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All members of the Arabidopsis DGAT and PDAT acyltransferase families operate during high and low temperatures.
Shomo, Zachery D; Mahboub, Samira; Vanviratikul, Hathaichanok; McCormick, Mason; Tulyananda, Tatpong; Roston, Rebecca L; Warakanont, Jaruswan.
Afiliación
  • Shomo ZD; Center for Plant Science Innovation, Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE 68588, USA.
  • Mahboub S; Center for Plant Science Innovation, Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE 68588, USA.
  • Vanviratikul H; Department of Botany, Kasetsart University, Chatuchak, Bangkok 10900, Thailand.
  • McCormick M; Center for Plant Science Innovation, Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE 68588, USA.
  • Tulyananda T; School of Bioinnovation and Bio-Based Product Intelligence, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.
  • Roston RL; Center for Plant Science Innovation, Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, NE 68588, USA.
  • Warakanont J; Department of Botany, Kasetsart University, Chatuchak, Bangkok 10900, Thailand.
Plant Physiol ; 195(1): 685-697, 2024 Apr 30.
Article en En | MEDLINE | ID: mdl-38386316
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 PHOSPHOLIPIDDIACYLGLYCEROL 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.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Triglicéridos / Aciltransferasas / Arabidopsis / Frío / Proteínas de Arabidopsis / Diacilglicerol O-Acetiltransferasa Idioma: En Revista: Plant Physiol Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Triglicéridos / Aciltransferasas / Arabidopsis / Frío / Proteínas de Arabidopsis / Diacilglicerol O-Acetiltransferasa Idioma: En Revista: Plant Physiol Año: 2024 Tipo del documento: Article País de afiliación: Estados Unidos