Société Française de Biochimie et Biologie Moléculaire

Laure AYME - June 2019

IJPB, INRA, AgroParisTech, CNRS, Université Paris-Saclay, 78000, Versailles, France Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in triacyglycerol metabolism Scientific Report, 8, 17254 (2018) Aymé L., Arragain S., Canonge M., Baud S., Touati N., Binet L., Jagic F., Louis-Mondésir C., Briozzo P., Fontecave M., Chardot T.


Laure Aymé, 30 years old, is currently a postdoctoral researcher at the Institut Français du Pétrole Energies nouvelles (Rueil-Malmaison) where she is investigating the activity of microbial cellulases involved in the degradation of agricultural co-products. After studies at AgroParisTech, in 2016, she obtained a PhD under the supervision of Dr. Thierry Chardot (Jean-Pierre Bourgin Institute, INRA, Versailles). Her main area of interest is biomolecule engineering and during her thesis, she characterized the activity of enzymes belonging to the three major families of diacylglycerol acyltransferases (DGATs). These enzymes catalyze the last step of triacylglycerol synthesis. In the selected publication published in the journal Scientific Reports under the title « Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis », Laure Aymé and her collaborators described for the first time, a metalloprotein with a DGAT activity, the DGAT3 of Arabidopsis thaliana, harboring a [2Fe-2S] cluster. The binding domain of this cluster is conserved within the plant specific family of DGAT3s.


Laure Aymé

IFPEN 1-4 Avenue du Bois Préau, 92852 Rueil-Malmaison


Acyl-CoA:diacylglycerol acyltransferases 3 (DGAT3) are described as plant cytosolic enzymes synthesizing triacylglycerol. Their protein sequences exhibit a thioredoxin-like ferredoxin domain typical of a class of ferredoxins harboring a [2Fe-2S] cluster. The Arabidopsis thaliana DGAT3 (AtDGAT3; At1g48300) protein is detected in germinating seeds. The recombinant purified protein produced from Escherichia coli, although very unstable, exhibits DGAT activity in vitro. A shorter protein version devoid of its N-terminal putative chloroplast transit peptide, Δ46AtDGAT3, was more stable in vitro, allowing biochemical and spectroscopic characterization. The results obtained demonstrate the presence of a [2Fe-2S] cluster in the protein. To date, AtDGAT3 is the first metalloprotein described as a DGAT.