Functional divergence of diacylglycerol acyltransferases in the unicellular green alga Haematococcus pluvialis

© The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 72(2021), 2 vom: 02. Feb., Seite 510-524
1. Verfasser: Ma, Haiyan (VerfasserIn)
Weitere Verfasser: Wu, Xiaoying, Wei, Ziwang, Zhao, Liang, Li, Zhongze, Liang, Qing, Zheng, Jie, Wang, Yu, Li, Yanhua, Huang, Linfei, Hu, Qiang, Han, Danxiang
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Acyl-CoA:diacylglycerol acyltransferase (DGAT) functional divergence and convergence lipids lysophosphatidic acyltransferase (LPAAT) microalgae triacylglycerol biosynthesis Diglycerides Triglycerides mehr... Acyltransferases EC 2.3.- Diacylglycerol O-Acyltransferase EC 2.3.1.20
LEADER 01000naa a22002652 4500
001 NLM315763051
003 DE-627
005 20231225155622.0
007 cr uuu---uuuuu
008 231225s2021 xx |||||o 00| ||eng c
024 7 |a 10.1093/jxb/eraa451  |2 doi 
028 5 2 |a pubmed24n1052.xml 
035 |a (DE-627)NLM315763051 
035 |a (NLM)33005924 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Ma, Haiyan  |e verfasserin  |4 aut 
245 1 0 |a Functional divergence of diacylglycerol acyltransferases in the unicellular green alga Haematococcus pluvialis 
264 1 |c 2021 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 13.05.2021 
500 |a Date Revised 13.05.2021 
500 |a published: Print 
500 |a Citation Status MEDLINE 
520 |a © The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. 
520 |a Acyl-CoA:diacylglycerol acyltransferase (DGAT) catalyzes the final committed step in triacylglycerol biosynthesis in eukaryotes. In microalgae, the copy number of DGAT genes is extraordinarily expanded, yet the functions of many DGATs remain largely unknown. This study revealed that microalgal DGAT can function as a lysophosphatidic acyltransferase (LPAAT) both in vitro and in vivo while losing its original function as DGAT. Among the five DGAT-encoding genes identified and cloned from the green microalga Haematococcus pluvialis, four encoded HpDGATs that showed triacylglycerol synthase activities in yeast functional complementation analyses; the exception was one of the type II DGAT encoding genes, HpDGTT2. The hydrophobic recombinant HpDGTT2 protein was purified in soluble form and was found to function as a LPAAT via enzymatic assay. Introducing this gene into the green microalga Chlamydomonas reinhardtii led to retarded cellular growth, enlarged cell size, and enhanced triacylglycerol accumulation, identical to the phenotypes of transgenic strains overexpressing CrLPAAT. This study provides a framework for dissecting uncharacterized DGATs, and could pave the way to decrypting the structure-function relationship of this large group of enzymes that are critical to lipid biosynthesis 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Acyl-CoA:diacylglycerol acyltransferase (DGAT) 
650 4 |a functional divergence and convergence 
650 4 |a lipids 
650 4 |a lysophosphatidic acyltransferase (LPAAT) 
650 4 |a microalgae 
650 4 |a triacylglycerol biosynthesis 
650 7 |a Diglycerides  |2 NLM 
650 7 |a Triglycerides  |2 NLM 
650 7 |a Acyltransferases  |2 NLM 
650 7 |a EC 2.3.-  |2 NLM 
650 7 |a Diacylglycerol O-Acyltransferase  |2 NLM 
650 7 |a EC 2.3.1.20  |2 NLM 
700 1 |a Wu, Xiaoying  |e verfasserin  |4 aut 
700 1 |a Wei, Ziwang  |e verfasserin  |4 aut 
700 1 |a Zhao, Liang  |e verfasserin  |4 aut 
700 1 |a Li, Zhongze  |e verfasserin  |4 aut 
700 1 |a Liang, Qing  |e verfasserin  |4 aut 
700 1 |a Zheng, Jie  |e verfasserin  |4 aut 
700 1 |a Wang, Yu  |e verfasserin  |4 aut 
700 1 |a Li, Yanhua  |e verfasserin  |4 aut 
700 1 |a Huang, Linfei  |e verfasserin  |4 aut 
700 1 |a Hu, Qiang  |e verfasserin  |4 aut 
700 1 |a Han, Danxiang  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Journal of experimental botany  |d 1985  |g 72(2021), 2 vom: 02. Feb., Seite 510-524  |w (DE-627)NLM098182706  |x 1460-2431  |7 nnns 
773 1 8 |g volume:72  |g year:2021  |g number:2  |g day:02  |g month:02  |g pages:510-524 
856 4 0 |u http://dx.doi.org/10.1093/jxb/eraa451  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 72  |j 2021  |e 2  |b 02  |c 02  |h 510-524