Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP-synthase

Petra Fromme, Peter Gräber, Johann Salnikow

Research output: Contribution to journalArticle

38 Scopus citations

Abstract

The subunit composition of highly active purified ATP-synthase from chloroplasts, CF0F1, was investigated by SDS gel electrophoresis. An additional subunit of CF0, was detected with an apparent molecular mass of 20 kDa. It is stained weakly with Coomassie blue but very strongly with silver. This subunit was isolated on a preparative SDS gel and the N-terminal amino acid sequence analyzed. It shows that the 20 kDa protein is identical with the protein encoded by the spinach chloroplast gene atpI, called subunit IV [(1986) Mol. Genet. 203, 117-128]. However, in comparison to the gene-derived sequence, the first 18 amino acids are missing, indicating N-terminal processing.

Original languageEnglish (US)
Pages (from-to)27-30
Number of pages4
JournalFEBS Letters
Volume218
Issue number1
DOIs
StatePublished - Jun 22 1987
Externally publishedYes

Keywords

  • ATP-synthase
  • Amino acid sequence
  • CF subunit
  • CFF
  • Chloroplast

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP-synthase'. Together they form a unique fingerprint.

  • Cite this