The pds2 mutation is a lesion in the Arabidopsis homogentisate solanesyltransferase gene involved in plastoquinone biosynthesis

Li Tian, Dean DellaPenna, Richard A. Dixon

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

Plastoquinone plays critical roles in photosynthesis, chlororespiration and carotenoid biosynthesis. The previously isolated pds2 mutant from Arabidopsis was deficient in tocopherol and plastoquinone accumulation, and the biochemical phenotype of this mutant could not be reversed by externally applied homogentisate, suggesting a later step in tocopherol and/or plastoquinone biosynthesis had been disrupted. Recently, the protein encoded by At3g11950 (AtHST) was shown to condense homogentisate with solanesyl diphosphate (SDP), the substrate for plastoquinone synthesis, but not phytyl diphosphate (PDP), the substrate for tocopherol biosynthesis. We have sequenced the AtHST allele in the pds2 mutant background and identified an in-frame 6 bp (2 aa) deletion in the gene. The pds2 mutation could be functionally complemented by constitutive expression of AtHST, demonstrating that the molecular basis for the pds2 mutation is this 6 bp-lesion in the AtHST gene. Confocal microscopy of EGFP tagged AtHST suggested that AtHST is localized to the chloroplast envelope, supporting the hypothesis that plastoquinone synthesis occurs in the plastid.

Original languageEnglish (US)
Pages (from-to)1067-1073
Number of pages7
JournalPlanta
Volume226
Issue number4
DOIs
StatePublished - Sep 2007
Externally publishedYes

Keywords

  • Homogentisate
  • pds2
  • Plastoquinone
  • Prenyltransferase
  • Solanesyl diphosphate

ASJC Scopus subject areas

  • Plant Science

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