Diverse Mutations in the Acetolactate Synthase Gene Confer Chlorsulfuron Resistance in Kochia (Kochia scoparia) Biotypes

The DNA sequence of an 83-base pair region of the acetolactate synthase (ALS) gene was compared for 10 chlorsulfuron-resistant (R) and three chlorsulfuron-susceptible (S) kochia biotypes. Point mutation in the codon for the proline residue at position 173 in Domain A of the ALS protein was observed...

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Bibliographic Details
Published in:Weed science 1995-06, Vol.43 (2), p.175-178
Main Authors: Guttieri, Mary J., Eberlein, Charlotte V., Thill, Donald C.
Format: Article
Language:English
Subjects:
acetolactate synthase
Alleles
amino acid sequences
Amino acids
Bassia scoparia
biotypes
chlorsulfuron
Codons
DNA
genes
Genetic mutation
genetic resistance
genetic variation
Herbicide resistance
herbicide-resistant weeds
imazethapyr
mutation
Nucleotide sequences
Physiology, Chemistry and Biochemistry
Point mutation
Polymerase chain reaction
Sequencing
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Summary:The DNA sequence of an 83-base pair region of the acetolactate synthase (ALS) gene was compared for 10 chlorsulfuron-resistant (R) and three chlorsulfuron-susceptible (S) kochia biotypes. Point mutation in the codon for the proline residue at position 173 in Domain A of the ALS protein was observed in seven of 10 R biotypes. Among these seven R biotypes, mutation to threonine, serine, arginine, leucine, glutamine, and alanine was identified. The mechanism of resistance was determined for the R biotypes that did not have mutation in Domain A; all were resistant due to modified ALS, which indicated that at least one non-Domain A mutation site for resistance exists in kochia. Sequence results indicate that multiple mutations for resistance have occurred, and that geographically widespread ALS-inhibitor resistance in kochia is not the result of a single resistance allele.
ISSN:0043-1745
1550-2759
DOI:10.1017/s0043174500081029