ArticlePloS one2018
Cloning of the pks3 gene of Aurantiochytrium limacinum and functional study of the 3-ketoacyl-ACP reductase and dehydratase enzyme domains.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 27 citations in OpenAlex.
- Substrate specificities of two ketosynthases in eukaryotic microalgal and prokaryotic marine bacterial DHA synthases.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Enhancing fatty acid and omega-3 production in Schizochytrium sp. using developed safe-harboring expression system.Journal of biological engineering · 2024Article
- Functional analysis of the dehydratase domains of the PUFA synthase from Emiliania huxleyi in Escherichia coli and Arabidopsis thaliana.Biotechnology for biofuels and bioproducts · 2022Article
- Deciphering and engineering the polyunsaturated fatty acid synthase pathway from eukaryotic microorganisms.Frontiers in bioengineering and biotechnology · 2022Review
- Article
- Method Development Progress in Genetic Engineering of Thraustochytrids.Marine drugs · 2021Review
- Function of ORFC of the polyketide synthase gene cluster on fatty acid accumulation in Schizochytrium limacinum SR21.Biotechnology for biofuels · 2021Article
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Authors and funding
11 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Aurantiochytrium limacinum has received attention because of its abundance of polyunsaturated fatty acids (PUFAs), particularly docosahexaenoic acid (DHA). DHA is synthesized through the polyketide synthase (PKS) pathway in A. limacinum. The related enzymes of the PKS pathway are mainly expressed by three gene clusters, called pks1, pks2 and pks3. In this study, the full-length pks3 gene was obtained by polymerase chain reaction amplification and Genome Walking technology. Based on a domain analysis of the deduced amino acid sequence of the pks3 gene, 3-ketoacyl-ACP reductase (KR) and dehydratase (DH) enzyme domains were identified. Herein, A. limacinum OUC168 was engineered by gene knock-in of KR and DH using the 18S rDNA sequence as the homologous recombination site. Total fatty acid contents and the degree of unsaturation of total fatty acids increased after the kr or dh gene was knocked in. The cloning and functional study of the pks3 gene of A. limacinum establishes a foundation for revealing the DHA synthetic pathway. Gene knock-in of the enzyme domain associated with PKS synthesis has the potential to provide effective recombinant strains with higher DHA content for industrial applications.
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