Skip to main content
Log in

The molecular bases for resistance to acetyl co-enzyme A carboxylase (ACCase) inhibiting herbicides in two target-based resistant biotypes of annual ryegrass (Lolium rigidum)

Planta Aims and scope Submit manuscript

Abstract

Acetyl-CoA carboxylase (ACCase) (EC.6.4.1.2) is an essential enzyme in fatty acid biosynthesis and, in world agriculture, commercial herbicides target this enzyme in plant species. In nearly all grass species the plastidic ACCase is strongly inhibited by commercial ACCase inhibiting herbicides [aryloxyphenoxypropionate (APP) and cyclohexanedione (CHD) herbicide chemicals]. Many ACCase herbicide resistant biotypes (populations) of L. rigidum have evolved, especially in Australia. In many cases, resistance to ACCase inhibiting herbicides is due to a resistant ACCase enzyme. Two ACCase herbicide resistant L. rigidum biotypes were studied to identify the molecular basis of ACCase inhibiting herbicide resistance. The carboxyl-transferase (CT) domain of the plastidic ACCase gene was amplified by PCR and sequenced. Amino acid substitutions in the CT domain were identified by comparison of sequences from resistant and susceptible plants. The amino acid residues Gln-102 (CAG codon) and Ile-127 (ATA codon) were substituted with a Glu residue (GAG codon) and Leu residue (TTA codon), respectively, in both resistant biotypes. Amino acid positions 102 and 127 within the fragment sequenced from L. rigidum corresponded to amino acid residues 1756 and 1781, respectively, in the A. myosuroides full ACCase sequence. Allele-specific PCR results further confirmed the mutations linked with resistance in these populations. The Ile-to-Leu substitution at position 1781 has been identified in other resistant grass species as endowing resistance to APP and CHD herbicides. The Gln-to-Glu substitution at position 1756 has not previously been reported and its role in herbicide resistance remains to be established.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

ACCase:

Acetyl-CoA carboxylase

CT:

Carboxyl-transferase

APP:

Aryloxyphenoxypropionate

CHD:

Cyclohexanedione

SNPs:

Single nucleotide polymorphisms

References

  • Brown AC, Moss SR, Wilson ZA, Field LM (2002) An isoleucine to leucine substitution in the ACCase of Alopecurus myosuroides (black-grass) is associated with resistance to the herbicide sethoxydim. Pestic Biochem Physiol 72:160–168

    Article  CAS  Google Scholar 

  • Burton JD, Gronwald JW, Keith RA, Somers DA, Gegenbach BG, Wyse DL (1991) Kinetics of inhibition of acetyl-coenzyme A carboxylase by sethoxydim and haloxyfop. Pestic Biochem Physiol 39:100–109

    Article  CAS  Google Scholar 

  • Christoffers MJ, Berg ML, Messersmith CG (2002) An isoleucine to leucine mutation in acetyl-CoA carboxylase confers herbicide resistance in wild oat. Genome 45:1049–1056

    Article  PubMed  CAS  Google Scholar 

  • Délye C, Calmès É, Matéjicek A (2002a) SNP markers for black-grass (Alopecurus myosuroides Huds.) genotypes resistant to acetyl CoA-carboxylase inhibiting herbicides. Theor Appl Genet 104:1114–1120

    Article  CAS  Google Scholar 

  • Délye C, Matéjicek A, Gasquez J (2002b) PCR-based detection of resistance to acetyl-CoA carboxylase-inhibiting herbicides in black-grass (Alopecurus myosuroides Huds) and ryegrass (Lolium rigidum Gaud). Pest Manag Sci 58:474–478

    Article  CAS  Google Scholar 

  • Délye C, Wang T, Darmency H (2002c) An isoleucine-leucine substitution in chloroplastic acetyl-Co A carboxylase from green foxtail (Setaria viridis L. Beauv.) is responsible for resistance to the cyclohexanedione herbicide sethoxydim. Planta 214:421–427

    Article  CAS  Google Scholar 

  • Délye C, Zhang X-Q, Chalopin C, Michel S, Powles SB (2003) An isoleucine residue within the carboxyl-transferase domain of multidomain acetyl-CoA carboxylase is a major determinant of sensitivity to aryloxyphenoxypropionate but not to cyclohexanedione inhibitors. Plant Physiol 132:1716–1723

    Article  PubMed  CAS  Google Scholar 

  • Délye C, Zhang X-Q, Michel S, Matejicek A, Powles SB (2005) Molecular bases for sensitivity to acetyl-coenzyme A carboxylase inhibitors in black-grass. Plant Physiol 137:794–806

