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      A phospholipid:diacylglycerol acyltransferase is involved in the regulation of phospholipids homeostasis in oleaginous Aurantiochytrium sp.

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          Abstract

          Background

          Thraustochytrids have gained attention as a potential source for the production of docosahexaenoic acid (DHA), where DHA is predominantly stored in the form of triacylglycerol (TAG). The TAG biosynthesis pathways, including the acyl-CoA-dependent Kennedy pathway and the acyl-CoA-independent pathway, have been predicted in thraustochytrids, while the specific details regarding their roles are currently uncertain.

          Results

          Phospholipid:diacylglycerol acyltransferase (PDAT) plays a key role in the acyl-CoA-independent pathway by transferring acyl-group from phospholipids (PL) to diacylglycerol (DAG) to from TAG. In thraustochytrid Aurantiochytrium sp. SD116, an active AuPDAT was confirmed by heterologous expression in a TAG-deficient yeast strain H1246. Analysis of AuPDAT function in vivo revealed that deletion of AuPDAT led to slow growth and a significant decrease in cell number, but improved PL content in the single cell during the cell growth and lipid accumulation phases. Interestingly, deletion of AuPDAT did not affect total lipid and TAG content, but both were significantly increased within a single cell. Moreover, overexpression of AuPDAT also resulted in a decrease in cell number, while the total lipid and cell diameter of a single cell were markedly increased. Altogether, both up-regulation and down-regulation of AuPDAT expression affected the cell number, which further associated with the total lipid and TAG content in a single cell.

          Conclusions

          Our study demonstrates that AuPDAT-mediated pathway play a minor role in TAG synthesis, and that the function of AuPDAT may be involved in regulating PL homeostasis by converting PL to TAG in a controlled manner. These findings expand our understanding of lipid biosynthesis in Aurantiochytrium sp. and open new avenues for developing “customized cell factory” for lipid production.

          Supplementary Information

          The online version contains supplementary material available at 10.1186/s13068-023-02396-y.

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          Most cited references30

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          Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants.

          A DAHLQVIST, U Stahl, M Lenman … (2000)
          Triacylglycerol (TAG) is known to be synthesized in a reaction that uses acyl-CoA as acyl donor and diacylglycerol (DAG) as acceptor, and which is catalyzed by the enzyme acyl-CoA:diacylglycerol acyltransferase. We have found that some plants and yeast also have an acyl-CoA-independent mechanism for TAG synthesis, which uses phospholipids as acyl donors and DAG as acceptor. This reaction is catalyzed by an enzyme that we call phospholipid:diacylglycerol acyltransferase, or PDAT. PDAT was characterized in microsomal preparations from three different oil seeds: sunflower, castor bean, and Crepis palaestina. We found that the specificity of the enzyme for the acyl group in the phospholipid varies between these species. Thus, C. palaestina PDAT preferentially incorporates vernoloyl groups into TAG, whereas PDAT from castor bean incorporates both ricinoleoyl and vernoloyl groups. We further found that PDAT activity also is present in yeast microsomes. The substrate specificity of this PDAT depends on the head group of the acyl donor, the acyl group transferred, and the acyl chains of the acceptor DAG. The gene encoding the enzyme was identified. The encoded PDAT protein is related to lecithin:cholesterol acyltransferase, which catalyzes the acyl-CoA-independent synthesis of cholesterol esters. However, budding yeast PDAT and its relatives in fission yeast and Arabidopsis form a distinct branch within this protein superfamily, indicating that a separate PDAT enzyme arose at an early point in evolution.
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            Phospholipid:diacylglycerol acyltransferase is a multifunctional enzyme involved in membrane lipid turnover and degradation while synthesizing triacylglycerol in the unicellular green microalga Chlamydomonas reinhardtii.

            Qiang Hu, Milton Sommerfeld, Danxiang Han … (2012)
            Many unicellular microalgae produce large amounts (∼20 to 50% of cell dry weight) of triacylglycerols (TAGs) under stress (e.g., nutrient starvation and high light), but the synthesis and physiological role of TAG are poorly understood. We present detailed genetic, biochemical, functional, and physiological analyses of phospholipid:diacylglycerol acyltransferase (PDAT) in the green microalga Chlamydomonas reinhardtii, which catalyzes TAG synthesis via two pathways: transacylation of diacylglycerol (DAG) with acyl groups from phospholipids and galactolipids and DAG:DAG transacylation. We demonstrate that PDAT also possesses acyl hydrolase activities using TAG, phospholipids, galactolipids, and cholesteryl esters as substrates. Artificial microRNA silencing of PDAT in C. reinhardtii alters the membrane lipid composition, reducing the maximum specific growth rate. The data suggest that PDAT-mediated membrane lipid turnover and TAG synthesis is essential for vigorous growth under favorable culture conditions and for membrane lipid degradation with concomitant production of TAG for survival under stress. The strong lipase activity of PDAT with broad substrate specificity suggests that this enzyme could be a potential biocatalyst for industrial lipid hydrolysis and conversion, particularly for biofuel production.
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              Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae.

