> Detailanzeige

Vande Berg, Brian J; Hammer, Philip E; Chun, Betty L; Schouten, Laura C; Carr, Brian; Guo, Rong; Peters, Cheryl; Hinson, Todd K; Beilinson, Vadim; Shekita, Amy; Deter, Rebekah; Chen, Zhixian; Samoylov, Vladimir; Bryant, Charles T; Stauffer, Maria E; Eberle, Timothy; Moellenbeck, Dan J; Carozzi, Nadine B; Koziel, Mike G; Duck, Nicholas B

Characterization and plant expression of a glyphosate‐tolerant enolpyruvylshikimate phosphate synthase

Literatur-
verwaltung

Zur
Merkliste

Lösche von
Merkliste

Per Whatsapp teilen

Schließen

Merkliste



Sie können Bookmarks mittels Listen verwalten, loggen Sie sich dafür bitte in Ihr SLUB Benutzerkonto ein.
  • Medientyp: E-Artikel
  • Titel: Characterization and plant expression of a glyphosate‐tolerant enolpyruvylshikimate phosphate synthase
  • Beteiligte: Vande Berg, Brian J; Hammer, Philip E; Chun, Betty L; Schouten, Laura C; Carr, Brian; Guo, Rong; Peters, Cheryl; Hinson, Todd K; Beilinson, Vadim; Shekita, Amy; Deter, Rebekah; Chen, Zhixian; Samoylov, Vladimir; Bryant, Charles T; Stauffer, Maria E; Eberle, Timothy; Moellenbeck, Dan J; Carozzi, Nadine B; Koziel, Mike G; Duck, Nicholas B
  • Erschienen: Wiley, 2008
  • Erschienen in: Pest Management Science
  • Sprache: Englisch
  • DOI: 10.1002/ps.1507
  • ISSN: 1526-498X; 1526-4998
  • Schlagwörter: Insect Science ; Agronomy and Crop Science ; General Medicine
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: <jats:title>Abstract</jats:title><jats:p><jats:bold>BACKGROUND:</jats:bold> Glyphosate tolerance is a dominant trait in modern biotech crops.</jats:p><jats:p><jats:bold>RESULTS:</jats:bold> A gene encoding a glyphosate‐tolerant EPSP synthase (<jats:italic>aro</jats:italic>A<jats:sub>1398</jats:sub>) from bacterial strain ATX1398 was cloned and characterized. The protein is initiated at a GTG translational start codon to produce a protein that provides robust glyphosate resistance in <jats:italic>Escherichia coli</jats:italic> (Mig) Cast &amp; Chalm. The <jats:italic>aro</jats:italic>A<jats:sub>1398</jats:sub> protein was expressed and purified from <jats:italic>E. coli</jats:italic>, and key kinetic values were determined (<jats:italic>K</jats:italic><jats:sub><jats:italic>i</jats:italic></jats:sub> = 161 µ<jats:sc>M</jats:sc>; <jats:italic>K</jats:italic><jats:sub><jats:italic>m</jats:italic></jats:sub>(PEP) = 11.3 µ<jats:sc>M</jats:sc>; <jats:italic>k</jats:italic><jats:sub>cat</jats:sub> = 28.3 s<jats:sup>−1</jats:sup>). The full‐length enzyme is 800‐fold more resistant to glyphosate than the maize EPSP synthase while retaining high affinity for the substrate phosphoenol pyruvate. To evaluate further the potential of <jats:italic>aro</jats:italic>A<jats:sub>1398</jats:sub>, transgenic maize events expressing the <jats:italic>aro</jats:italic>A<jats:sub>1398</jats:sub> protein were generated. T<jats:sub>0</jats:sub> plants were screened for tolerance to glyphosate sprays at 1.3× commercial spray rates, and T<jats:sub>1</jats:sub> plants were selected that completely resisted glyphosate sprays at 1×, 2× and 4× recommended spray rates in field trials.</jats:p><jats:p><jats:bold>CONCLUSION:</jats:bold> These data suggest that <jats:italic>aro</jats:italic>A<jats:sub>1398</jats:sub> is a suitable candidate for conferring glyphosate tolerance in transgenic crop plants. Copyright © 2008 Society of Chemical Industry</jats:p>