Sammanfattning

BackgroundExtensive population growth and climate change accelerate the search for alternative ways of plant-based biomass, biofuel and feed production. Here, we focus on hitherto unknow, new promising cold-stimulated function of phospholipid:diacylglycerol acyltransferase1 (PDAT1) - an enzyme catalyzing the last step of triacylglycerol (TAG) biosynthesis.ResultOverexpression of AtPDAT1 boosted seed yield by 160% in Arabidopsis plants exposed to long-term cold compared to standard conditions. Such seeds increased both their weight and acyl-lipids content. This work also elucidates PDAT1's role in leaves, which was previously unclear. Aerial parts of AtPDAT1-overexpressing plants were characterized by accelerated growth at early and vegetative stages of development and by biomass weighing three times more than control. Overexpression of PDAT1 increased the expression of SUGAR-DEPENDENT1 (SDP1) TAG lipase and enhanced lipid remodeling, driving lipid turnover and influencing biomass increment. This effect was especially pronounced in cold conditions, where the elevated synergistic expression of PDAT1 and SDP1 resulted in double biomass increase compared to standard conditions. Elevated phospholipid remodeling also enhanced autophagy flux in AtPDAT1-overexpresing lines subjected to cold, despite the overall diminished autophagy intensity in cold conditions.ConclusionsOur data suggest that PDAT1 promotes greater vitality in cold-exposed plants, stimulates their longevity and boosts oilseed oil production at low temperature.

Nyckelord

Phospholipid; diacylglycerol acyltransferase; Seed yield; Lipid remodeling; Oilseed biotechnology; Lipid composition; Abiotic stress; Cold tolerance; Cold acclimation; Autophagy; Brassicaceae

Publicerad i

BMC Plant Biology
2023, Volym: 23, nummer: 1, artikelnummer: 370
Utgivare: BMC

SLU författare

• Demski, Kamil

  • Institutionen för växtförädling, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Botanik


Publikationens identifierare

DOI: https://doi.org/10.1186/s12870-023-04379-5

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/123422