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SILKY WINDGRASS
(
Apera spica-venti
)
with
GROUP B/2 resistance: (INHIBITION OF ACETOLACTATE SYNTHASE )
Inhibition of Acetolactate Synthase
MUTATION: PROLINE 197 to ASPARAGINE
Silky Windgrass
(
Apera spica-venti
) is a monocot plant in the poaceae family. A single amino acid substitution from Proline 197 to Asparagine has led to resistance to Inhibition of Acetolactate Synthase as indicated in the table below.
Silky Windgrass
Chemical Family
Example Herbicide
Resistance Level
Imidazolinones
Imazethapyr
Not Determined
Pyrimidinyl benzoates
Bispyribac-Na
Not Determined
Sulfonylureas
Chlorsulfuron
Resistant > 10 fold
Triazolopyrimidine - Type 1
Chloransulam-methyl
Intermediate Resistance < 10 fold
Triazolinones
Flucarbazone-Na
Intermediate Resistance < 10 fold
REFERENCES
Massa, D., B. Krenz, And R. Gerhards
.
2011
.
Target-site resistance to ALS-inhibiting herbicides in Apera spica-venti populations is conferred by documented and previously unknown mutations
.
Weed Research
51
:
294 - 303
.
In this study, whole-plant bioassays were performed on 72 Apera spica-venti populations that have survived application of acetolactate synthase (ALS)-inhibiting herbicides in recent years. Molecular genetic analysis of the ALS gene revealed a Thr mutation at Pro197 within 67 populations. Sequencing of the whole ALS gene from wild-type and resistant plants not carrying the above-mentioned mutation revealed the presence of a Leu mutation at Trp574 within two populations and an Asn mutation at Pro197 within two populations. As the Pro197-Asn amino acid substitution is reported for the first time in a field-selected weed population, a Cleaved Amplified Polymorphic Sequences (CAPS) marker was developed for its quick detection. In addition, one novel mutation was found within a population that coded for a His substitution at Arg377. Enzyme assays confirmed a significant reduction in inhibition of ALS activity compared with the wild type. This population showed resistance to sulfonylureas (SUs) and cross-resistance to sulfonylaminocarbonyltriazolinones (SCTs) and triazolopyrimidines (TPs) within the whole-plant bioassays. ALS protein sequence alignments from weedy and cultural plants revealed that the Arg377 is highly conserved among known wild-type enzymes. In agreement with existing literature concerning the structure and mechanisms of inhibition of plant ALS, this mutation is probably involved in target-site resistance to ALS inhibitors. Our results suggest that further single-nucleotide polymorphisms impairing proper herbicide performance might be selected within field populations in the near future, making the short- and long-range evolution of target-site resistance difficult to predict depending solely on herbicide use history
.
This case was entered by Patrick Tranel Email:
tranel@illinois.edu
PERMISSION MUST BE OBTAINED FIRST if you intend to base a significant portion of a scientific paper on data derived from this site.
Cite this site as:
Heap, I. The International Survey of Herbicide Resistant Weeds. Online. Internet.
Saturday, December 7, 2024
. Available
www.weedscience.org
Copyright © 1993-
2024
WeedScience.org All rights reserved. Fair use of this material is encouraged. Proper citation is requested.
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