Study on Mutations in ALS for Resistance to Tribenuron-Methyl in Galium aparine L.  

作　　者：SUN Jian WANG Jin-xin ZHANG Hong-jun LIU Jun-liang BIAN Sheng-nan 

机构地区：[1]College of Plant Protection, Shandong Agricultural University, Tai＇an 271018, PR.China [2]Institute for the Control of Agrochemicals, Ministry of Agriculture, Beijing 100125, P.R.China

出　　处：《Agricultural Sciences in China》2011年第1期86-91,共6页中国农业科学（英文版）

基　　金：funded by the National High-Tech R&D Program of China (863 Program, 2006BAD08A09)

摘　　要：In recent years, Galium aparine L. has not been controlled by tribenuron-methyl in major Chinese winter wheat fields. The objective of this study is to understand the molecular basis of the resistance mechanism to tribenuron-methyl in G. aparine and to find the specific mutation sites in amino acid sequence of acetolactate synthase （ALS） in the resistant biotype of G. aparine. Fragments that encode the ALS were amplified and cloned from susceptible （S） and resistant （R） biotypes of G. aparine to tribenuron-methyl and sequenced subsequently. The result showed that the nucleotide sequence of Rbiotype of G. aparine differed from that of the S biotype with three amino acid substitutions, of which, the amino acid substitution of Trp57-4 （TGG） to Gly （GGG） is located in the highly conserved region Domain B. The substitution of Trp574 might be responsible for the resistance to tribenuron-methyl in the R-biotype of G. aparine.In recent years, Galium aparine L. has not been controlled by tribenuron-methyl in major Chinese winter wheat fields. The objective of this study is to understand the molecular basis of the resistance mechanism to tribenuron-methyl in G. aparine and to find the specific mutation sites in amino acid sequence of acetolactate synthase （ALS） in the resistant biotype of G. aparine. Fragments that encode the ALS were amplified and cloned from susceptible （S） and resistant （R） biotypes of G. aparine to tribenuron-methyl and sequenced subsequently. The result showed that the nucleotide sequence of Rbiotype of G. aparine differed from that of the S biotype with three amino acid substitutions, of which, the amino acid substitution of Trp57-4 （TGG） to Gly （GGG） is located in the highly conserved region Domain B. The substitution of Trp574 might be responsible for the resistance to tribenuron-methyl in the R-biotype of G. aparine.

关 键 词：RESISTANCE Galium aparine L. acetolactate synthase gene mutation 

分 类 号：S451.221[农业科学—植物保护] TQ457.29[化学工程—农药化工]