title: The TOC159 mutant of Arabidopsis thaliana accumulates altered levels of saturated and polyunsaturated fatty acids.
abstract: We evaluated whether the TOC159 mutant of Arabidopsis called plastid protein import 2-2 (ppi2-2) accumulates normal levels of fatty acids, and transcripts of fatty acid desaturases and galactolipid synthesis enzymes. The ppi2-2 mutant accumulates decreased pigments and total fatty acid content. The MGD1 gene was downregulated and the mutant accumulates decreased levels of monogalactosyldiacylglycerol (MGDG) and 16:3, which suggests that the prokaryotic pathway was impaired in the mutant. The HY5 gene, which encodes long hypocotyl5 transcription factor, was upregulated in the mutant. The DGD1 gene, an HY5 target was marginally increased and the mutant accumulates digalactosyldiacylglycerol at the control level. The mutant had increased expression of 3-ketoacyl-ACP synthase II gene, which encodes a plastid enzyme that elongates 16:0 to 18:0. Interestingly, glycerolipids in the mutant accumulate increased levels of 18:0. A gene that encodes stearoyl-ACP desaturase (SAD) was expressed at the control level and 18:1 was increased, which suggest that SAD may be strongly regulated at the posttranscriptional level. The molar ratio of MGDG to bilayer forming plastid lipids was decreased in the cold-acclimated wild type but not in the ppi2-2 mutant. This indicates that the mutant was unresponsive to cold-stress, and is consistent with increased levels of 18:0, and decreased 16:3 and 18:3 in the ppi2-2 mutant. Overall, these data indicate that a defective Toc159 receptor impaired the synthesis of MGDG, and affected desaturation of 16 and 18-carbon fatty acids. We conclude that expression of the MGD1 gene and synthesis of MGDG are tightly linked to plastid biogenesis.
authors.affiliation: Department of Biological Sciences, Western Illinois University, Waggoner Hall 311, 1 University Circle, Macomb, IL 61455, USA. Electronic address: m-afitlhile@wiu.edu.
authors.forename: Meshack
authors.initials: M
authors.lastname: Afitlhile
authors.affiliation: Department of Biological Sciences, Western Illinois University, Waggoner Hall 311, 1 University Circle, Macomb, IL 61455, USA.
authors.forename: Morgan
authors.initials: M
authors.lastname: Fry
authors.affiliation: Department of Biological Sciences, Western Illinois University, Waggoner Hall 311, 1 University Circle, Macomb, IL 61455, USA.
authors.forename: Samantha
authors.initials: S
authors.lastname: Workman
mesh_terms: D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D050976:Basic-Leucine Zipper Transcription Factors / Q000235:genetics / Q000378:metabolism; D005231:Fatty Acids, Unsaturated / Q000096:biosynthesis* / Q000235:genetics; D038983:Galactolipids / Q000096:biosynthesis / Q000235:genetics; D005700:Galactosyltransferases / Q000235:genetics / Q000378:metabolism; D050356:Lipid Metabolism / Q000502:physiology*; D009154:Mutation; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D018087:Plastids / Q000235:genetics / Q000378:metabolism*
chemical_list: D029681:Arabidopsis Proteins; D050976:Basic-Leucine Zipper Transcription Factors; D005231:Fatty Acids, Unsaturated; D038983:Galactolipids; C109254:HY5 protein, Arabidopsis; D009687:Nuclear Proteins; C007388:digalactosyldiacylglycerol; C009909:monogalactosyldiacylglycerol; C119967:DGD1 protein, Arabidopsis; D005700:Galactosyltransferases; C528622:MGD1 protein, Arabidopsis
keywords: 16:3; 18:0; 18:3; MGD1; MGDG; ppi2-2 mutant