THE F1 GENES OF THE F1F0 ATP SYNTHASE FROM THE ACIDOPHILIC BACTERIUM THIOBACILLUS-FERROOXIDANS COMPLEMENT ESCHERICHIA-COLI F1 UNC MUTANTS

An atp gene cluster from the extreme acidophile Thiobacillus ferrooxidans was able to complement Escherichia coli F-1 unc mutants for growth on minimal medium plus succinate. Complementation with all four E. coli F-1 mutants tested was observed and subunits for the F-1 portion of the T. ferrooxidans ATP synthase formed a functional association with the F-0 subunits of the E. coli enzyme. In addition, a hybrid F-1 enzyme in which some units were derived from E. coli and some from T. ferrooxidans was partially functional. No clones capable of complementing E. coli F-0 unc mutants were isolated. The nucleotide sequence of the gene cluster was determined and the genes for the F-0 and the F-1 ATP synthase subunits were found to be physically linked.