小麦田麦家公对苯磺隆的抗性机理
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摘要
为明确麦田阔叶杂草麦家公Lithospermum arvense L.对苯磺隆的抗性机理,以苯磺隆抗性和敏感型麦家公为材料,比较分析这2个生物型麦家公靶标酶乙酰乳酸合成酶(acetolactate synthase,ALS)、解毒酶谷胱甘肽-S-转移酶(glutathione-S-transferase,GST)以及保护酶过氧化物酶(peroxidase,POD)、超氧化物歧化酶(superoxide dismutase,SOD)和过氧化氢酶(catalase,CAT)对苯磺隆的响应差异性。结果表明,抗性麦家公ALS对苯磺隆的敏感性较敏感型麦家公显著下降,苯磺隆的抑制中浓度分别为0.187、0.036μmol/L。苯磺隆胁迫后,抗性和敏感型麦家公ALS活性都出现下降,但抗性麦家公ALS活性可恢复,而敏感型麦家公ALS活性则不能恢复;2个生物型麦家公GST活性都能被苯磺隆诱导,但抗性麦家公GST累计活性为29.31 U,高于敏感型麦家公(25.90 U);抗性麦家公SOD累计活性为24.49 U,较敏感型麦家公(19.31 U)高,且具有较强的恢复能力;抗性麦家公POD和CAT累计活性分别为126.92～550.68 U和41.41～77.19 U,也高于敏感型麦家公的93.75～271.04 U、42.17～57.28 U。因此,靶标酶ALS对苯磺隆敏感性减弱是麦家公产生抗性的一个重要原因,解毒酶GST、SOD、POD和CAT活性升高可能与抗性有关。
To clarify the tribenuron-methyl-resistance mechanism in the broad-leaf weed Lithospermum arvense L. in wheat fields, the difference in the response of the target enzymes acetolactate synthase(ALS), metabolic enzyme glutathione-S-transferase(GST) and protective enzymes superoxide dismutase(SOD), peroxidase(POD), and catalase(CAT) to herbicides was analyzed by using tribenuronmethyl susceptible and resistant plants. The results showed that the in vitro ALS sensitivity to tribenuron-methyl was significantly reduced in resistant plants when compared with susceptible plants, and the IC50 values of tribenuron-methyl for ALS were 0.187 and 0.036 μmol/L for susceptible and resistant plants, respectively. In vivo experiments revealed that the ALS activity of resistant biotype could be recovered after temporarily inhibited by tribenuron-methyl treatment. However, the in vivo ALS activity of susceptible biotype was consistently reduced after tribenuron-methyl treatment. The GST activity could be induced by tribenuron-methyl treatment in all biotypes, while the resistant biotype had a greater accumulative activity(29.31 U) than the susceptible biotype(25.90 U). In addition, resistant plants had a higher SOD accumulative activity(24.49 U) and stronger recovery ability of SOD than that in sensitive plants(19.31 U); the resistant plants also hold higher POD activity(126.92-550.68 U), CAT activity(41.41-77.19 U) than those in susceptible plants(93.75-271.04 U, 42.17-57.28 U). Based on these findings, reduced ALS sensitivity to tribenuron-methyl was partly responsible for the tribenuronmethyl-resistance in L. arvense L., and the enhanced GST, SOD, POD, CAT activities might also contribute to the tribenuron-methyl resistance.
To clarify the tribenuron-methyl-resistance mechanism in the broad-leaf weed Lithospermum arvense L. in wheat fields, the difference in the response of the target enzymes acetolactate synthase(ALS), metabolic enzyme glutathione-S-transferase(GST) and protective enzymes superoxide dismutase(SOD), peroxidase(POD), and catalase(CAT) to herbicides was analyzed by using tribenuronmethyl susceptible and resistant plants. The results showed that the in vitro ALS sensitivity to tribenuron-methyl was significantly reduced in resistant plants when compared with susceptible plants, and the IC50 values of tribenuron-methyl for ALS were 0.187 and 0.036 μmol/L for susceptible and resistant plants, respectively. In vivo experiments revealed that the ALS activity of resistant biotype could be recovered after temporarily inhibited by tribenuron-methyl treatment. However, the in vivo ALS activity of susceptible biotype was consistently reduced after tribenuron-methyl treatment. The GST activity could be induced by tribenuron-methyl treatment in all biotypes, while the resistant biotype had a greater accumulative activity(29.31 U) than the susceptible biotype(25.90 U). In addition, resistant plants had a higher SOD accumulative activity(24.49 U) and stronger recovery ability of SOD than that in sensitive plants(19.31 U); the resistant plants also hold higher POD activity(126.92-550.68 U), CAT activity(41.41-77.19 U) than those in susceptible plants(93.75-271.04 U, 42.17-57.28 U). Based on these findings, reduced ALS sensitivity to tribenuron-methyl was partly responsible for the tribenuronmethyl-resistance in L. arvense L., and the enhanced GST, SOD, POD, CAT activities might also contribute to the tribenuron-methyl resistance.
