1972
DOI: 10.1099/00221287-70-3-507
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A Mutant of Escherichia coli with a Defect in Energy Metabolism

Abstract: A mutant of Escherichia coli with a decreased growth efficiency has been investigated. The results of growth studies with different substrates and of measurement of P/O ratios in membrane preparations suggest that the strain is defective in the ability to couple synthesis of ATP to electron transport. I N T R O D U C T I O NEscherichia coli strain 15-28 is a mutant containing an abnormally high concentration of the immediate precursor to the 50 s ribosomal subunit (MacDonald, Turnock & Forchhammer, 1967). The … Show more

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Cited by 18 publications
(8 citation statements)
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“…Alternatively, internalization of the aminoglycoside when bound to a ribosomal site could enhance the protonmotive force due to the electrochemical characteristics of aminoglycosides. An increased rate of streptomycin and gentamicin entry has been shown here to occur with AN120 and apparently in a mutant described by Turnock et al (38,39), so this seems a feasible proposal. Mutants 12,1977 on May 12, 2018 by guest http://aac.asm.org/ (F. L. Jackson, unpublished data) (uncoupled bacteria utilize succinate poorly as an energy source), and loss of permeability control for amino acids and nucleotides (1,18).…”
supporting
confidence: 61%
“…Alternatively, internalization of the aminoglycoside when bound to a ribosomal site could enhance the protonmotive force due to the electrochemical characteristics of aminoglycosides. An increased rate of streptomycin and gentamicin entry has been shown here to occur with AN120 and apparently in a mutant described by Turnock et al (38,39), so this seems a feasible proposal. Mutants 12,1977 on May 12, 2018 by guest http://aac.asm.org/ (F. L. Jackson, unpublished data) (uncoupled bacteria utilize succinate poorly as an energy source), and loss of permeability control for amino acids and nucleotides (1,18).…”
supporting
confidence: 61%
“…A number of mutants ofEscherichia coli have been isolated with a defect in oxidative phosphorylation [1][2][3][4][5][6][7]. The mutants isolated thus far, all map in the same region of the chromosome (73.5 min) and all are affected in the membrane Mg 2÷-Ca 2+ ATPase complex.…”
Section: Introductionmentioning
confidence: 99%
“…The mutants isolated thus far, all map in the same region of the chromosome (73.5 min) and all are affected in the membrane Mg 2÷-Ca 2+ ATPase complex. One class of mutants has been shown to lack ATPase catalytic activity [1,3,5,7], while a second class of mutants retains the ATPase activity [2,4,6], but in a form which is resistant to the energy transfer inhibitor DCCD** [2]. Studies of active transport in mutants of the first class have provided evidence that phosphate-bond energy is not required for the aerobic transport of certain solutes in E. coli [5,8,9].…”
Section: Introductionmentioning
confidence: 99%
“…Mutants lacking this enzyme were isolated in several laboratories (1)(2)(3)(4)(5)(6)(7). Studies with such mutants have been useful in distinguishing transport systems driven by an energized membrane state from those that require substrate level phosphorylation (8,9).…”
mentioning
confidence: 99%