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. 1973 Dec;116(3):1124–1129. doi: 10.1128/jb.116.3.1124-1129.1973

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

Barry P Rosen 1
PMCID: PMC246465  PMID: 4270946

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-β-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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