistance. ALS-inhibitor resistance was confirmed in a common waterhemp population near Davis City, IA. The Davis City common waterhemp population was cross resistant to both imidazolinone and sulfonylurea herbicides, but not to lactofen. Approximately 10% of the Davis City common waterhemp population was sensitive to a rate of imazaquin 4 times the normal field rate. Davis City common waterhemp isolated ALS was much less sensitive to imazaquin and primisulfuron inhibition than was grain amaranth or an ALS-sensitive common waterhemp isolated ALS. Imazaquin I50values were 366.4 and 3.4 μM for ALS isolated from Davis City common waterhemp and grain amaranth, respectively. Primisulfuron I50values were 3.6 and 0.007 μM for ALS isolated from Davis City common waterhemp and grain amaranth, respectively. A whole plant ALS assay was developed that allowed for much more rapid detection of an ALS-resistant species and used less plant material than a conventional ALS assay.

Multiple Pro197ALS Substitutions Endow Resistance to ALS Inhibitors within and among Mayweed Chamomile Populations

Weed Science ◽  
2011 ◽  
Vol 59 (3) ◽  
pp. 431-437 ◽  
Author(s):  
Suphannika Intanon ◽  
Alejandro Perez-Jones ◽  
Andrew G. Hulting ◽  
Carol A. Mallory-Smith
Keyword(s):  
Pacific Northwest ◽  
Genotypic Variation ◽  
Point Mutations ◽  
Acetolactate Synthase ◽  
Cross Resistance ◽  
Collection Site ◽  
Whole Plant ◽  
The Pacific ◽  
Als Inhibitors

Mayweed chamomile seeds were collected from six different fields across the Pacific Northwest. All populations (each collection site was considered a population) were suspected to have some level of acetolactate synthase (ALS) resistance. Greenhouse and laboratory studies were conducted to determine if these populations were resistant to three different classes of ALS inhibitors: sulfonylureas (SU), imidazolinones (IMI), and triazolopyrimidines (TP). A whole-plant dose–response andin vitroALS activity studies confirmed cross-resistance to thifensulfuron + tribenuron/chlorsulfuron (SU), imazethapyr (IMI), and cloransulam (TP); however, resistance varied by herbicide class and population. TwoALSisoforms of theALSgene (ALS1andALS2) were identified in mayweed chamomile; however, only mutations inALS1were responsible for resistance. No mutations were found inALS2. Sequence analysis of the partialALSgene identified four point mutations at position 197 (Pro197to Leu, Gln, Thr, or Ser) in the resistant populations. This study demonstrates genotypic variation associated with cross-resistance to ALS inhibitors within and between populations.

scholarly journals Point Mutations as Main Resistance Mechanism Together With P450-Based Metabolism Confer Broad Resistance to Different ALS-Inhibiting Herbicides in Glebionis coronaria From Tunisia

2021 ◽  
Vol 12 ◽  
Author(s):  
Zeineb Hada ◽  
Yosra Menchari ◽  
Antonia M. Rojano-Delgado ◽  
Joel Torra ◽  
Julio Menéndez ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Dose Response ◽  
Resistance Mechanism ◽  
Point Mutations ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Cross Resistance ◽  
P450 Monooxygenase ◽  
Target Site Resistance ◽  
Sites Of Action

