Interconversion of high and low ATPase activity forms of ECF1 by the detergent lauryldimethylamine oxide

Lotscher, Hans Ruedi; DeJong, Catharina; Capaldi, Roderick A.

doi:10.1021/bi00313a020

Cited by 126 publications

(106 citation statements)

References 22 publications

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“…We suppose that EF 1 can also be activated without dissociation of ⑀ subunit, but the activated complex is more unstable than the corresponding form of TF 1 so that ⑀ subunit is lost from the complex in a short period. Lotscher et al (57) reported that ␣ 3 ␤ 3 ␥⑀ complex of EF 1 was activated 5-6-fold without dissociating ⑀ subunit when a detergent, lauryldimethylamine oxide, was present in the assay solution, and it was reverted to low activity form by diluting out the detergent. Although it was reported later that lauryldimethylamine oxide activated ␣ 3 ␤ 3 ␥ complex of EF 1 (58) and of TF 1 (53), it is …”

Section: Discussionmentioning

confidence: 99%

“…B, gel-filtration analysis of the activated ␣ 3 ␤ 3 ␥⑀ complex. The rest of the sample was subjected to a G3000SWXL gelfiltration column that was equilibrated and eluted with a buffer containing 1 mM ATP-Mg. A peak fraction at elution volume of 6.6 ml was recovered and was analyzed by 14% SDS-PAGE (inset a) and by 6% native-PAGE (inset b worth considering the fact that this detergent-induced activation accompanied the movement of ⑀ subunit in the complex as reflected by the greatly reduced yield of chemical cross-linking between ␤-⑀ subunits (57). For CF 1 , activation without dissociating ⑀ subunit has been achieved by reduction of the disulfide bond of the ␥ subunit (28).…”

Section: Fig 6 Re-isolation and Analysis Of Activated Subunit Complexmentioning

confidence: 99%

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Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

Kato

Matsui²,

Tanaka

et al. 1997

Journal of Biological Chemistry

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of thermophilic F 1 -ATPase were prepared, and their catalytic properties were compared to know the role of ␦ and ⑀ subunits in catalysis. The presence of ␦ subunit in the complexes had slight inhibitory effect on the ATPase activity. The effect of ⑀ subunit was more profound. The (؊⑀) complexes, ␣ 3 ␤ 3 ␥ and ␣ 3 ␤ 3 ␥␦, initiated ATP hydrolysis without a lag. In contrast, the (؉⑀) complexes, ␣ 3 ␤ 3 ␥⑀ and ␣ 3 ␤ 3 ␥␦⑀, started hydrolysis of ATP (<700 M) with a lag phase that was gradually activated during catalytic turnover. As ATP concentration increased, the lag phase of the (؉⑀) complexes became shorter, and it was not observed above 1 mM ATP. Analysis of binding and hydrolysis of the ATP analog, 2 ,3 -O-(2,4,6-trinitrophenyl)-ATP, suggested that the (؉⑀) complexes bound substrate only slowly. Differing from Escherichia coli F 1 -ATPase, the activation of the (؉⑀) complexes from the lag phase was not due to dissociation of ⑀ subunit since the re-isolated activated complex retained ⑀ subunit. This indicates that there are two alternative forms of the (؉⑀) complex, inhibited form and activated form, and the inhibited one is converted to the activated one during catalytic turnover.

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Section: Discussionmentioning

confidence: 99%

Section: Fig 6 Re-isolation and Analysis Of Activated Subunit Complexmentioning

confidence: 99%

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

Kato

Matsui²,

Tanaka

et al. 1997

Journal of Biological Chemistry

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“…Concanamycin A-sensitive ATPase activity was assayed by a coupled enzyme assay (20) performed in the absence and presence of 200 nM concanamycin A. Protein concentrations were determined by Lowry assay (21).…”

Section: Methodsmentioning

confidence: 99%

The Yeast Vacuolar Proton-translocating ATPase Contains a Subunit Homologous to the Manduca sexta and Bovine e Subunits That Is Essential for Function

