Diacylglycerol acyltransferase 1 is activated by phosphatidate and inhibited by SnRK1-catalyzed phosphorylation

The Plant Journal : for Cell and Molecular Biology
Kristian Mark P CaldoM Joanne Lemieux

Abstract

Diacylglycerol acyltransferase 1 (DGAT1) catalyzes the final and committed step in the Kennedy pathway for triacylglycerol (TAG) biosynthesis and, as such, elucidating its mode of regulation is critical to understand the fundamental aspects of carbon metabolism in oleaginous crops. In this study, purified Brassica napus diacylglycerol acyltransferase 1 (BnaDGAT1) in n-dodecyl-β-d-maltopyranoside micelles was lipidated to form mixed micelles and subjected to detailed biochemical analysis. The degree of mixed micelle fluidity appeared to influence acyltransferase activity. BnaDGAT1 exhibited a sigmoidal response and eventual substrate inhibition with respect to increasing concentrations of oleoyl-CoA. Phosphatidate (PA) was identified as a feed-forward activator of BnaDGAT1, enabling the final enzyme in the Kennedy pathway to adjust to the incoming flow of carbon leading to TAG. In the presence of PA, the oleoyl-CoA saturation plot became more hyperbolic and desensitized to substrate inhibition indicating that PA facilitates the transition of the enzyme into the more active state. PA may also relieve possible autoinhibition of BnaDGAT1 brought about by the N-terminal regulatory domain, which was shown to interact with PA. Indeed,...Continue Reading

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Citations

Mar 12, 2021·Journal of Experimental Botany·Muhammed Jamsheer KVibha Srivastava
Apr 9, 2021·Frontiers in Plant Science·Zhiyang ZhaiJohn Shanklin
Apr 15, 2021·The Plant Journal : for Cell and Molecular Biology·Linhui YuChangcheng Xu
Apr 26, 2019·Chemical Reviews·Ana-Nicoleta Bondar, M Joanne Lemieux

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