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Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis

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; At1g...

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Detalles Bibliográficos
Autores principales: Aymé, Laure, Arragain, Simon, Canonge, Michel, Baud, Sébastien, Touati, Nadia, Bimai, Ornella, Jagic, Franjo, Louis-Mondésir, Christelle, Briozzo, Pierre, Fontecave, Marc, Chardot, Thierry
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6250708/
https://www.ncbi.nlm.nih.gov/pubmed/30467384
http://dx.doi.org/10.1038/s41598-018-35545-7
Descripción
Sumario: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.