Mutation of the TGD1 Chloroplast Envelope Protein Affects Phosphatidate Metabolism in<i>Arabidopsis</i>

DOI PDF 10 Citations
  • Changcheng Xu
    Department of Biochemistry and Molecular Biology  Michigan State University  East Lansing  Michigan 48824
  • Jilian Fan
    Department of Biochemistry and Molecular Biology  Michigan State University  East Lansing  Michigan 48824
  • John E. Froehlich
    Department of Energy  Plant Research Laboratory  Michigan State University  East Lansing  Michigan  48824
  • Koichiro Awai
    Department of Biochemistry and Molecular Biology  Michigan State University  East Lansing  Michigan 48824
  • Christoph Benning
    Department of Biochemistry and Molecular Biology  Michigan State University  East Lansing  Michigan 48824

Description

<jats:title>Abstract</jats:title><jats:p>Phosphatidate (PA) is a central metabolite of lipid metabolism and a signaling molecule in many eukaryotes, including plants. Mutations in a permease-like protein, TRIGALACTOSYLDIACYLGLYCEROL1 (TGD1), in Arabidopsis thaliana caused the accumulation of triacylglycerols, oligogalactolipids, and PA. Chloroplast lipids were altered in their fatty acid composition consistent with an impairment of lipid trafficking from the endoplasmic reticulum (ER) to the chloroplast and a disruption of thylakoid lipid biosynthesis from ER-derived precursors. The process mediated by TGD1 appears to be essential as mutation of the protein caused a high incidence of embryo abortion. Isolated tgd1 mutant chloroplasts showed a decreased ability to incorporate PA into galactolipids. The TGD1 protein was localized to the inner chloroplast envelope and appears to be a component of a lipid transporter. As even partial disruption of TGD1 function has drastic consequences on central lipid metabolism, the tgd1 mutant provides a tool to explore regulatory mechanisms governing lipid homeostasis and lipid trafficking in plants.</jats:p>

Journal

  • The Plant Cell

    The Plant Cell 17 (11), 3094-3110, 2005-09-30

    Oxford University Press (OUP)

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