Two plastidial lysophosphatidic acid acyltransferases differentially mediate the biosynthesis of membrane lipids and triacylglycerols in Phaeodactylum tricornutum
文献类型： 外文期刊
作者： You, Lingjie 1 ; Polonska, Ada 2 ; Jasieniecka-Gazarkiewicz, Katarzyna 2 ; Richard, Fabien 3 ; Jouhet, Juliette 3 ; Marechal, Eric 3 ; Banas, Antoni 2 ; Hu, Hanhua 4 ; Pan, Yufang 4 ; Hao, Xiahui 1 ; Jin, Hu 5 ; Allen, Andrew E. 6 ; Amato, Alberto 3 ; Gong, Yangmin 1 ;
作者机构： 1.Chinese Acad Agr Sci, Oil Crops Res Inst, Wuhan 430062, Peoples R China
2.Intercollegiate Fac Biotechnol UG & MUG, PL-80307 Gdansk, Poland
3.Univ Grenoble Alpes, CNRS, Unite Mixte Rech 5168, Lab Physiol Cellulaire & Vegetale,Commissariata En, F-38041 Grenoble, France
4.Chinese Acad Sci, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China
5.Chinese Acad Sci, Ctr Microalgal Biotechnol & Biofuels, Inst Hydrobiol, Wuhan 430072, Peoples R China
6.Univ Calif San Diego, Scripps Inst Oceanog, La Jolla, CA 92093 USA
7.J Craig Venter Inst, 4120 Capricorn Lane, La Jolla, CA 92037 USA
8.Chinese Acad Agr Sci, Minist Agr, Oil Crops Res Inst, Key Lab Biol & Genet Improvement Oil Crops, Wuhan 430062, Peoples R China
关键词： chloroplast membrane lipids; lysophosphatidic acid acyltransferase; multiplexed CRISPR/Cas9; Phaeodactylum tricornutum; triacylglycerol
期刊名称：NEW PHYTOLOGIST （ 影响因子：9.4； 五年影响因子：10.5 ）
ISSN： 0028-646X
年卷期： 2023 年
页码：
收录情况： SCI
摘要： Lysophosphatidic acid acyltransferases (LPAATs) catalyze the formation of phosphatidic acid (PA), a central metabolite in both prokaryotic and eukaryotic organisms for glycerolipid biosynthesis. Phaeodactylum tricornutum contains at least two plastid-localized LPAATs (ptATS2a and ptATS2b), but their roles in lipid synthesis remain unknown. Both ptATS2a and ptATS2b could complement the high temperature sensitivity of the bacterial plsC mutant deficient in LPAAT. In vitro enzyme assays showed that they prefer lysophosphatidic acid over other lysophospholipids. ptATS2a is localized in the plastid inner envelope membrane and CRISPR/Cas9-generated ptATS2a mutants showed compromised cell growth, significantly changed plastid and extra-plastidial membrane lipids at nitrogen-replete condition and reduced triacylglycerols (TAGs) under nitrogen-depleted condition. ptATS2b is localized in thylakoid membranes and its knockout led to reduced growth rate and TAG content but slightly altered molecular composition of membrane lipids. The changes in glycerolipid profiles are consistent with the role of both LPAATs in the sn-2 acylation of sn-1-acyl-glycerol-3-phosphate substrates harboring 20:5 at the sn-1 position. Our findings suggest that both LPAATs are important for membrane lipids and TAG biosynthesis in P. tricornutum and further highlight that 20:5-Lyso-PA is likely involved in the massive import of 20:5 back to the plastid to feed plastid glycerolipid syntheses.
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