Amino acid substitution (Gly‐654‐Tyr) in acetolactate synthase (ALS) confers broad spectrum resistance to ALS‐inhibiting herbicides. Issue 2 (8th October 2021)
- Record Type:
- Journal Article
- Title:
- Amino acid substitution (Gly‐654‐Tyr) in acetolactate synthase (ALS) confers broad spectrum resistance to ALS‐inhibiting herbicides. Issue 2 (8th October 2021)
- Main Title:
- Amino acid substitution (Gly‐654‐Tyr) in acetolactate synthase (ALS) confers broad spectrum resistance to ALS‐inhibiting herbicides
- Authors:
- Cao, Yi
Zhou, Xinxin
Huang, Zhaofeng - Abstract:
- Abstract: BACKGROUND: Amaranthus retroflexus L. is a problematic weed in agricultural fields. In China, the repeated use of acetolactate synthase (ALS) inhibiting herbicides has led to the evolution of many A. retroflexus resistant populations. The objective of this research was to investigate the physiological and molecular basis for resistance to ALS‐inhibiting herbicides in A. retroflexus . RESULTS: Sequence analysis of the ALS revealed a Trp to Leu substitution at amino acid position 574 (Trp‐574‐Leu), and a previously unreported substitution of Gly to Tyr substitution at 654 (Gly‐654‐Tyr) in the resistant A. retroflexus population. A purified R‐Tyr654 subpopulation homozygous for the Gly‐654‐Tyr mutation was generated and characterized in response to five different classes of ALS‐inhibiting herbicides. Dose–response analysis revealed that the R‐Tyr654 population was highly resistant to two imidazolinones (imazethapyr, >42‐fold; imazamox, 48.3‐fold), one triazolopyrimidine (flumetsulam, 57.4‐fold), and one sulfonylamino‐carbonyltriazolinone (flucarbazone, 17.3‐fold). Moreover, it was moderately resistant to two sulfonylureas (thifensulfuron‐methyl, 4.9‐fold; nicosulfuron, 9.1‐fold), and one pyrimidinylthio‐benzoate (bispyribac‐sodium, 3.1‐fold). An in vitro ALS activity assay showed that ALS with the Gly‐654‐Tyr substitution was resistant to all the tested ALS‐inhibiting herbicides. However, the field rate of herbicides binding other sites of action demonstratedAbstract: BACKGROUND: Amaranthus retroflexus L. is a problematic weed in agricultural fields. In China, the repeated use of acetolactate synthase (ALS) inhibiting herbicides has led to the evolution of many A. retroflexus resistant populations. The objective of this research was to investigate the physiological and molecular basis for resistance to ALS‐inhibiting herbicides in A. retroflexus . RESULTS: Sequence analysis of the ALS revealed a Trp to Leu substitution at amino acid position 574 (Trp‐574‐Leu), and a previously unreported substitution of Gly to Tyr substitution at 654 (Gly‐654‐Tyr) in the resistant A. retroflexus population. A purified R‐Tyr654 subpopulation homozygous for the Gly‐654‐Tyr mutation was generated and characterized in response to five different classes of ALS‐inhibiting herbicides. Dose–response analysis revealed that the R‐Tyr654 population was highly resistant to two imidazolinones (imazethapyr, >42‐fold; imazamox, 48.3‐fold), one triazolopyrimidine (flumetsulam, 57.4‐fold), and one sulfonylamino‐carbonyltriazolinone (flucarbazone, 17.3‐fold). Moreover, it was moderately resistant to two sulfonylureas (thifensulfuron‐methyl, 4.9‐fold; nicosulfuron, 9.1‐fold), and one pyrimidinylthio‐benzoate (bispyribac‐sodium, 3.1‐fold). An in vitro ALS activity assay showed that ALS with the Gly‐654‐Tyr substitution was resistant to all the tested ALS‐inhibiting herbicides. However, the field rate of herbicides binding other sites of action demonstrated effective control of the R‐Tyr654 population. CONCLUSION: These results indicate that the molecular basis of ALS‐inhibiting herbicide resistance in A. retroflexus was caused by the Trp‐574‐Leu and Gly‐654‐Tyr substitutions in the ALS. This is the first report of Gly‐654‐Tyr substitution in ALS, and this substitution confers broad spectrum resistance to ALS‐inhibiting herbicides. © 2021 Society of Chemical Industry. Abstract : This is the first report of Gly‐654‐Tyr substitution in ALS, and this substitution confers broad spectrum resistance to ALS‐inhibiting herbicides. … (more)
- Is Part Of:
- Pest management science. Volume 78:Issue 2(2022)
- Journal:
- Pest management science
- Issue:
- Volume 78:Issue 2(2022)
- Issue Display:
- Volume 78, Issue 2 (2022)
- Year:
- 2022
- Volume:
- 78
- Issue:
- 2
- Issue Sort Value:
- 2022-0078-0002-0000
- Page Start:
- 541
- Page End:
- 549
- Publication Date:
- 2021-10-08
- Subjects:
- Amaranthus retroflexus -- resistance -- acetolactate synthase -- herbicide -- target site mutation
Pests -- Control -- Periodicals
Pesticides -- Periodicals
632.9 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/ps.6658 ↗
- Languages:
- English
- ISSNs:
- 1526-498X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6428.332000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 20331.xml