Plastid Glycerol-3-phosphate Acyltransferase Enhanced Plant Growth and Prokaryotic Glycerolipid Synthesis in Brassica napus

Int J Mol Sci. 2020 Jul 27;21(15):5325. doi: 10.3390/ijms21155325.

Abstract

Plastid-localized glycerol-3-phosphate acyltransferase (ATS1) catalyzes the first-step reaction in glycerolipid assembly through transferring an acyl moiety to glycerol-3-phosphate (G3P) to generate lysophosphatidic acid (LPA), an intermediate in lipid metabolism. The effect of ATS1 overexpression on glycerolipid metabolism and growth remained to be elucidated in plants, particularly oil crop plants. Here, we found that overexpression of BnATS1 from Brassica napus enhanced plant growth and prokaryotic glycerolipid biosynthesis. BnATS1 is localized in chloroplasts and an in vitro assay showed that BnATS1 had acylation activity toward glycerol 3-phosphate to produce LPA. Lipid profiling showed that overexpression of BnATS1 led to increases in multiple glycerolipids including phosphatidylglycerol (PG), monogalactosyldiacylglycerol (MGDG), phosphatidylcholine (PC), and phosphatidylinositol (PI), with increased polyunsaturated fatty acids. Moreover, increased MGDG was attributed to the elevation of 34:6- and 34:5-MGDG, which were derived from the prokaryotic pathway. These results suggest that BnATS1 promotes accumulation of polyunsaturated fatty acids in cellular membranes, thus enhances plant growth under low-temperature conditions in Brassica napus.

Keywords: glycerol-3-phosphate acyltransferase; lipid metabolism; plant growth; prokaryotic glycerolipids.

MeSH terms

  • Brassica napus* / genetics
  • Brassica napus* / metabolism
  • Chloroplasts* / genetics
  • Chloroplasts* / metabolism
  • Glycerol-3-Phosphate O-Acyltransferase* / genetics
  • Glycerol-3-Phosphate O-Acyltransferase* / metabolism
  • Glycerophosphates* / biosynthesis
  • Glycerophosphates* / genetics
  • Plant Proteins* / genetics
  • Plant Proteins* / metabolism

Substances

  • Glycerophosphates
  • Plant Proteins
  • Glycerol-3-Phosphate O-Acyltransferase