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 Citations (Scopus)

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
Pages (from-to)27-30
Number of pages4
JournalFEBS Letters
Volume218
Issue number1
DOIs
Publication statusPublished - Jun 22 1987

Fingerprint

Chloroplast Proton-Translocating ATPases
Genes
Gels
Chloroplast Genes
Membranes
Viverridae
Amino Acids
Spinacia oleracea
Molecular mass
Electrophoresis
Silver
Amino Acid Sequence
Proteins
Processing
Chemical analysis

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP-synthase. / Fromme, Petra; Gräber, Peter; Salnikow, Johann.

In: FEBS Letters, Vol. 218, No. 1, 22.06.1987, p. 27-30.

Research output: Contribution to journalArticle

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