جهش‌ در آنزیم استیل کوآنزیم آ کربوکسیلاز، مکانیسم مقاومت عرضی بیوتیپ‌های یولاف وحشی(Avena ludoviciana Deuri.) به علف‌کش‌های بازدارنده ACCase

نوع مقاله: مقاله پژوهشی

نویسندگان

1 دانشگاه صنعتی اصفهان

2 موسسه تحقیقات گیاهپزشکی

3 دانشگاه تهران

4 دانشگاه فردوسی مشهد

چکیده

به منظور تشخیص مکانیزم احتمالی مقاومت براساس محل عمل و نوع جهش‌های صورت گرفته در آنزیم ACCase، 13 بیوتیپ یولاف وحشی(Avena ludoviciana Deuri.)  جمع‌آوری شده از استان خوزستان که دارای مقاومت عرضی به علفکش‌های بازدارنده ACCase بودند آزمایشات مولکولی انجام شد. در این آزمایشات جهش‌های مهم  در محل کربوکسیل ترانسفراز آنزیم ACCase (شامل چهار جهش ایزولوسین-2041-آسپاراژین، سیستین-2088-آرژنین، ایزولوسین-1781-لوسین و آسپارتیک اسید-2078-گلایسین) مورد بررسی قرارگرفتند. برای انجام این مطالعه از روش‌های CAPS و dCAPS استفاده شد. هردو روش شامل سه مرحله استخراج  DNAاز بیوتیپ‌‌های مورد آزمایش،PCR با استفاده از پرایمرهای اختصاصی و در نهایت هضم توسط آنزیم برشی اختصاصی بود. نتایج این تحقیق نشان داد که 8/53 درصد بیوتیپ‌‌های مقاوم به بازدارنده‌های ACCase دارای جهش ایزولوسین-1781-لوسین و 6/7 درصد بیوتیپ‌‌ها دارای جهش آسپارتیک اسید-2078-گلایسین‌می‌باشند. در بین بیوتیپ‌های مورد بررسی تنها یک بیوتیپ دارای دو جهش (ایزولوسین-1781-لوسین و آسپارتیک اسید-2078-گلایسین) بود و در هیچکدام از بیوتیپ‌های مورد مطالعه جهش  ایزولوسین-2041-آسپاراژین و سیستین-2088-آرژنین دیده نشد. بنابراین الگوهای مختلف مقاومت عرضی بیوتیپ‌های یولاف وحشی به دلیل وجود جهش‌های مختلف در ناحیه کربوکسیل ترانسفراز آنزیم ACCase می‌باشد.

کلیدواژه‌ها


عنوان مقاله [English]

Mutations in Acetyl-CoA Carboxylase Enzyme, Mechanism of Cross Resistance in Wild Oat (Avena ludoviciana Deuri.) Biotypes to ACCase Inhibitor Herbicides

نویسندگان [English]

  • Fatemeh Benakashani 1
  • Eskandar Zand 2
  • Mohammad Reza Naghavi 3
  • Hamid Reza Sasanfar 4
چکیده [English]

In order to detect the probability of ACCase inhibitor herbicides target-site based resistance of 13 wild oat (Avena ludoviciana Deuri.) biotypes, molecular experiments were performed using CAPS and dCAPS methods. Biotypes were collected from khuzestan province and which showed cross-resitance to ACCase inhibitors. The above-mentioned molecular methods were used to identify the locations of four important mutations (Isoleucine-2041-Asparagine, Cystein-2088-Arginin, Isoleucine-1781-Leucine and Aspartic acid-2078-Glycine) responsible for target site based herbicide resistance in the carboxyltransferase domain of ACCase enzyme. Both approaches involve DNA extraction, PCR using specific primers and restriction digests of PCR products with restriction enzymes. Results of experiments showed that Isoleucine-1781-Leucine and Aspartic acid-2078-Glycine mutations were observed in 53.8% and 7.6% of resistant wild oat biotypes, respectively. Among the investigated biotypes, only one biotype had two mutations (Isoleucine -1781-Leucine and Aspartic acid-2078-Glycine). Thus, different mutations in the carboxyl transferase domain of ACCase enzyme were the reason of various cross resistance patterns among wild oat biotypes.

کلیدواژه‌ها [English]

  • Mutation
  • Target site-based resistance
  • ACCase enzyme
  • CAPS
  • dCAPS
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