Resistance to acetolactate synthase (ALS) inhibiting herbicides has recently been reported in Glebionis coronaria from wheat fields in northern Tunisia, where the weed is widespread. However, potential resistance mechanisms conferring resistance in these populations are unknown. The aim of this research was to study target-site resistance (TSR) and non-target-site resistance (NTSR) mechanisms present in two putative resistant (R) populations. Dose–response experiments, ALS enzyme activity assays, ALS gene sequencing, absorption and translocation experiments with radiolabeled herbicides, and metabolism experiments were carried out for this purpose. Whole plant trials confirmed high resistance levels to tribenuron and cross-resistance to florasulam and imazamox. ALS enzyme activity further confirmed cross-resistance to these three herbicides and also to bispyribac, but not to flucarbazone. Sequence analysis revealed the presence of amino acid substitutions in positions 197, 376, and 574 of the target enzyme. Among the NTSR mechanisms investigated, absorption or translocation did not contribute to resistance, while evidences of the presence of enhanced metabolism were provided. A pretreatment with the cytochrome P450 monooxygenase (P450) inhibitor malathion partially synergized with imazamox in post-emergence but not with tribenuron in dose–response experiments. Additionally, an imazamox hydroxyl metabolite was detected in both R populations in metabolism experiments, which disappeared with the pretreatment with malathion. This study confirms the evolution of cross-resistance to ALS inhibiting herbicides in G. coronaria from Tunisia through TSR and NTSR mechanisms. The presence of enhanced metabolism involving P450 is threatening the chemical management of this weed in Tunisian wheat fields, since it might confer cross-resistance to other sites of action.

scholarly journals The occurrence of herbicide-resistant Avena fatua (wild oats) populations to ACCase-inhibiting herbicides in Ireland

2021 ◽  
Author(s):  
R. Byrne ◽  
A.V. Vijaya Bhaskar ◽  
J. Spink ◽  
R. Freckleton ◽  
P. Neve ◽  
...  
Keyword(s):  
Herbicide Resistance ◽  
Weed Management ◽  
Resistance Mechanism ◽  
Point Mutations ◽  
Acetolactate Synthase ◽  
Avena Fatua ◽  
Integrated Weed Management ◽  
Cross Resistance ◽  
Wild Oats ◽  
Als Inhibitor

Following growers’ reports of herbicide control problems, populations of 30 wild oats, Avena fatua, were collected from the south-east main arable counties of Ireland in 2016 and investigated for the occurrence and potential for herbicide resistance to acetyl-CoA carboxylase (ACCase) inhibitors pinoxaden, propaquizafop and cycloxydim, as well as acetolactate synthase (ALS) inhibitor mesosulfuron + iodosulfuron. Plant survival ≥20% was considered as the discriminating threshold between resistant and susceptible populations, when plants were treated with full recommended field rates of ACCase/ALS inhibitors. Glasshouse sensitivity screens revealed 2 out of 30 populations were cross-resistant to all three ACCase inhibitors. While three populations were cross-resistant to both pinoxaden and propaquizafop, and additionally, two populations were resistant to propaquizafop only. Different degree of resistance and cross-resistance between resistant populations suggest the involvement of either different point mutations or more than one resistance mechanism. Nevertheless, all populations including the seven ACCase-resistant populations were equally susceptible to ALS inhibitor. An integrated weed management (cultural/non-chemical control tactics and judicious use of herbicides) approach is strongly recommended to minimize the risk of herbicide resistance evolution.

Multiple herbicide resistance in California Italian ryegrass (Lolium perenne ssp. multiflorum): characterization of ALS-inhibiting herbicide resistance

Weed Science ◽  
2019 ◽  
Vol 67 (3) ◽  
pp. 273-280 ◽  
Author(s):  
Parsa Tehranchian ◽  
Vijay K. Nandula ◽  
Maor Matzrafi ◽  
Marie Jasieniuk
Keyword(s):  
Lolium Perenne ◽  
Herbicide Resistance ◽  
Resistance Mechanism ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Italian Ryegrass ◽  
Resistance Level ◽  
Als Inhibitors ◽  
Inhibitor Resistance ◽  
Als Inhibitor

