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Theunc operon ofEscherichia coli was split into two fragments by the restriction endonucleaseHin dIII. The operator-proximal portion was cloned into plasmid pACYC184, forming plasmid pAN51, which included the genesuncB, uncE , anduncA . When plasmid pAN51 was used as template in an in vitro transcription/translation system, the α subunit (from theuncA gene) and δ subunit of the F1 adenosine triphosphatase (ATPase) were formed. In addition, three polypeptides of molecular weights 18,000, 17,000, and 14,000 were formed, and the significance of these polypeptides is discussed. The operator-distal portion of theunc operon was also cloned into plasmid pACYC184, forming plasmid pAN36, which included theuncD anduncC genes. When this plasmid was used as template in an in vitro transcription/translation system, the β subunit (from theuncD gene) and the ε subunit (from theuncC gene) of the F1 ATPase were formed. A polypeptide of a molecular weight similar to the ε subunit but of different net charge was also formed. Plasmid pAN45, carrying the completeunc operon, was isolated after digestion of a mixture of plasmids pAN51 and pAN36 with the restriction endonucleaseHin dIII and then religation with T4 deoxyribonucleic acid ligase. It was concluded that aHin dIII restriction site occurred within the newly describeduncG gene, which was shown, by complementation studies with Mu-induced mutants, to be located between theuncA anduncD genes to give the gene orderuncBEAGDC . TheuncG gene appears to code for the γ subunit of the F1 ATPase.

Subunits of the Adenosine Triphosphatase Complex Translated In Vitro from the Escherichia coli unc Operon