气候变化领域集成服务门户(CCPortal): Endoplasmic reticulum acyltransferase with prokaryotic substrate preference contributes to triacylglycerol assembly in Chlamydomonas

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DOI	10.1073/pnas.1715922115
	Endoplasmic reticulum acyltransferase with prokaryotic substrate preference contributes to triacylglycerol assembly in Chlamydomonas
	Kim Y.; Terng E.L.; Riekhof W.R.; Cahoon E.B.; Cerutti H.
发表日期	2018
ISSN	0027-8424
起始页码	1652
结束页码	1657
卷号	115 期号:7
英文摘要	Understanding the unique features of triacylglycerol (TAG) metabolism in microalgae may be necessary to realize the full potential of these organisms for biofuel and biomaterial production. In the unicellular green alga Chlamydomonas reinhardtii a chloroplastic (prokaryotic) pathway has been proposed to play a major role in TAG precursor biosynthesis. However, as reported here, C. reinhardtii contains a chlorophyte-specific lysophosphatidic acid acyltransferase, CrLPAAT2, that localizes to endoplasmic reticulum (ER) membranes. Unlike canonical, ER-located LPAATs, CrLPAAT2 prefers palmitoyl-CoA over oleoyl-CoA as the acyl donor substrate. RNA-mediated suppression of CrLPAAT2 indicated that the enzyme is required for TAG accumulation under nitrogen deprivation. Our findings suggest that Chlamydomonas has a distinct glycerolipid assembly pathway that relies on CrLPAAT2 to generate prokaryotic-like TAG precursors in the ER. © 2018 National Academy of Sciences. All Rights Reserved.
英文关键词	Algae; Biofuels; Lipid droplets; LPAAT; Triacylglycerol metabolism
语种	英语
scopus关键词	acyl donor substrate; acyltransferase; chlorophyte specific lysophosphatidic acid acyltransferase; lysophosphatidic acid acyltransferase; oleoyl coenzyme A; palmitoyl coenzyme A hydrolase; RNA; triacylglycerol; unclassified drug; acyltransferase; algal protein; triacylglycerol; Article; Chlamydomonas reinhardtii; controlled study; endoplasmic reticulum membrane; enzyme localization; enzyme repression; enzyme substrate; glycerolipid assembly; lipid composition; nitrogen deficiency; nitrogen deprivation; nonhuman; priority journal; prokaryote; prokaryotic substrate preference; protein assembly; signal transduction; Chlamydomonas reinhardtii; chloroplast; endoplasmic reticulum; enzyme specificity; growth, development and aging; metabolism; phylogeny; Acyltransferases; Algal Proteins; Chlamydomonas reinhardtii; Chloroplasts; Endoplasmic Reticulum; Phylogeny; Substrate Specificity; Triglycerides
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160544
作者单位	Kim, Y., School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States, Center for Plant Science Innovation, University of Nebraska-Lincoln, Lincoln, NE 68588, United States; Terng, E.L., School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States, Center for Plant Science Innovation, University of Nebraska-Lincoln, Lincoln, NE 68588, United States; Riekhof, W.R., School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States; Cahoon, E.B., Center for Plant Science Innovation, University of Nebraska-Lincoln, Lincoln, NE 68588, United States, Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE 68588, United States; Cerutti, H., School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE 68588, United States, Center for Plant Science Innovation, University of Nebraska-Lincoln, Lincoln, NE 68588, United States
推荐引用方式 GB/T 7714	Kim Y.,Terng E.L.,Riekhof W.R.,et al. Endoplasmic reticulum acyltransferase with prokaryotic substrate preference contributes to triacylglycerol assembly in Chlamydomonas[J],2018,115(7).
APA	Kim Y.,Terng E.L.,Riekhof W.R.,Cahoon E.B.,&Cerutti H..(2018).Endoplasmic reticulum acyltransferase with prokaryotic substrate preference contributes to triacylglycerol assembly in Chlamydomonas.Proceedings of the National Academy of Sciences of the United States of America,115(7).
MLA	Kim Y.,et al."Endoplasmic reticulum acyltransferase with prokaryotic substrate preference contributes to triacylglycerol assembly in Chlamydomonas".Proceedings of the National Academy of Sciences of the United States of America 115.7(2018).