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6 results for “Acetolactate synthase”
Figure 1 in Characterization of Acetolactate Synthase (ALS)-Inhibitor Resistance in Pennsylvania smartweed (PersicOriO pensylvOnicO)
Figure 1. Dose–response assay using four-parameter log logistic model for (A) bensulfuron-methyl, (B) imazethapyr, and (C) bispyribac-sodium herbicides in Persicaria pensylvanica resistant (R) and susceptible (S) biotypes. Each data point is a mean response of 30 plants (10 plants per replication).
Figure 2 in Characterization of Acetolactate Synthase (ALS)-Inhibitor Resistance in Pennsylvania smartweed (PersicOriO pensylvOnicO)
Figure 2. Two ALS gene mutations conferring ALS-inhibitor resistance in Persicaria pensylvanica. The underlined nucleotides (TCA and TCC) code for the amino acid serine instead of an alanine and proline at two different locations (122 and 197) of the ALS gene. R1, R2, and S refer to two resistant and one susceptible individuals, respectively.
Data from: Identification and evaluation of novel acetolactate synthase inhibitors as antifungal agents
High-throughput phenotypic screening against yeast Saccharomyces cerevisiae revealed a series of triazolo-pyrimidine-sulfonamide compounds with broad-spectrum antifungal activity, no significant cytotoxicity, and low protein binding. To elucidate the target of this series we have applied a chemogenomic profiling approach using the S. cerevisiae deletion collection. All compounds of the series yielded highly similar profiles that suggested acetolactate synthase (Ilv2p, catalyzes the first common step in branched chain amino acid biosynthesis) as a possible target. High correlation to profiles of known Ilv2p inhibitors like chlorimuron-ethyl provided further evidence for a similar mechanism of action. Genome-wide mutagenesis in S. cerevisiae identified 13 resistant clones with 3 different mutations in the catalytic subunit of acetolactate synthase that also conferred cross-resistance to established Ilv2p inhibitors. Mapping the mutations into the published Ilv2p crystal structure outlined the chlorimuron-ethyl binding cavity and it was possible to dock the triazolo-pyrimidine-sulfonamide compound into this pocket in silico. However, fungal growth inhibition could be bypassed through supplementation with exogenous branched chain amino acids, or by the addition of serum to the medium in all of the fungal organisms tested except for Aspergillus fumigatus. Thus, these data support the identification of triazolo-pyrimidine-sulfonamide as inhibitors of acetolactate synthase but suggest that targeting may be compromised due to the possibility of nutrient bypass in vivo.
Data from: Identification and evaluation of novel acetolactate synthase inhibitors as antifungal agents
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The Staphylococcus aureus α-Acetolactate Synthase ALS Confers Resistance to Nitrosative Stress
GEO Series GSE99563. Staphylococcus aureus subsp. aureus USA300_FPR3757. 4 samples. Type: Expression profiling by high throughput sequencing.
Transcriptome changes in chlorsulfuron-treated plants are caused by acetolactate synthase inhibition and not induction of a herbicide detoxification system in Marchantia polymorpha
GEO Series GSE212280. Marchantia polymorpha. 86 samples. Type: Expression profiling by high throughput sequencing.
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