All members of the Arabidopsis DGAT and PDAT acyltransferase families operate during high and low temperatures
Issued Date
2024-04-30
Resource Type
eISSN
15322548
Scopus ID
2-s2.0-85192027995
Pubmed ID
38386316
Journal Title
Plant physiology
Volume
195
Issue
1
Start Page
685
End Page
697
Rights Holder(s)
SCOPUS
Bibliographic Citation
Plant physiology Vol.195 No.1 (2024) , 685-697
Suggested Citation
Shomo Z.D., Mahboub S., Vanviratikul H., McCormick M., Tulyananda T., Roston R.L., Warakanont J. All members of the Arabidopsis DGAT and PDAT acyltransferase families operate during high and low temperatures. Plant physiology Vol.195 No.1 (2024) , 685-697. 697. doi:10.1093/plphys/kiae074 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/98284
Title
All members of the Arabidopsis DGAT and PDAT acyltransferase families operate during high and low temperatures
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Corresponding Author(s)
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Abstract
The 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.