1991Pesticide ScienceRequires access

Inhibition of acetolactate synthase in susceptible and resistant biotypes of Stellaria media

Malcolm D. Devine, M. A. Susan Maries, Linda M. Hall

Open publisher page 51 citations

Abstract

Abstract Acetolactate synthase (ALS) from one susceptible and two chlorsulfuronresistant biotypes of Stellaria media(L.) Vill. was assayed in the presence of eight known ALS inhibitors. As expected, ALS from the chlorsulfuronresistant biotypes (R1 and R2) showed reduced sensitivity to chlorsulfuron and other sulfonylurea herbicides. The patterns of cross‐resistance varied, however, indicating that the alteration in ALS that confers chlorsulfuron resistance does not confer the same level of resistance to other sulfonylurea herbicides. The resistant biotypes were highly cross‐resistant to sulfometuron‐methyl and DPX‐A7H81, but less cross‐resistant to triasulfuron. Both R1 and R2 were highly cross‐resistant to DTPS (N‐[2,6‐dichlorophenyl]‐5,7‐dimethyl‐1,2,4‐iriazolo[1,5a]pyrimidine‐2‐siilfoiiamide), but only slightly cross‐resistant to imazamethahenz, an imidazolinone herbicide. The differences in the patterns of cross‐resistance observed presumably reflect differences in the binding affinity of the herbicides for the altered ALS. The data presented suggest, but do not confirm, that R1 and R2 contain the same ALS mutation.

About this research paper

What this paper is about

Abstract Acetolactate synthase (ALS) from one susceptible and two chlorsulfuronresistant biotypes of Stellaria media(L.) Vill. was assayed in the presence of eight known ALS inhibitors. As expected, ALS from the chlorsulfuronresistant biotypes (R1 and R2) showed reduced sensitivity to chlorsulfuron and other sulfonylurea herbicides. The patterns of cross‐resistance varied, however, indicating that the alteration in ALS that confers chlorsulfuron resistance does not confer the same level of resistance to other sulfonylurea herbicides. The resistant biotypes were highly cross‐resistant to sulfometuron‐methyl and DPX‐A7H81, but less cross‐resistant to triasulfuron. Both R1 and R2 were highly cross‐resistant to DTPS (N‐[2,6‐dichlorophenyl]‐5,7‐dimethyl‐1,2,4‐iriazolo[1,5a]pyrimidine‐2‐siilfoiiamide), but only slightly cross‐resistant to imazamethahenz, an imidazolinone herbicide. The differences in the patterns of cross‐resistance observed presumably reflect differences in the binding affinity of the herbicides for the altered ALS. The data presented suggest, but do not confirm, that R1 and R2 contain the same ALS mutation.

Why it matters

OpenAlex reports 51 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Abstract Acetolactate synthase (ALS) from one susceptible and two chlorsulfuronresistant biotypes of Stellaria media(L.) Vill. was assayed in the presence of eight known ALS inhibitors. As expected, ALS from the chlorsulfuronresistant biotypes (R1 and R2) showed reduced sensitivity to chlorsulfuron and other sulfonylurea herbicides. The patterns of cross‐resistance varied, however, indicating that the alteration in ALS that confers chlorsulfuron resistance does not confer the same level of resistance to other sulfonylurea herbicides. The resistant biotypes were highly cross‐resistant to sulfometuron‐methyl and DPX‐A7H81, but less cross‐resistant to triasulfuron. Both R1 and R2 were highly cross‐resistant to DTPS (N‐[2,6‐dichlorophenyl]‐5,7‐dimethyl‐1,2,4‐iriazolo[1,5a]pyrimidine‐2‐siilfoiiamide), but only slightly cross‐resistant to imazamethahenz, an imidazolinone herbicide. The differences in the patterns of cross‐resistance observed presumably reflect differences in the binding affinity of the herbicides for the altered ALS. The data presented suggest, but do not confirm, that R1 and R2 contain the same ALS mutation.

Key concepts: Acetolactate synthase, Sulfonylurea, Cross-resistance, Stellaria media, Biology, Enzyme, Biochemistry, Chemistry

Related papers

Back to paper searchBrowse research topicsOriginal source
Inhibition of acetolactate synthase in susceptible and resistant biotypes of Stellaria media — Research Paper | ScholarLens