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.
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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
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
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
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
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
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
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
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
Devine MD (1997) Mechanisms of resistance to acetyl-coenzyme A carboxylase inhibitors: a review. Pestic Sci 51:259–264
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
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
Devine MD, Shukla A (2000) Altered target sites as mechanism of herbicide resistance. Crop Prot 19:881–889
Harwood JL (1988) Fatty acid metabolism. Annu Rev Plant Physiol 39:101–138
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
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
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
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
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
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
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
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
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
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WAHRI is funded by the Grains Research and Development Corporation. Thanks to Mechelle Owen for technical assistance with growing plants.
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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
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DOI: https://doi.org/10.1007/s00425-005-0095-x