Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis. Issue 1 (December 2018)

• Record Type: Journal Article
• Authors: Aymé, Laure; Arragain, Simon; Canonge, Michel; Baud, Sébastien; Touati, Nadia; Bimai, Ornella; Jagic, Franjo; Louis-Mondésir, Christelle; Briozzo, Pierre; Fontecave, Marc; Chardot, Thierry
• Is Part Of: Scientific reports. Volume 8:Issue 1(2018)
• Page Start: 1
• Page End: 10
• Publication Date: 2018-12
• Subjects: Natural history -- Research -- Periodicals; Biology -- Research -- Periodicals; Physical sciences -- Research -- Periodicals; Earth sciences -- Research -- Periodicals; Environmental sciences -- Research -- Periodicals; 502.85
• DOI: 10.1038/s41598-018-35545-7
• Languages: English
• ISSNs: 2045-2322

Abstract

Abstract 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. TheArabidopsis thaliana DGAT3 (AtDGAT3; At1g48300) protein is detected in germinating seeds. The recombinant purified protein produced fromEscherichia coli, although very unstable, exhibits DGAT activityin vitro . A shorter protein version devoid of its N-terminal putative chloroplast transit peptide, Δ46AtDGAT3, was more stablein 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.