AbstractMultiple resistance to glyphosate, sethoxydim, and paraquat was previously confirmed in two Italian ryegrass [Lolium perenne L. ssp. multiflorum (Lam.) Husnot] populations, MR1 and MR2, in northern California. Preliminary greenhouse studies revealed that both populations were also resistant to imazamox and mesosulfuron, both of which are acetolactate synthase (ALS)-inhibiting herbicides. In this study, three subpopulations, MR1-A (from seed of MR1 plants that survived a 16X rate of sethoxydim), MR1-P (from seed of MR1 plants that survived a 2X rate of paraquat), and MR2 (from seed of MR2 plants that survived a 16X rate of sethoxydim), were investigated to determine the resistance level to imazamox and mesosulfuron, evaluate other herbicide options for the control of these multiple resistant L. perenne ssp. multiflorum, and characterize the underlying ALS-inhibitor resistance mechanism(s). Based on LD50 values, the MR1-A, MR1-P, and MR2 subpopulations were 38-, 29-, 8-fold and 36-, 64-, and 3-fold less sensitive to imazamox and mesosulfuron, respectively, relative to the susceptible (Sus) population. Only MR1-P and MR2 plants were cross-resistant to rimsulfuron, whereas both MR1 subpopulations were cross-resistant to imazethapyr. Pinoxaden (ACCase inhibitor [phenylpyrazoline 'DEN']) only controlled MR2 and Sus plants at the labeled field rate. However, all plants were effectively controlled (>99%) with the labeled field rate of glufosinate. Based on I50 values, MR1-A, MR-P, and MR2 plants were 712-, 1,104-, and 3-fold and 10-, 18-, and 5-fold less responsive to mesosulfuron and imazamox, respectively, than the Sus plants. Sequence alignment of the ALS gene of resistant plants revealed a missense single-nucleotide polymorphism resulting in a Trp-574-Leu substitution in MR1-A and MR1-P plants, heterozygous in both, but not in the MR2 plants. An additional homozygous substitution, Asp-376-Glu, was identified in the MR1-A plants. Addition of malathion or piperonyl butoxide did not alter the efficacy of mesosulfuron on MR2 plants. In addition, the presence of 2,4-D had no effect on the response of mesosulfuron on the MR2 and Sus. These results suggest an altered target site is the mechanism of resistance to ALS inhibitors in MR1-A and MR1-P plants, whereas a non–target site based resistance apparatus is present in the MR2 plants.

scholarly journals A complex suite of loci and elements in eukaryotic type II topoisomerases determine selective sensitivity to distinct poisoning agents

2019 ◽  
Vol 47 (15) ◽  
pp. 8163-8179 ◽  
Author(s):  
Tim R Blower ◽  
Afif Bandak ◽  
Amy S Y Lee ◽  
Caroline A Austin ◽  
John L Nitiss ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Amino Acid ◽  
Drug Targets ◽  
Topoisomerase Ii ◽  
Point Mutations ◽  
Amino Acid Position ◽  
Drug Binding ◽  
Type Ii ◽  
Resistance Mutations ◽  
Selective Sensitivity

AbstractType II topoisomerases catalyze essential DNA transactions and are proven drug targets. Drug discrimination by prokaryotic and eukaryotic topoisomerases is vital to therapeutic utility, but is poorly understood. We developed a next-generation sequencing (NGS) approach to identify drug-resistance mutations in eukaryotic topoisomerases. We show that alterations conferring resistance to poisons of human and yeast topoisomerase II derive from a rich mutational ‘landscape’ of amino acid substitutions broadly distributed throughout the entire enzyme. Both general and discriminatory drug-resistant behaviors are found to arise from different point mutations found at the same amino acid position and to occur far outside known drug-binding sites. Studies of selected resistant enzymes confirm the NGS data and further show that the anti-cancer quinolone vosaroxin acts solely as an intercalating poison, and that the antibacterial ciprofloxacin can poison yeast topoisomerase II. The innate drug-sensitivity of the DNA binding and cleavage region of human and yeast topoisomerases (particularly hTOP2β) is additionally revealed to be significantly regulated by the enzymes’ adenosine triphosphatase regions. Collectively, these studies highlight the utility of using NGS-based methods to rapidly map drug resistance landscapes and reveal that the nucleotide turnover elements of type II topoisomerases impact drug specificity.

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