Restoration of Active Transport in an Mg2+-Adenosine Triphosphatase-Deficient Mutant of Escherichia coli
AUTOR(ES)
Rosen, Barry P.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=246465Documentos Relacionados
- Properties of Escherichia coli mutants with alterations in Mg2+-adenosine triphosphatase.
- Physiological suppression of a transport defect in Escherichia coli mutants deficient in Ca2+, Mg2+-stimulated adenosine triphosphatase.
- Changes in active transport, intracellular adenosine 5'-triphosphate levels, macromolecular syntheses, and glycolysis in an energy-uncoupled mutant of Escherichia coli.
- Bacillus megaterium mutant deficient in membrane-bound adenosine triphosphatase activity.
- Membrane Mg2+-(Ca2+)-Activated Adenosine Triphosphatase of Escherichia coli: Characterization in the Membrane-Bound and Solubilized States1