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J Bacteriol. 1972 April; 110(1): 18-25
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Biochemical and Genetic Studies on Ubiquinone Biosynthesis in Escherichia coli K-12: 4-Hydroxybenzoate Octaprenyltransferase

Department of Biochemistry, John Curtin School of Medical Research, The Institute of Advanced Studies, Australian National University, Canberra, A.C.T., Australia

ABSTRACT

Three ubiquinone-deficient mutants of Escherichia coli unable to convert 4-hydroxybenzoate into 3-octaprenyl-4-hydroxybenzoate were isolated and examined. The results of genetic analysis suggest that each of the mutants carries a mutation in a gene designated ubiA which can be represented at minute 79 on the E. coli chromosome map. The conversion of 4-hydroxybenzoate into 3-octaprenyl-4-hydroxybenzoate, catalyzed by 4-hydroxybenzoate octaprenyltransferase, was studied with a strain of E. coli that is blocked in the common pathway of aromatic biosynthesis and consequently accumulates the precursor of the side chain of ubiquinone. Both the side-chain precursor and 4-hydroxybenzoate octaprenyltransferase were shown to be membrane-bound. The enzyme required Mg²⁺ for optimal activity. The ubiA^– mutants were found to lack 4-hydroxybenozate octaprenyltransferase activity, which suggested that the ubiA gene is the structural gene coding for this enzyme.

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