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J Bacteriol. 1979 February; 137(2): 711-718
Copyright © 1979, American Society for Microbiology. All Rights Reserved.

A Fifth Gene (uncE) in the Operon Concerned with Oxidative Phosphorylation in Escherichia coli

¹ Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, A.C.T. Australia 2601

ABSTRACT

Three mutant unc alleles (unc-408, unc-410, and unc-429) affecting the coupling of electron transport to oxidative phosphorylation in Escherichia coli K-12 have been characterized. Genetic complementation analyses using previously defined mutant unc alleles indicated that the new mutant unc alleles affect a previously undescribed gene designated uncE. The phenotype of strains carrying the uncE408 or uncE429 allele is similar in that Mg²⁺-adenosine triphosphatase activity is only found in the cytoplasmic fraction, and membranes do not bind the F₁ portion of adenosine triphosphatase purified from a normal strain. In contrast, adenosine triphosphatase activity is present both in the cytoplasm and on the membranes from a strain carrying the unc-410 allele, and normal F₁ binds to F₁-depleted membranes from this strain. The adenosine triphosphatase solubilized from membranes of a strain carrying the unc-410 allele reconstituted ATP-dependent membrane energization in F₁-depleted membranes from a normal strain. Genetic complementation tests using various Mu-induced unc alleles in partial diploid strains show that the uncE gene is in the unc operon and that the order of genes is uncB E A D C. The unc-410 allele differs from the uncE408 and uncE429 alleles in that complementation tests with the Mu-induced unc alleles indicate that more than one gene is affected. It is concluded that this is due to a deletion which includes part of the uncE gene and another gene, or genes, between the uncE and uncA genes.

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