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Protein S-acyl Transferase 15 is Involved in Seed Triacylglycerol Catabolism during Early Seedling Growth in Arabidopsis

Li, Y, Xu, J, Li, G, Wan, S, Batistic, O, Sun, M, Zhang, Y, Scott, R and Qi, B Protein S-acyl Transferase 15 is Involved in Seed Triacylglycerol Catabolism during Early Seedling Growth in Arabidopsis. Journal of Experimental Botany. ISSN 0022-0957 (Accepted)

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Abstract

Seeds of Arabidopsis contain ~40% of triacylglycerol. It is converted to sugar to support post germination growth. We identified an Arabidopsis T-DNA knockout mutant that was sugar dependent during early seedling establishment. Our study showed that the β-oxidation process involved in catabolising the free fatty acids released from the seed triacylglycerol was impaired in this mutant. This mutant was confirmed to be transcriptional null for the Protein Acyl Transferase 15, AtPAT15 (At5g04270), one of the 24 protein acyl transferases in Arabidopsis. Although it is the shortest AtPAT15 contains the signature ‘Asp-His-His-Cys cysteine rich domain’ which is essential for the enzyme activity of this family of proteins. The function of AtPAT15 was validated because it rescued the growth defect of the yeast protein acyl transferase mutant akr1 and it was also auto-acylated in vitro. Transient expression of AtPAT15 in Arabidopsis and tobacco localized AtPAT15 in the Golgi apparatus. Taken together, our data clearly demonstrated that AtPAT15 is involved in β-oxidation of triacylglycerol, revealing the importance of protein S-acylation in seed storage lipid breakdown during early seedling growth of Arabidopsis.

Item Type: Article
Uncontrolled Keywords: 0607 Plant Biology, 0703 Crop and Pasture Production, 0604 Genetics
Subjects: R Medicine > RM Therapeutics. Pharmacology
R Medicine > RV Botanic, Thomsonian, and eclectic medicine
Divisions: Pharmacy & Biomolecular Sciences
Publisher: Oxford University Press (OUP)
Date Deposited: 20 Sep 2019 11:17
Last Modified: 20 Sep 2019 11:17
DOI or Identification number: 10.1093/jxb/erz282
URI: http://researchonline.ljmu.ac.uk/id/eprint/11363

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