    Article  PubMed  CAS  Google Scholar 

  • Devine MD (1997) Mechanisms of resistance to acetyl-coenzyme A carboxylase inhibitors: a review. Pestic Sci 51:259–264

    Article  CAS  Google Scholar 

  • Devine MD, Preston C (2000) The molecular basis of herbicide resistance. In: Cobb AH, Kirkwood RC (eds) Herbicides and their mechanisms of action. Sheffield Academic Press, UK, pp 72–104

    Google Scholar 

  • Devine MD, Shimabukuro RH (1994) Resistance to acetyl coenzyme A carboxylase inhibiting herbicides. In: Powles SB, Holtum JAM (eds) Herbicide resistance in plants: biology and biochemistry. Lewis Publishers, Boca Raton, pp 141–169

    Google Scholar 

  • Devine MD, Shukla A (2000) Altered target sites as mechanism of herbicide resistance. Crop Prot 19:881–889

    Article  CAS  Google Scholar 

  • Harwood JL (1988) Fatty acid metabolism. Annu Rev Plant Physiol 39:101–138

    Article  CAS  Google Scholar 

  • Konishi T, Sasaki Y (1994) Compartimentalization of two forms of acetyl-CoA carboxylase in plants and the origin of their tolerance towards herbicides. Proc Natl Acad Sci USA 91:3598–3601

    Article  PubMed  CAS  Google Scholar 

  • Konishi T, Shinohara K, Yamada K, Sasaki Y (1996) Acetyl-CoA carboxylase in higher plants: most plants other than gramineae have both the prokaryotic and the eukaryotic forms of this enzyme. Plant Cell Physiol 37:117–122

    PubMed  CAS  Google Scholar 

  • Nikolskaya T, Zagnikto O, Tevzadze G, Haselkorn R, Gornicki P (1999) Herbicide sensitivity determinant of wheat plastid acetyl-CoA carboxylase is located in a 400-amino acid fragment of the carboxyltransferase domain. Proc Natl Acad Sci USA 96:14647–14651

    Article  PubMed  CAS  Google Scholar 

  • Powles SB, Matthews JM (1992) Multiple herbicide resistance in annual ryegrass (Lolium rigidum): a driving force for the adoption of integrated weed management strategies. In: Resistance 91: achievements and developments in combating pesticide resistance. Elsevier Press, Amsterdam, pp 75–87

  • Sasaki Y, Konishi T, Nagano Y (1995) The compartmentation of acetyl-coenzyme A carboxylase in plants. Plant Physiol 108:445–449

    PubMed  CAS  Google Scholar 

  • Sommer SS, Groszbar AR, Bottema CDK (1992) PCR amplification of specific alleles (PASA) is a general method for rapid detecting known single base-pair changes. Biotechniques 12:82–87

    PubMed  CAS  Google Scholar 

  • Tardif FJ, Powles SB (1994) Herbicide multiple-resistance in a Lolium rigidum biotype is endowed by multiple mechanisms: isolation of a subset with resistant acetyl-CoA carboxylase. Physiologia Plantarum 91:488–494

    Article  CAS  Google Scholar 

  • Tardif FJ, Holtum JAM, Powles SB (1993) Occurrence of a herbicide-resistant acetyl-coenzyme A carboxylase mutant in annual ryegrass (Lolium rigidum) selected by sethoxydim. Planta 190:176–181

    Article  CAS  Google Scholar 

  • Zagnitko O, Jelenska J, Tevzadze G, Haselkorn R, Gornicki P (2001) An isoleucine/leucine residue in the carboxyltransferase domain of acetyl-CoA carboxylase is critical for interaction with aryloxyphenoxypropionate and cyclohexanedione inhibitors. Proc Natl Acad Sci USA 98:6617–6622

    Article  PubMed  CAS  Google Scholar 

  • Zhang X-Q, Devine MD (2000) A possible point mutation of plastidic ACCase gene conferring resistance to sethoxydim in green foxtail (Setaria viridis). Weed Sci Soc Am Abstr 40:81

    CAS  Google Scholar 

Download references

Acknowledgements

WAHRI is funded by the Grains Research and Development Corporation. Thanks to Mechelle Owen for technical assistance with growing plants.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Stephen B Powles.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Zhang, XQ., Powles, S.B. The molecular bases for resistance to acetyl co-enzyme A carboxylase (ACCase) inhibiting herbicides in two target-based resistant biotypes of annual ryegrass (Lolium rigidum). Planta 223, 550–557 (2006). https://doi.org/10.1007/s00425-005-0095-x

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s00425-005-0095-x

Keywords

Navigation