Structural analysis of the isolated chloroplast coupling factor and the N,N'-dicyclohexylcarbodiimide binding proteolipid

J. E. Mullet, U. Pick, C. J. Arntzen

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

Negative staining of purified spinach dicyclohexylcarbodiimide (DCCD) sensitive ATPase revealed a population of 110 Å subunits attached by stalks to short string-like aggregates. The interpretation of these data is that 110 Å CF1 are attached by stalks to an aggregate of CF0. The CF1-CF0 complex was incorporated into phospholipid vesicles; freezefracture analysis of this preparation revealed a homogeneous population of particles spanning the lipid bilayer; these averaged 96 Å in diameter. The DCCD binding proteolipid (apparent molecular weight 7500), an integral component of CF0, was isolated from membranes by butanol extraction and was incorporated rated into phospholipid vesicles. Freeze-fracture analysis of the DCCD-binding proteolipid/vesicle preparation revealed a population of particles averaging 83 Å in diameter suggesting that the DCCD-binding proteolipid self-associates in lipid to form a stable complex. This complex may be required for proton transport across chloroplast membranes in vivo. The size difference between CF0 and DCCD-proteolipid freeze-fracture particles may be related to differences in polypeptide composition of the two complexes.

Original languageEnglish (US)
Pages (from-to)149-157
Number of pages9
JournalBBA - Biomembranes
Volume642
Issue number1
DOIs
StatePublished - Mar 20 1981

Keywords

  • (Chloroplast)
  • ATPase
  • Coupling factor
  • Dicyclohexylcarbodiimide
  • Proteolipid
  • Reconstitution

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

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