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Restoration of Active Transport in an Mg²⁺-Adenosine Triphosphatase-Deficient Mutant of Escherichia coli

¹ Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore, Maryland 21201

ABSTRACT

A neomycin-resistant mutant of Escherichia coli, NR70, lacking membrane-bound Mg²⁺-adenosine triphosphatase (EC 3.6.1.3) activity has been isolated. Both whole cells and membrane vesicles exhibit a reduced ability to accumulate amino acids and sugars. Other membrane-related functions such as oxygen consumption, the in vivo hydrolysis of o-nitrophenyl-ß-D-galactoside, and the phosphoenolpyruvate-dependent phosphotransferase system did not exhibit reduced activities in NR70. Amino acid transport could be partially restored by the addition of N,N'-dicyclohexylcarbodiimide. The results suggest that a role of the Mg²⁺-adenosine triphosphatase may be to participate in the coupling of energy derived from the electron transport chain to other processes such as transport.

This article has been cited by other articles:

• Kaback, H. R. (1974). Transport Studies in Bacterial Membrane Vesicles. Science 186: 882-892 [Abstract]