Characterization of sulfonylurea-resistant Schoenoplectus juncoides having a target-site Asp376Glu mutation in the acetolactate synthase

被引:23
作者
Sada, Yoshinao [1 ,2 ]
Ikeda, Hajime [1 ]
Yamato, Seiji [1 ]
Kizawa, Satoru [1 ]
机构
[1] Sumitomo Chem Co Ltd, Hlth & Crop Sci Res Lab, Takarazuka, Hyogo, Japan
[2] Sumitomo Chem Co Ltd, Crop Protect Div Int, Tokyo, Japan
关键词
Schoenoplectus juncoides; Asp(376)Glu mutation; Heterologously-expressed ALS; Cross resistance; Dose-response; Resistance factor; INHIBITING HERBICIDES; MOLECULAR-BASIS; POPULATIONS; BIOTYPES;
D O I
10.1016/j.pestbp.2013.05.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Schoenoplectus juncoides, a noxious weed for paddy rice, is known to become resistant to sulfonylurea (SU) herbicides by a target-site mutation in either of the two acetolactate synthase (ALS) genes (ALS1 and ALS2). SU-resistant S. juncoides plants having an Asp(376)Glu mutation in ALS2 were found from a paddy rice field in Japan, but their resistance profile has not been quantitatively investigated. In this study, dose response of the SU-resistant accession was compared with that of a SU-susceptible accession at in vivo whole-plant level as well as at in vitro enzymatic level. In whole-plant tests, resistance factors (RFs) based on 50% growth reduction (GR(50)) for imazosulfuron bensulfuron-methyl (BSM), metsulfuron-methyl (MSM), bispyribac-sodium (BPS), and imazaquin (IMQ) were 176, 40, 14, 5.2 and 1.5, respectively. Thus, the accession having an Asp(376)Glu mutation in ALS2 was highly resistant to the three SU herbicides and moderately resistant to BPS, but was not substantially resistant to IMQ. This is slightly different from the earlier results reported from other weeds with an Asp(376)Glu mutation, in which the mutation confers resistance to broadly all the chemical classes of ALS-inhibiting herbicides. In enzymatic tests, ALS2 of S. juncoides was expressed in E. coli; the resultant ALS2 was subjected to an in vitro assay. RFs of the mutated ALS2 based on 50% enzymatic inhibition (I-50) for ISF, BSM, MSM, BPS, and IMQ were 3699, 2438, 322, 80, and 4.8, respectively. The RFs of ALS2 were highly correlated with those of the whole-plant; this suggests that the Asp(376)Glu mutation in ALS2 is a molecular basis for the whole-plant resistance. The presence of two ALS genes in S. juncoides can at least partially explain why the whole-plant RFs were less than those of the expressed ALS2 enzymes. (C) 2013 Elsevier Inc. All rights reserved.
引用
收藏
页码:106 / 111
页数:6
相关论文
共 25 条
[1]   Characterization and diagnostic tests of resistance to acetohydroxyacid synthase inhibitors due to an Asp376Glu substitution in Amaranthus powellii [J].
Ashigh, Jamshid ;
Corbett, Cheryl-Ann L. ;
Smith, Peter J. ;
Laplante, Julie ;
Tardif, Francois J. .
PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY, 2009, 95 (01) :38-46
[2]   Acetolactate Synthase Inhibitor-Resistant False Cleavers (Galium spurium) in Western Canada [J].
Beckie, Hugh J. ;
Warwick, Suzanne I. ;
Sauder, Connie A. ;
Kelln, Gina M. ;
Lozinski, Chris .
WEED TECHNOLOGY, 2012, 26 (01) :151-155
[3]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[4]   Expression, purification and characterization of Arabidopsis thaliana acetohydroxyacid synthase [J].
Chang, AK ;
Duggleby, RG .
BIOCHEMICAL JOURNAL, 1997, 327 :161-169
[5]  
Corbett C. L., 2004, THESIS U GUELPH GUEL
[6]  
Duggleby RG, 2000, J BIOCHEM MOL BIOL, V33, P1
[7]  
Falco S. C., 1989, Developments in Industrial Microbiology, V30, P187
[8]   Genetic diversity of sulfonylurea-resistant and -susceptible Monochoria vaginalis populations in Japan [J].
Imaizumi, T. ;
Wang, G. X. ;
Ohsako, T. ;
Tominaga, T. .
WEED RESEARCH, 2008, 48 (02) :187-196
[9]   Two consecutive aspartic acid residues conferring herbicide resistance in tobacco acetohydroxy acid synthase [J].
Le, DT ;
Yoon, MY ;
Kim, YT ;
Choi, JD .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2005, 1749 (01) :103-112
[10]   Molecular basis of sulfonylurea herbicide inhibition of acetohydroxyacid synthase [J].
Pang, SS ;
Guddat, LW ;
Duggleby, RG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (09) :7639-7644