Restoration of active transport in an Mg2+-adenosine triphosphatase-deficient mutant of Escherichia coli.
A neomycin-resistant mutant of Escherichia coli, NR70, lacking membrane-bound Mg(2+)-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-beta-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 Mg(2+)-adenosine triphosphatase may be to participate in the coupling of energy derived from the electron transport chain to other processes such as transport.
D000251:Adenosine Triphosphatases / Q000096:biosynthesis* / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism*; D001693:Biological Transport, Active; D002234:Carbodiimides / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D006027:Glycosides / Q000378:metabolism*; D006868:Hydrolysis; D008274:Magnesium / Q000378:metabolism; D009154:Mutation; D009355:Neomycin / Q000494:pharmacology; D010101:Oxygen Consumption; D011392:Proline / Q000378:metabolism
D000596:Amino Acids; D002234:Carbodiimides; D006027:Glycosides; D011392:Proline; D000251:Adenosine Triphosphatases; D009355:Neomycin; D008274:Magnesium