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

Author:

Shomo Zachery D1ORCID,Mahboub Samira1,Vanviratikul Hathaichanok2ORCID,McCormick Mason1ORCID,Tulyananda Tatpong3ORCID,Roston Rebecca L1ORCID,Warakanont Jaruswan2ORCID

Affiliation:

1. Center for Plant Science Innovation, Department of Biochemistry, University of Nebraska-Lincoln , Lincoln, NE 68588 , USA

2. Department of Botany, Kasetsart University , Chatuchak, Bangkok 10900 , Thailand

3. School of Bioinnovation and Bio-Based Product Intelligence, Faculty of Science, Mahidol University , Bangkok 10400 , Thailand

Abstract

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.

Funder

National Science Foundation

Nebraska Agricultural Experiment Station

Hatch Multistate Research

USDA National Institute of Food and Agriculture

Kasetsart University Research and Development Institute

National Science and Technology Development Agency

Publisher

Oxford University Press (OUP)

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