Korean Journal of Weed Science (한국잡초학회지)

The Korean Society of Weed Science & The Turfgrass Society of Korea Archive (한국잡초학회 & 한국잔디학회)
권호 표지

Resistance Mechanisms to the Herbicides Inhibiting Acetolactate Synthase

Acetolactate Synthase 저해 제초제에 대한 식물체내 저항성 발현 기작

Hwang, In-Taek
황인택

  • Published : 20030000
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Abstract

Most cases of resistance to herbicides have occurred in fields in which these herbicides have been used continuously for 3 to 20 years with no use of other herbicides having a different mechanism of action. Recent phenomena of herbicide-resistance are target site cross-resistance, non-target site cross-resistance, multiple-resistance, and back cross-resistance. Also, herbicide resistance has been identified at least four different resistance mechanisms which were target-site mutation, target-site over-expression, metabolism-based resistance, and reduced activation of pro-herbicides. Biochemical and physiological effect of target site resistance to herbicides inhibiting acetolactate synthase (ALS) have been studied in several field-evolved weed species and in a number of laboratory-derived mutants. In all of the populations where the mechanism of resistance has been determined, the resistance is due to the selection of an altered ALS enzyme that is no longer sensitive to the herbicides. The patterns of cross-resistance among the ALS inhibitors are variable. The considerable variation in the level of resistance across and within various ALS-inhibiting herbicide chemistries is likely to be due to different binding by particular herbicides on the ALS and different mutations of ALS. Research on the genetics of ALS resistance shows that there are at lease 10 different sites within conserved regions of the ALS gene where mutations result in a resistant enzyme. However, it appears that most of the mutations occur in one of four sites. Cross-resistance studies have shown that substitutions of Pro197 to one of amino acids among Ser, Gln, Ala, His, and Leu result primarily in resistance to sulfonylureas (SUs) and triazolopyrimidines (TPs). Secondly, substitution of Ala155 to Asp showed high resistant to SUs but have no cross-resistance to other ALS inhibitors. Thirdly, Substitution of Ser653 to Asn showed high resistant to imidazolinones (IMs) but susceptible to SUs and TPs. Lastly, substitution of Trp591 to Leu becomes a broad cross-resistance to all family of ALS inhibitors. In greenhouse studies, the SUs-resistant Monochoria vaginalis population occurred in Chonnam province of Korea showed index of 21.2 and 42.4 to pyrazosulfuron-ethyl (PYR) and bensulfuron-methyl (BEN), respectively. The resistant type of M. vaginalis showed high levels of cross-resistance to PYR, BEN, cyclosulfamuron (CYC), and flumetsulam (FLU), but not to imazaquin. The resistant type of M. vaginalis did not show multiple resistance to other herbicides having different modes of action. In vitro acetolactate synthase (ALS) assay showed that the pI50 values of BEN to the wild and resistant type of M. vaginalis were 9.3 and 7.1, respectively. Also, the pI50 values of FLU to the wild and resistant type of M. vaginalis were 7.7 and 6.0 but those of IMA were 8.3 and 8.2, respectively. Acetolactate accumulation in the resistant type of M. vaginalis plants treated with BEN or FLU followed by 1,1-cyclopropane dicarboxylic acid were significantly higher than that of wild type. However, the accumulation of acetolactate in the plants treated with IMA was not significantly different in the wild and the resistant type of M. vaginalis. In vitro and in vivo assay results showed that the resistance mechanism of M. vaginalis to ALS inhibitors might be due to the altered acetolactate synthase.

Keywords

References

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