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Acyltransferases Regulate Oil Quality in Camelina sativa Through Both Acyl Donor and Acyl Acceptor Specificities

Lager, Ida and Jeppsson, Simon and Gippert, Anna-Lena and Feussner, Ivo and Stymne, Sten and Marmon, Sofia (2020). Acyltransferases Regulate Oil Quality in Camelina sativa Through Both Acyl Donor and Acyl Acceptor Specificities. Frontiers in Plant Science. 11 , 1144
[Journal article]

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Abstract

Camelina sativais an emerging biotechnology oil crop. However, more information is needed regarding its innate lipid enzyme specificities. We have therefore characterized several triacylglycerol (TAG) producing enzymes by measuringin vitrosubstrate specificities using different combinations of acyl-acceptors (diacylglycerol, DAG) and donors. Specifically,C. sativaacyl-CoA:diacylglycerol acyltransferase (DGAT) 1 and 2 (which both use acyl-CoA as acyl donor) and phospholipid:diacylglycerol acyltransferase (PDAT, with phosphatidylcoline as acyl donor) were studied. The results show that the DGAT1 and DGAT2 specificities are complementary, with DGAT2 exhibiting a high specificity for acyl acceptors containing only polyunsaturated fatty acids (FAs), whereas DGAT1 prefers acyl donors with saturated and monounsaturated FAs. Furthermore, the combination of substrates that resulted in the highest activity for DGAT2, but very low activity for DGAT1, corresponds to TAG species previously shown to increase inC. sativaseeds with downregulated DGAT1. Similarly, the combinations of substrates that gave the highest PDAT1 activity were also those that produce the two TAG species (54:7 and 54:8 TAG) with the highest increase in PDAT overexpressingC. sativaseeds. Thus, thein vitrodata correlate well with the changes in the overall fatty acid profile and TAG species inC. sativaseeds with altered DGAT1 and PDAT activity. Additionally,in vitrostudies ofC. sativaphosphatidycholine:diacylglycerol cholinephosphotransferase (PDCT), another activity involved in TAG biosynthesis, revealed that PDCT accepts substrates with different desaturation levels. Furthermore, PDCT was unable to use DAG with ricineoleyl groups, and the presence of this substrate also inhibited PDCT from using other DAG-moieties. This gives insights relating to previousin vivostudies regarding this enzyme.

Authors/Creators:Lager, Ida and Jeppsson, Simon and Gippert, Anna-Lena and Feussner, Ivo and Stymne, Sten and Marmon, Sofia
Title:Acyltransferases Regulate Oil Quality in Camelina sativa Through Both Acyl Donor and Acyl Acceptor Specificities
Series Name/Journal:Frontiers in Plant Science
Year of publishing :2020
Volume:11
Article number:1144
Number of Pages:13
Publisher:FRONTIERS MEDIA SA
ISSN:1664-462X
Language:English
Publication Type:Journal article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Biochemistry and Molecular Biology
(A) Swedish standard research categories 2011 > 4 Agricultural Sciences > 404 Agricultural Biotechnology > Plant Biotechnology
Keywords:Camelina, Kennedy pathway, fatty acid composition, acyltransferase, diacylglycerol acyltransferase, diacylglycerol, triacylglycerol, phosphatidylcholine
URN:NBN:urn:nbn:se:slu:epsilon-p-107908
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-107908
Additional ID:
Type of IDID
DOI10.3389/fpls.2020.01144
Web of Science (WoS)000566111700001
ID Code:22675
Faculty:LTV - Fakulteten för landskapsarkitektur, trädgårds- och växtproduktionsvetenskap
Department:(LTJ, LTV) > Department of Plant Breeding (from 130101)
Deposited By: SLUpub Connector
Deposited On:01 Mar 2021 08:43
Metadata Last Modified:01 Mar 2021 08:51

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