Complementation of Escherichia coli unc mutant strains by chloroplast and cyanobacterial F1-ATPase subunits

H. Lill*, Andreas Burkovski, Karlheinz Altendorf, Wolfgang Junge, Siegfried Engelbrecht

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review


The genes encoding the five subunits of the F1 portion of the ATPases from both spinach chloroplasts and the cyanobacterium Synechocystis sp. PCC 6803 were cloned into expression vectors and expressed in Escherichia coli. The recombinant subunits formed inclusion bodies within the cells. Each particular subunit was expressed in the respective unc mutant, each unable to grow on non-fermentable carbon sources. The following subunits restored growth under conditions of oxidative phosphorylation: α (both sources, cyanobacterial subunit more than spinach subunit), β (cyanobacterial subunit only), δ (both spinach and Synechocystis), and ε{lunate} (both sources), whereas no growth was achieved with the γ subunits from both sources. Despite a high degree of sequence homology the large subunits α and β of spinach and cyanobacterial F1 were not as effective in the substitution of their E. coli counterparts. On the other hand, the two smallest subunits of the E. coli ATPase could be more effectively replaced by their cyanobacterial or chloroplast counterparts, although the sequence identity or even similarity is very low. We attribute these findings to the different roles of these subunits in F1: The large α and β subunits contribute to the catalytic centers of the enzyme, a function rendering them very sensitive to even minor changes. For the smaller δ and ε{lunate} subunits it was sufficient to maintain a certain tertiary structure during evolution, with little emphasis on the conservation of particular amino acids.

Original languageEnglish
Pages (from-to)278-284
Number of pages7
JournalBiochimica et Biophysica Acta (BBA) - Bioenergetics
Issue number3
Publication statusPublished - 4 Oct 1993
Externally publishedYes


  • (E. coli)
  • (Synechocystis sp. PCC 6803)
  • ATPase, F-
  • Gene complementation
  • Gene expression
  • Mutant strain
  • Mutant strain complementation


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