title: Role of aminoalcoholphosphotransferases 1 and 2 in phospholipid homeostasis in Arabidopsis.
abstract: Aminoalcoholphosphotransferase (AAPT) catalyzes the synthesis of phosphatidylcholine (PC) and phosphotidylethanolamine (PE), which are the most prevalent membrane phospholipids in all eukaryotic cells. Here, we show that suppression of AAPTs results in extensive membrane phospholipid remodeling in Arabidopsis thaliana. Double knockout (KO) mutants that are hemizygous for either aapt1 or aapt2 display impaired pollen and seed development, leading to embryotic lethality of the double KO plants, whereas aapt1 or aapt2 single KO plants show no overt phenotypic alterations. The growth rate and seed yield of AAPT RNA interference (RNAi) plants are greatly reduced. Lipid profiling shows decreased total galactolipid and phospholipid content in aapt1-containing mutants, including aapt1, aapt1/aapt1 aapt2/AAPT2, aapt1/AAPT1 aapt2/aapt2, and AAPT RNAi plants. The level of PC in leaves was unchanged, whereas that of PE was reduced in all AAPT-deficient plants, except aapt2 KO. However, the acyl species of PC was altered, with increased levels of C34 species and decreased C36 species. Conversely, the levels of PE and phosphatidylinositol were decreased in C34 species. In seeds, all AAPT-deficient plants, including aapt2 KO, displayed a decrease in PE. The data show that AAPT1 and AAPT2 are essential to plant vegetative growth and reproduction and have overlapping functions but that AAPT1 contributes more than AAPT2 to PC production in vegetative tissues. The opposite changes in molecular species between PC and PE and unchanged PC level indicate the existence of additional pathways that maintain homeostatic levels of PC, which are crucial for the survival and proper development of plants.
authors.affiliation: Department of Biology, University of Missouri, St. Louis, Missouri 63121 Donald Danforth Plant Science Center, St. Louis, Missouri 63132.
authors.forename: Yu
authors.identifier: http://orcid.org/0000-0002-8813-9511
authors.initials: Y
authors.lastname: Liu
authors.affiliation: Department of Biology, University of Missouri, St. Louis, Missouri 63121 Donald Danforth Plant Science Center, St. Louis, Missouri 63132.
authors.forename: Geliang
authors.initials: G
authors.lastname: Wang
authors.affiliation: Department of Biology, University of Missouri, St. Louis, Missouri 63121 Donald Danforth Plant Science Center, St. Louis, Missouri 63132 swang@danforthcenter.org.
authors.forename: Xuemin
authors.identifier: http://orcid.org/0000-0002-6251-6745
authors.initials: X
authors.lastname: Wang
mesh_terms: D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development / Q000502:physiology; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D006706:Homeostasis; D009154:Mutation; D010713:Phosphatidylcholines / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism*; D010770:Phosphotransferases / Q000235:genetics / Q000378:metabolism*; D018515:Plant Leaves / Q000201:enzymology / Q000235:genetics / Q000254:growth & development / Q000502:physiology; D030821:Plants, Genetically Modified; D011058:Pollen / Q000201:enzymology / Q000235:genetics / Q000254:growth & development; D012098:Reproduction; D012639:Seeds / Q000201:enzymology / Q000235:genetics / Q000254:growth & development / Q000502:physiology
chemical_list: D029681:Arabidopsis Proteins; D010713:Phosphatidylcholines; D010743:Phospholipids; D010770:Phosphotransferases; C423366:aminoalcoholphosphotransferase