مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Verion

Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

video

Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

sound

Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Version

Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

View:

1,225
Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Download:

0
Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Cites:

Information Journal Paper

Title

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

Pages

  179-190

Abstract

 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.

Cites

  • No record.
  • References

  • No record.
  • Cite

    APA: Copy

    BENAKASHANI, FATEMEH, ZAND, ESKANDAR, NAGHAVI, MOHAMMAD REZA, & Sasanfar, Hamidreza. (2014). Mutations in Acetyl-CoA Carboxylase Enzyme, Mechanism of Cross Resistance in Wild Oat (Avena ludoviciana Deuri. ) Biotypes to ACCase Inhibitor Herbicides. IRANIAN JOURNAL OF WEED SCIENCE, 10(2 ), 179-190. SID. https://sid.ir/paper/185254/en

    Vancouver: Copy

    BENAKASHANI FATEMEH, ZAND ESKANDAR, NAGHAVI MOHAMMAD REZA, Sasanfar Hamidreza. Mutations in Acetyl-CoA Carboxylase Enzyme, Mechanism of Cross Resistance in Wild Oat (Avena ludoviciana Deuri. ) Biotypes to ACCase Inhibitor Herbicides. IRANIAN JOURNAL OF WEED SCIENCE[Internet]. 2014;10(2 ):179-190. Available from: https://sid.ir/paper/185254/en

    IEEE: Copy

    FATEMEH BENAKASHANI, ESKANDAR ZAND, MOHAMMAD REZA NAGHAVI, and Hamidreza Sasanfar, “Mutations in Acetyl-CoA Carboxylase Enzyme, Mechanism of Cross Resistance in Wild Oat (Avena ludoviciana Deuri. ) Biotypes to ACCase Inhibitor Herbicides,” IRANIAN JOURNAL OF WEED SCIENCE, vol. 10, no. 2 , pp. 179–190, 2014, [Online]. Available: https://sid.ir/paper/185254/en

    Related Journal Papers

    Related Seminar Papers

  • No record.
  • Related Plans

  • No record.
  • Recommended Workshops






    Move to top