globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1715922115
论文题名:
Endoplasmic reticulum acyltransferase with prokaryotic substrate preference contributes to triacylglycerol assembly in Chlamydomonas
作者: Kim Y.; Terng E.L.; Riekhof W.R.; Cahoon E.B.; Cerutti H.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期:7
起始页码: 1652
结束页码: 1657
语种: 英语
英文关键词: Algae ; Biofuels ; Lipid droplets ; LPAAT ; Triacylglycerol metabolism
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
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.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163742
Appears in Collections:气候变化与战略

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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

Recommended Citation:
Kim Y.,Terng E.L.,Riekhof W.R.,et al. Endoplasmic reticulum acyltransferase with prokaryotic substrate preference contributes to triacylglycerol assembly in Chlamydomonas[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(7)
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