This study established a new system for potato transformation using toxoflavin as selection agent and toxoflavin lyase (tflA) as selectable marker gene. Potato plants expressing tflA was successfully transformed on toxoflavin medium with 27% efficiency, similar to that for the hygromycin/hpt selection system. The transgenic potato expressing tflA also showed resistance to Burkholderia glumea infection.
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Investigations into the Biosynthesis, Regulation, and Self-Resistance of Toxoflavin in Pseudomonas protegens Pf-5.
Chembiochem
August 2015
Agricultural Research Service, US Department of Agriculture, 3420 N.W. Orchard Avenue, Corvallis, OR 97330 (USA).
Pseudomonas spp. are prolific producers of natural products from many structural classes. Here we show that the soil bacterium Pseudomonas protegens Pf-5 is capable of producing trace levels of the triazine natural product toxoflavin (1) under microaerobic conditions.
View Article and Find Full Text PDFToxoflavin lyase enzyme as a marker for selecting potato plant transformants.
Biosci Biotechnol Biochem
June 2013
Green-Bio Research Center, KRIBB, Daejeon, Korea.
This study established a new system for potato transformation using toxoflavin as selection agent and toxoflavin lyase (tflA) as selectable marker gene. Potato plants expressing tflA was successfully transformed on toxoflavin medium with 27% efficiency, similar to that for the hygromycin/hpt selection system. The transgenic potato expressing tflA also showed resistance to Burkholderia glumea infection.
View Article and Find Full Text PDFIdentification of the product of toxoflavin lyase: degradation via a Baeyer-Villiger oxidation.
J Am Chem Soc
March 2012
Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States.
Toxoflavin (an azapteridine) is degraded to a single product by toxoflavin lyase (TflA) in a reaction dependent on reductant, Mn(II), and oxygen. The isolated product was fully characterized by NMR and MS and was identified as a triazine in which the pyrimidine ring was oxidatively degraded. A mechanism for toxoflavin degradation based on the identification of the enzymatic product and the recently determined crystal structure of toxoflavin lyase is proposed.
View Article and Find Full Text PDFToxoflavin lyase requires a novel 1-His-2-carboxylate facial triad.
Biochemistry
February 2011
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, United States.
High-resolution crystal structures are reported for apo, holo, and substrate-bound forms of a toxoflavin-degrading metalloenzyme (TflA). In addition, the degradation reaction is shown to be dependent on oxygen, Mn(II), and dithiothreitol in vitro. Despite its low sequence identity with proteins of known structure, TflA is structurally homologous to proteins of the vicinal oxygen chelate superfamily.
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