Essential role of membrane ATPase or coupling factor for anaerobic growth and anaerobic active transport in Escherichia coli

Yamamoto, Thomas; Mével-Ninio, Maryvonne; Valentine, Raymond C.

doi:10.1016/0005-2728(73)90111-4

Cited by 49 publications

(25 citation statements)

References 11 publications

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“…Mutants of E. coli and Salmonella typhimurium that are energy-uncoupled for oxidative phosphorylation have been described previously (7,9,11,12,(30)(31)(32), and are defective in the Mg,Ca-ATPase (uncA mutants) or energy coupling proteins (uncB in E. coli, etc in S. typhimurium). These mutants cannot grow on succinate, fumarate, malate, or D-lactate as sole carbon and energy source and grow on glucose with a markedly reduced rate and growth yield.…”

Section: Discussionmentioning

confidence: 99%

“…However, in striking contrast to these mutants, which have normal aerobic transport capability (7,8; J.-s. Hong, manuscript in preparation) t, t There have been three reports in which uncA mutations were isolated and shown to result in defective aerobic transport (9, 12; 32). However, the involvement of a functional ATPase in aerobic transport remains controversial (7)(8)(9)12 The normal transport activity at 420 by the membrane vesicles prepared from JSH4 is surprising. Two possible explanations are (i) an extensive dilution during the vesicle preparation of a possible cytoplasmic inhibitor of the mutated ECF protein and (ii) the mutated ECF protein is altered during the vesicle preparation such that it is active and no longer sensitive to high temperature.…”

Section: Discussionmentioning

confidence: 99%

“…In whole cells the main energy source utilized for aerobic transport comes from respiration and the generation or utilization of ATP does not seem to be involved (7,8). On the other hand, cells apparently utilize the energy derived from the hydrolysis of ATP for anaerobic transport, as demonstrated in studies on mutants defective in the CaMg-ATPase (7,9). The form of the metabolic energy, whether it be a high-energy intermediate of oxidative phosphorylation, an energized membrane state, or some other form, has not yet been determined (2,(10)(11)(12).…”

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A Mutant of Escherichia coli Defective in the Coupling of Metabolic Energy to Active Transport

Lieberman

Hong

1974

Proc. Natl. Acad. Sci. U.S.A.

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The isolation of a temperature-sensitive mutant of E. coli K12 whose active transport of amino acids and sugars is not coupled to metabolic energy at 420 is described. This The ecfta mutation has been mapped to be in the 54.5-to 60-min region of the E. coli chromosome map. Possible interactions between the metC mutation and the mutated energy coupling factor protein are discussed.The molecular mechanisms by which metabolic energy is coupled to active transport in bacteria have been a subject of considerable interest (1-5). In the Escherichia coli membrane vesicle system the oxidation of D-lactate to pyruvate facilitates the transport of a wide variety of amino acids and sugars against a concentration gradient (1, 6). In whole cells the main energy source utilized for aerobic transport comes from respiration and the generation or utilization of ATP does not seem to be involved (7,8). On the other hand, cells apparently utilize the energy derived from the hydrolysis of ATP for anaerobic transport, as demonstrated in studies on mutants defective in the CaMg-ATPase (7, 9). The form of the metabolic energy, whether it be a high-energy intermediate of oxidative phosphorylation, an energized membrane state, or some other form, has not yet been determined (2, 10-12).In this paper we describe a mutant that is temperaturesensitive in a pleiotropic manner for the active transport of amino acids and sugars and is altered in a component energy coupling factor (ECF) that is necessary for the coupling of metabolic energy to transport. We also present evidence that a derivative of methionine may be interacting with the altered protein. MATERIALS AND METHODSBacterial Strains. All strains used were of E. coli K12 and are listed in Table 1

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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A Mutant of Escherichia coli Defective in the Coupling of Metabolic Energy to Active Transport

Lieberman

Hong

1974

Proc. Natl. Acad. Sci. U.S.A.

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“…Studies of ATPase-deficient mutants of Escherichia coli have led to the conclusion that one function of the ATPase is to catalyze the synthesis of ATP during oxidative phosphorylation (1)(2)(3)(4)(5). A second function of this enzvme, distinguished under anaerobic conditions, is thought to be the coupling of ATP hydrolysis to essential membrane events that require the expenditure of metabolic energy.…”

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confidence: 99%

“…A second function of this enzvme, distinguished under anaerobic conditions, is thought to be the coupling of ATP hydrolysis to essential membrane events that require the expenditure of metabolic energy. In the absence of respiration, ATPasenegative mutants cannot utilize ATP from substrate level phosphorylations to drive the ATP-linked transhydrogenase (6, 7)'or the accumulation of various metabolites (3,5,8). Such anaerobic function of the ATPase is also suggested by the effects of NN'-dicyclohexylcarbodiimide (DCCD), an inhibitor of this enzyme (9,10).…”

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A Protonmotive Force Drives ATP Synthesis in Bacteria

Maloney

Kashket

Wilson

1974

Proc. Natl. Acad. Sci. U.S.A.

147

103

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When cells of Streptococcus lactis or Escherichia coli were suspended in-a potassium-free medium, a membrane potential (negative inside) could be artificially generated by the addition of-the potassium ionophore, valinomycin. In 'response to this inward directed protonmotive force, ATP synthesis catalyzed by the mnembrane-bound'ATPase (EC 3.6.1.3) was observed. (Fig. 1A). Thus, the electrochemical potential of protons (the protonmotive force) provides the driving force for ATP synthesis. The alternative (anaerobic) function of the ATPase is required when protons cannot be extruded by the respiratory chain. Under these conditions, the ATPase couples the hydrolysis of ATP to the electrogenic movement of protons out of the cell (Fig. 11B). The protonmotive force generated by ATP hydrolysis is then utilized by energy-dependent reactions such as the "ATP-linked" transhydrogenase, or the active transport of metabolites.Evidence in support of this anaerobic function of the ATPase has been presented by Harold and his collaborators, who have studied the anaerobe S. fecalis (faecium). They showed that glycolyzing cells establish both a pH gradient (interior alkaline) and a membrane potential (interior negative), and that DCCD inhibits the formation of each of these components of the protonmotive force (17)(18)(19) 1% (w/v)

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The Active Transport of Carbohydrates by Escherichia coli

Henderson

Kornberg

1975

Ciba Foundation Symposium 31 ‐ Energy Transformation in Biological Systems

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Essential role of membrane ATPase or coupling factor for anaerobic growth and anaerobic active transport in Escherichia coli

Cited by 49 publications

References 11 publications

A Mutant of Escherichia coli Defective in the Coupling of Metabolic Energy to Active Transport

A Mutant of Escherichia coli Defective in the Coupling of Metabolic Energy to Active Transport

A Protonmotive Force Drives ATP Synthesis in Bacteria

The Active Transport of Carbohydrates by Escherichia coli

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