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dc.contributor.authorRau, E-Ming
dc.contributor.authorBartosova, Zdenka
dc.contributor.authorKristiansen, Kåre Andre
dc.contributor.authorAasen, Inga Marie
dc.contributor.authorBruheim, Per
dc.contributor.authorErtesvåg, Helga
dc.date.accessioned2022-06-16T08:22:37Z
dc.date.available2022-06-16T08:22:37Z
dc.date.created2022-02-03T15:56:50Z
dc.date.issued2022
dc.identifier.citationFrontiers in Microbiology, 2022, 13, 1-13en_US
dc.identifier.issn1664-302X
dc.identifier.urihttps://hdl.handle.net/11250/2999002
dc.description.abstractThraustochytrids are heterotrophic marine eukaryotes known to accumulate large amounts of triacylglycerols, and they also synthesize terpenoids like carotenoids and squalene, which all have an increasing market demand. However, a more extensive knowledge of the lipid metabolism is needed to develop thraustochytrids for profitable biomanufacturing. In this study, two putative type-2 Acyl-CoA:diacylglycerol acyltransferases (DGAT2) genes of Aurantiochytrium sp. T66, T66ASATa, and T66ASATb, and their homologs in Aurantiochytrium limacinum SR21, AlASATa and AlASATb, were characterized. In A. limacinum SR21, genomic knockout of AlASATb reduced the amount of the steryl esters of palmitic acid, SE (16:0), and docosahexaenoic acid, SE (22:6). The double mutant of AlASATa and AlASATb produced even less of these steryl esters. The expression and overexpression of T66ASATb and AlASATb, respectively, enhanced SE (16:0) and SE (22:6) production more significantly than those of T66ASATa and AlASATa. In contrast, these mutations did not significantly change the level of triacylglycerols or other lipid classes. The results suggest that the four genes encoded proteins possessing acyl-CoA:sterol acyltransferase (ASAT) activity synthesizing both SE (16:0) and SE (22:6), but with the contribution from AlASATb and T66ASATb being more important than that of AlASATa and T66ASATa. Furthermore, the expression and overexpression of T66ASATb and AlASATb enhanced squalene accumulation in SR21 by up to 88%. The discovery highlights the functional diversity of DGAT2-like proteins and provides valuable information on steryl ester and squalene synthesis in thraustochytrids, paving the way to enhance squalene production through metabolic engineering.en_US
dc.language.isoengen_US
dc.publisherFrontiersen_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.subjectdocosahexaenoic aciden_US
dc.subjectsqualene,en_US
dc.subjectsterol acyltransferasesen_US
dc.subjectdiacylglycerol acyltransferaseen_US
dc.subjectsteryl estersen_US
dc.subjectthraustochytridsen_US
dc.subjectAurantiochytriumen_US
dc.titleOverexpression of two new acyl-CoA:diacylglycerol acyltransferase 2-like acyl-CoA:sterol acyltransferases enhanced squalene accumulation in Aurantiochytrium limacinumen_US
dc.typePeer revieweden_US
dc.typeJournal articleen_US
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright © 2022 Rau, Bartosova, Kristiansen, Aasen, Bruheim and Ertesvåg. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.en_US
dc.source.pagenumber13en_US
dc.source.volume13en_US
dc.source.journalFrontiers in Microbiologyen_US
dc.identifier.doi10.3389/fmicb.2022.822254
dc.identifier.cristin1997509
dc.relation.projectNorges forskningsråd: 269432en_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode2


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