INTERNATIONAL HERBICIDE-RESISTANT WEED DATABASE
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GROUP B/2 resistance: (ALS INHIBITORS)
Inhibition of acetolactate synthase ALS (acetohydroxyacid synthase AHAS)
MUTATION: TRYPTOPHAN 574 to GLYCINE
) is a dicot plant in the rubiaceae family. A single amino acid substitution from Tryptophan 574 to Glycine has led to resistance to ALS inhibitors as indicated in the table below.
Resistant > 10 fold
Two additional ALS amino acid substitutions were identified in the R biotype, so it is not certain if the Trp574Gly substitution confers resistance and/or if one of the other substitutions plays a role.
Sun Jian ; Wang JinXin ; Zhang HongJun ; Liu JunLiang ; Bian ShengNan
Study on mutations in ALS for resistance to tribenuron-methyl in
Agricultural Sciences in China
86 - 91
In recent years,
L. has not been controlled by tribenuron-methyl in major Chinese winter wheat fields. The objective of this study is to understand the molecular basis of the resistance mechanism to tribenuron-methyl in
and to find the specific mutation sites in amino acid sequence of acetolactate synthase (ALS) in the resistant biotype of
. Fragments that encode the ALS were amplified and cloned from susceptible (S) and resistant (R) biotypes of
to tribenuron-methyl and sequenced subsequently. The result showed that the nucleotide sequence of R-biotype of
differed from that of the S biotype with three amino acid substitutions, of which, the amino acid substitution of Trp
(TGG) to Gly (GGG) is located in the highly conserved region Domain B. The substitution of Trp
might be responsible for the resistance to tribenuron-methyl in the R-biotype of
This case was entered by Patrick Tranel Email:
PERMISSION MUST BE OBTAINED FIRST if you intend to base a significant portion of a scientific paper on data derived from this site. Citation:
Heap, I. The International Herbicide-Resistant Weed Database. Online.
Wednesday, April 1, 2020
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