Dataset Information

Enhancing oil production in Arabidopsis through expression of a ketoacyl-ACP synthase domain of the PUFA synthase from Thraustochytrium.

ABSTRACT: Background:Plant seed oil is an important bioresource for human food and animal feed, as well as industrial bioproducts. Therefore, increasing oil content in seeds has been one of the primary targets in the breeding programs of oilseed crops. Thraustochytrium is a marine protist that can produce a high level of very long-chain polyunsaturated fatty acids (VLCPUFAs) using a PUFA synthase, a polyketide synthase-like fatty acid synthase with multiple catalytic domains. Our previous study showed that a KS domain from the synthase could complement an Escherichia coli mutant defective in ?-ketoacyl-ACP synthase I (FabB) and increase the total fatty acid production. In this study, this KS domain from the PUFA synthase was further functionally analyzed in Arabidopsis thaliana for the capacity of oil production. Results:The plastidial expression of the KS domain could complement the defective phenotypes of a KASI knockout mutant generated by CRISPR/Cas9. Seed-specific expression of the domain in wild-type Arabidopsis significantly increased seed weight and seed oil, and altered the unsaturation level of fatty acids in seeds, as well as promoted seed germination and early seedling growth. Conclusions:The condensation process of fatty acid biosynthesis in plants is a limiting step, and overexpression of the KS domain from a PUFA synthase of microbial origin offers a new strategy to increase oil production in oilseed plants.

SUBMITTER: Xie X

PROVIDER: S-EPMC6599236 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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Enhancing oil production in <i>Arabidopsis</i> through expression of a ketoacyl-ACP synthase domain of the PUFA synthase from <i>Thraustochytrium</i>.

Xie Xi X Meesapyodsuk Dauenpen D Qiu Xiao X

Biotechnology for biofuels 20190629

<h4>Background</h4>Plant seed oil is an important bioresource for human food and animal feed, as well as industrial bioproducts. Therefore, increasing oil content in seeds has been one of the primary targets in the breeding programs of oilseed crops. <i>Thraustochytrium</i> is a marine protist that can produce a high level of very long-chain polyunsaturated fatty acids (VLCPUFAs) using a PUFA synthase, a polyketide synthase-like fatty acid synthase with multiple catalytic domains. Our previous s ...[more]

PMID: 31297160

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Project description:BackgroundThe fatty-acid profile of the vegetable oils determines its properties and nutritional value. Palm-oil obtained from the African oil-palm [Elaeis guineensis Jacq. (Tenera)] contains 44% palmitic acid (C16:0), but, palm-oil obtained from the American oilpalm [Elaeis oleifera] contains only 25% C16:0. In part, the b-ketoacyl-[ACP] synthase II (KASII) [EC: 2.3.1.179] protein is responsible for the high level of C16:0 in palm-oil derived from the African oil-palm. To understand more about E. guineensis KASII (EgKASII) and E. oleifera KASII (EoKASII) proteins, it is essential to know its structures. Hence, this study was undertaken.ObjectiveThe objective of this study was to predict three-dimensional (3D) structure of EgKASII and EoKASII proteins using molecular modelling tools.Materials and methodsThe amino-acid sequences for KASII proteins were retrieved from the protein database of National Center for Biotechnology Information (NCBI), USA. The 3D structures were predicted for both proteins using homology modelling and ab-initio technique approach of protein structure prediction. The molecular dynamics (MD) simulation was performed to refine the predicted structures. The predicted structure models were evaluated and root mean square deviation (RMSD) and root mean square fluctuation (RMSF) values were calculated.ResultsThe homology modelling showed that EgKASII and EoKASII proteins are 78% and 74% similar with Streptococcus pneumonia KASII and Brucella melitensis KASII, respectively. The EgKASII and EoKASII structures predicted by using ab-initio technique approach shows 6% and 9% deviation to its structures predicted by homology modelling, respectively. The structure refinement and validation confirmed that the predicted structures are accurate.ConclusionThe 3D structures for EgKASII and EoKASII proteins were predicted. However, further research is essential to understand the interaction of EgKASII and EoKASII proteins with its substrates.

Dataset Information

Enhancing oil production in Arabidopsis through expression of a ketoacyl-ACP synthase domain of the PUFA synthase from Thraustochytrium.

Publications

Enhancing oil production in <i>Arabidopsis</i> through expression of a ketoacyl-ACP synthase domain of the PUFA synthase from <i>Thraustochytrium</i>.

Similar Datasets

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