All members of the Arabidopsis DGAT and PDAT acyltransferase families operate during high and low temperatures

dc.contributor.authorShomo Z.D.
dc.contributor.authorMahboub S.
dc.contributor.authorVanviratikul H.
dc.contributor.authorMcCormick M.
dc.contributor.authorTulyananda T.
dc.contributor.authorRoston R.L.
dc.contributor.authorWarakanont J.
dc.contributor.correspondenceShomo Z.D.
dc.contributor.otherMahidol University
dc.date.accessioned2024-05-09T18:34:27Z
dc.date.available2024-05-09T18:34:27Z
dc.date.issued2024-04-30
dc.description.abstractThe accumulation of triacylglycerol (TAG) in vegetative tissues is necessary to adapt to changing temperatures. It has been hypothesized that TAG accumulation is required as a storage location for maladaptive membrane lipids. The TAG acyltransferase family has five members (DIACYLGLYCEROL ACYLTRANSFERSE1/2/3 and PHOSPHOLIPID:DIACYLGLYCEROL ACYLTRANSFERASE1/2), and their individual roles during temperature challenges have either been described conflictingly or not at all. Therefore, we used Arabidopsis (Arabidopsis thaliana) loss of function mutants in each acyltransferase to investigate the effects of temperature challenge on TAG accumulation, plasma membrane integrity, and temperature tolerance. All mutants were tested under one high- and two low-temperature regimens, during which we quantified lipids, assessed temperature sensitivity, and measured plasma membrane electrolyte leakage. Our findings revealed reduced effectiveness in TAG production during at least one temperature regimen for all acyltransferase mutants compared to the wild type, resolved conflicting roles of pdat1 and dgat1 by demonstrating their distinct temperature-specific actions, and uncovered that plasma membrane integrity and TAG accumulation do not always coincide, suggesting a multifaceted role of TAG beyond its conventional lipid reservoir function during temperature stress.
dc.identifier.citationPlant physiology Vol.195 No.1 (2024) , 685-697
dc.identifier.doi10.1093/plphys/kiae074
dc.identifier.eissn15322548
dc.identifier.pmid38386316
dc.identifier.scopus2-s2.0-85192027995
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/98284
dc.rights.holderSCOPUS
dc.subjectBiochemistry, Genetics and Molecular Biology
dc.subjectAgricultural and Biological Sciences
dc.titleAll members of the Arabidopsis DGAT and PDAT acyltransferase families operate during high and low temperatures
dc.typeArticle
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85192027995&origin=inward
oaire.citation.endPage697
oaire.citation.issue1
oaire.citation.startPage685
oaire.citation.titlePlant physiology
oaire.citation.volume195
oairecerif.author.affiliationUniversity of Nebraska–Lincoln
oairecerif.author.affiliationKasetsart University
oairecerif.author.affiliationMahidol University

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