引文
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Deng W,Liu MJ,Yang Q,Mei Y,Li XF,Zheng MQ.2015.Tribenuronmethyl resistance and mutation diversity of Pro197 in flixweed(Descurainia sophia L.)accessions from China.Pesticide Biochemistry and Physiology,117:68-74
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Duggleby RG,McCourt JA,Guddat LW.2008.Structure and mechanism of inhibition of plant acetohydroxyacid synthase.Plant Physiology and Biochemistry,46(3):309-324
Fan ZJ,Qian CF,Yu WQ,Chen JP,Li ZM,Wang LX.2003.Study on enzymatic inhibition of acetolactate synthase from maize(Zea mays L.)by chlorsulfuron and tribenuron-methyl.Scientia Agricultura Sinica,36(2):173-178(in Chinese)[范志金,钱传范,于维强,陈俊鹏,李正名,王玲秀.2003.氯磺隆和苯磺隆对玉米乙酰乳酸合成酶抑制作用的研究.中国农业科学,36(2):173-178]
Gerwick BC,Subramanian MV,Loney-Gallant VI,Chandler DP.1990.Mechanism of action of the 1,2,4-triazolo[1,5-a]pyrimidines.Pesticide Science,29:357-364
Han XJ,Dong Y,Sun XN,Li XF,Zheng MQ.2012.Molecular basis of resistance to tribenuron-methyl in Descurainia sophia(L.)populations from China.Pesticide Biochemistry and Physiology,104(1):77-81
Heap IM.2018.The international survey of herbicide resistant weeds.http://www.weedscience.org/Summary/SOASummary.aspx.2018-12-20
Kwak SS,Kim SK,Lee MS,Jung KH,Park IH,Liu JR.1995.Acidic peroxidases from suspension-cultures of sweet potato.Phytochemistry,39(5):981-984
Li HS.2000.The experimental principle and technology of plant physiology and biochemistry.Beijing:Higher Education Press(in Chinese)[李合生.2000.植物生理生化实验原理和技术.北京:高等教育出版社]
Li YF,Zhang ZC,Yang X,Dong MC,Zhang B,Han JY.2015.Susceptibility of weeds in Echinochloa to aryloxyphenoxypropionate herbicides and the mechanism.Jiangsu Journal of Agricultural Sciences,31(3):543-551(in Chinese)[李永丰,张自常,杨霞,董明超,张彬,韩建勇.2015.稻田稗属杂草对芳氧苯氧丙酸酯类除草剂的差异敏感性及其机理.江苏农业学报,31(3):543-551]
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Liu WT,Wu CX,Guo WL,Du L,Yuan GH,Wang JX.2015a.Resistance mechanisms to an acetolactate synthase(ALS)inhibitor in water starwort(Myosoton aquaticum)populations from China.Weed Science,63(4):770-780
Liu WT,Yuan GH,Du L,Guo WL,Li LX,Bi YL,Wang JX.2015b.Anovel Pro197Glu substitution in acetolactate synthase(ALS)confers broad-spectrum resistance across ALS inhibitors.Pesticide Biochemistry and Physiology,117:31-38
Marshall R,Hanley SJ,Hull R,Moss SR.2013.The presence of two different target-site resistance mechanisms in individual plants of Alopecurus myosuroides Huds.,identified using a quick molecular test for the characterisation of six ALS and seven AC-Case SNPs.Pest Management Science,69(6):727-737
McCourt JA,Pang SS,King-Scott J,Guddat LW,Duggleby RG.2006.Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase.Proceedings of the National Academy of Sciences of the United States of America,103(3):569-573
Pan L,Gao HT,Xia WW,Zhang T,Dong LY.2016.Establishing a herbicide-metabolizing enzyme library in Beckmannia syzigachne to identify genes associated with metabolic resistance.Journal of Experimental Botany,67(6):1745-1757
Peng XG,Wang JX,Duan M,Yang JH.2008.The resistance to tribenuron-methyl in Galiuma parine in winter wheat fields in northern China.Journal of Plant Protection,35(5):458-462(in Chinese)[彭学岗,王金信,段敏,杨纪辉.2008.中国北方部分冬麦区猪殃殃对苯磺隆的抗性水平.植物保护学报,35(5):458-462]
Peng XG,Wang JX,Liu JL,Yang JH.2009.Mechanism of resistance to tribenuron-methyl in a resistant biotype of Galiuma parine.Chinese Journal of Pesticide Science,11(2):191-196(in Chinese)[彭学岗,王金信,刘君良,杨纪辉.2009.麦田抗性生物型猪殃殃对苯磺隆的抗性机制.农药学学报,11(2):191-196]
Powles SB,Yu Q.2010.Evolution in action:plants resistant to herbicides.Annual Review of Plant Biology,61:317-347
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