              George Carman, Gil-Soo Han (2011)
              The yeast Saccharomyces cerevisiae, with its full complement of organelles, synthesizes membrane phospholipids by pathways that are generally common to those found in higher eukaryotes. Phospholipid synthesis in yeast is regulated in response to a variety of growth conditions (e.g., inositol supplementation, zinc depletion, and growth stage) by a coordination of genetic (e.g., transcriptional activation and repression) and biochemical (e.g., activity modulation and localization) mechanisms. Phosphatidate (PA), whose cellular levels are controlled by the activities of key phospholipid synthesis enzymes, plays a central role in the transcriptional regulation of phospholipid synthesis genes. In addition to the regulation of gene expression, phosphorylation of key phospholipid synthesis catalytic and regulatory proteins controls the metabolism of phospholipid precursors and products.
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                Author and article information

                Contributors
                Xiaojin Song: songxj@qibebt.ac.cn
                Sen Wang: wangsen@qibebt.ac.cn
                Journal
                Journal ID (nlm-ta): Biotechnol Biofuels Bioprod
                Journal ID (iso-abbrev): Biotechnol Biofuels Bioprod
                Title: Biotechnology for Biofuels and Bioproducts
                Publisher: BioMed Central (London )
                ISSN (Electronic): 2731-3654
                Publication date (Electronic): 27 September 2023
                Publication date PMC-release: 27 September 2023
                Publication date Collection: 2023
                Volume: 16
                Electronic Location Identifier: 142
                Affiliations
                [1 ]GRID grid.9227.e, ISNI 0000000119573309, CAS Key Laboratory of Biofuels, Qingdao Institute of Bioenergy and Bioprocess Technology, , Chinese Academy of Sciences, ; No.189 Songling Road, Laoshan District, Qingdao, 266101 Shandong China
                [2 ]Academy of Plateau Science and Sustainability, Qinghai Normal University, ( https://ror.org/03az1t892) Xining, 810016 Qinghai China
                [3 ]GRID grid.458500.c, ISNI 0000 0004 1806 7609, Shandong Provincial Key Laboratory of Energy Genetics, Shandong Engineering Laboratory of Single Cell Oil, , Shandong Energy Institute, ; Qingdao, 266101 Shandong China
                [4 ]Qingdao New Energy Shandong Laboratory, Qingdao Engineering Laboratory of Single Cell Oil, Qingdao, 266101 Shandong China
                [5 ]Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, ( https://ror.org/04rdtx186) Qingdao, 266003 China
                Article
                Publisher ID: 2396
                DOI: 10.1186/s13068-023-02396-y
                PMC ID: 10523756
                PubMed ID: 37752571
                SO-VID: 7b22de35-c6dc-484f-858b-a1f9863e206e
                Copyright © © BioMed Central Ltd., part of Springer Nature 2023
                License:

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

                History
                Date received : 7 June 2023
                Date accepted : 18 September 2023
                Funding
                Funded by: National Natural Science Foundation of China
                Award ID: 42006114
                Award ID: 42106108
                Award ID: 32270045
                Award ID: 32001053
                Award Recipient :
                Funded by: Key Research and Development Program of Shandong Province
                Award ID: 2022SFGC0103
                Funded by: Shandong Province Natural Science Foundation
                Award ID: ZR2020QD099
                Award Recipient :
                Funded by: Shandong Energy Institute
                Award ID: SEI 1202123
                Award Recipient :
                Categories
                Subject: Research
                Custom metadata
                issue-copyright-statement © BioMed Central Ltd., part of Springer Nature 2023

                Keywords: aurantiochytrium,phospholipid:diacylglycerol acyltransferase,triacylglycerol,phospholipids,cell number
                Data availability:
                Keywords: aurantiochytrium, phospholipid:diacylglycerol acyltransferase, triacylglycerol, phospholipids, cell number

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