Reassembly of Synechocystis sp. PCC 6803 F1-ATPase from its over-expressed subunits

D. Steinemann, Siegfried Engelbrecht, H Lill

Research output: Contribution to JournalArticleAcademicpeer-review


Subunits alpha, beta, and gamma of the F1-part of cyanobacterial F0F1-ATPase have been cloned into expression vectors. Over-expressed subunit beta was found soluble in the cytoplasmic fraction of Escherichia coli cells under appropriate culture and induction conditions and was purified from cell extracts. Recombinant alpha and gamma subunits precipitated into inclusion bodies and had to be solubilized, purified and refolded. The correct folding and functional integrity of the alpha and beta subunits was monitored by their ability to bind nucleotides. Active cyanobacterial F1-ATPase was assembled from its purified subunits alpha, beta, gamma, delta and epsilon. The reassembled enzyme reconstituted ATP synthesis in F1-depleted thylakoid membranes of Synechocystis sp. PCC 6803 and hydrolyzed ATP.

Original languageEnglish
Pages (from-to)171-4
Number of pages4
JournalFEBS Letters
Issue number2
Publication statusPublished - 3 Apr 1995


  • Adenosine Triphosphate
  • Binding Sites
  • Cloning, Molecular
  • Cyanobacteria
  • Electrophoresis, Polyacrylamide Gel
  • Gene Expression
  • Genetic Vectors
  • Macromolecular Substances
  • Protein Folding
  • Proton-Translocating ATPases
  • Recombinant Proteins
  • Journal Article
  • Research Support, Non-U.S. Gov't


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