Phospholipid:diacylglycerol acyltransferase1-overexpression stimulates lipid turnover, oil production and fitness in cold-grown plants.
Phospholipids
/ metabolism
Arabidopsis Proteins
/ genetics
Diacylglycerol O-Acyltransferase
/ genetics
Diglycerides
/ metabolism
Triglycerides
Arabidopsis
/ metabolism
Plants
/ metabolism
Seeds
Plants, Genetically Modified
/ metabolism
Plant Oils
/ metabolism
Carboxylic Ester Hydrolases
/ metabolism
Abiotic stress
Autophagy
Brassicaceae
Cold acclimation
Cold tolerance
Lipid composition
Lipid remodeling
Oilseed biotechnology
Phospholipid:diacylglycerol acyltransferase
Seed yield
Journal
BMC plant biology
ISSN: 1471-2229
Titre abrégé: BMC Plant Biol
Pays: England
ID NLM: 100967807
Informations de publication
Date de publication:
26 Jul 2023
26 Jul 2023
Historique:
received:
06
03
2023
accepted:
12
07
2023
medline:
27
7
2023
pubmed:
26
7
2023
entrez:
25
7
2023
Statut:
epublish
Résumé
Extensive 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. Overexpression 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. Our data suggest that PDAT1 promotes greater vitality in cold-exposed plants, stimulates their longevity and boosts oilseed oil production at low temperature.
Sections du résumé
BACKGROUND
BACKGROUND
Extensive 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.
RESULT
RESULTS
Overexpression 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.
CONCLUSIONS
CONCLUSIONS
Our data suggest that PDAT1 promotes greater vitality in cold-exposed plants, stimulates their longevity and boosts oilseed oil production at low temperature.
Identifiants
pubmed: 37491206
doi: 10.1186/s12870-023-04379-5
pii: 10.1186/s12870-023-04379-5
pmc: PMC10369929
doi:
Substances chimiques
Phospholipids
0
Arabidopsis Proteins
0
Diacylglycerol O-Acyltransferase
EC 2.3.1.20
Diglycerides
0
Triglycerides
0
Plant Oils
0
SDP1 protein, Arabidopsis
EC 3.1.1.3
Carboxylic Ester Hydrolases
EC 3.1.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
370Subventions
Organisme : Narodowe Centrum Nauki
ID : UMO-2017/25/B/NZ3/00721
Informations de copyright
© 2023. The Author(s).
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