Sambade

Kane

2004

Journal of Biological Chemistry

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The yeast cwh36⌬ mutant was identified in a screen for yeast mutants exhibiting a Vma ؊ phenotype suggestive of loss of vacuolar proton-translocating ATPase (VATPase) activity. The mutation disrupts two genes, CWH36 and a recently identified open reading frame on the opposite strand, YCL005W-A. We demonstrate that disruption of YCL005W-A is entirely responsible for the Vma ؊ growth phenotype of the cwh36⌬ mutant. YCL005W-A encodes a homolog of proteins associated with the Manduca sexta and bovine chromaffin granule V-ATPase. The functional significance of these proteins for V-ATPase activity had not been tested, but we show that the protein encoded by YCL005W-A, which we call Vma9p, is essential for V-ATPase activity in yeast. V-ATPases 1 are highly conserved proton pumps responsible for acidification of multiple organelles, including the Golgi apparatus, endosomes, and lysosomes, in all eukaryotic cells (1, 2). All V-ATPases are multisubunit complexes comprised of a peripheral sector, V 1 , attached to a membrane sector, V 0 . In yeast cells, the V 1 sector contains eight different subunits, and the V 0 sector contains five subunits; all of these subunits have homologs in other eukaryotic cells (1, 2). Genetic deletion of any V-ATPase subunit results in a well defined set of growth defects in yeast, including sensitivity to elevated pH and calcium concentrations, inability to grow on non-fermentable carbon sources, and sensitivity to a variety of heavy metals (3, 4). This Vma Ϫ growth phenotype has been invaluable in determining the subunit composition of the yeast V-ATPase and in assessing the level of V-ATPase function in various mutants, and it has largely driven the emergence of yeast as the model system of choice in many studies of eukaryotic V-ATPases (5-7).Although V-ATPase subunit composition is very similar among eukaryotes, highly purified preparations of the Manduca sexta and bovine chromaffin granule V-ATPases both contain membrane proteins of 9 -10 kDa that had not been observed in other systems, including yeast (8, 9). This protein associated tightly with the V 0 sector in both preparations and appeared to be present at a comparable stoichiometry with the other V-ATPase subunits, prompting the investigators to name it the "e" subunit. However, it was impossible to determine whether these proteins played a critical role in V-ATPase function or were "accessory" proteins involved in assembly or regulation in an organelle-and/or species-specific manner. In fact, the bovine protein (8) showed limited homology to the yeast Vma21 protein, which is an endoplasmic reticulum protein essential for V-ATPase assembly (10). This suggested that higher eukaryotes had evolved a version of Vma21p that might play a similar role in assembly but remained attached to the assembled enzyme.We screened a library of yeast deletion strains for mutants exhibiting the Vma Ϫ phenotype characteristic of loss of VATPase activity. 2 One mutant, cwh36⌬, exhibited a very strong Vma Ϫ phenotype and no vacuolar acidification. Similar...

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“…5 b). The membrane-bound F,F, ATPase from E. coli, which also does not bear IF1, is stimulated by LDAO to a limited extent (Lotscher et al, 1984). Lastly, in submitochondrial particles extracted from beef heart, LDAO activates the ATPase by at least two different mechanisms, one of them being the release of the inhibitory effect of IF1 (Vizquez-Laslop and Dreyfus, 1986).…”

Section: Conformational Changes Related To the A'rpase Activationmentioning

confidence: 99%

The electrochemical‐proton‐gradient‐activated states of F₀F₁ ATPase in plant mitochondria as revealed by detergents

Valerio¹,

Diolez²,

Haraux³

1993

European Journal of Biochemistry

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ATP hydrolysis, triggered by the addition of polyoxyethylene-9-lauryl ether (Lubrol) or lauryldimethylamine oxide (LDAO) to energized plant mitochondria was studied in some details. The membrane disruption was quasi-instantaneous (2-3 s) with both detergents, as shown by the decrease of turbidity and the stopping of respiration. In pea leaf mitochondria, Lubrol triggered ATP hydrolysis in almost the same way as valinomycin plus nigericin, except that the activity was slightly stimulated and became insensitive to carboxyatractyloside. This allowed investigations of ATP hydrolysis without any interference of the ATP/ADP antiporter or the phosphate carrier. Lubrol did not prevent the ATPase from deactivating in pea leaf mitochondria, and did not trigger any ATP hydrolysis in potato tuber mitochondria. At variance with Lubrol, LDAO changed the properties of the FZ, ATPase. It made the enzyme oligomycin insensitive and froze it in an activated state. The activity was also 5 -8-times stimulated in pea leaf mitochondria. Moreover, LDAO revealed an important ATP hydrolase activity when added to energized potato tuber mitochondria. Despite the specific effect of LDAO, the activity triggered by this detergent strongly depended on the energized state of the organelles before detergent addition.

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Interconversion of high and low ATPase activity forms of ECF1 by the detergent lauryldimethylamine oxide

Cited by 126 publications

References 22 publications

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

The Yeast Vacuolar Proton-translocating ATPase Contains a Subunit Homologous to the Manduca sexta and Bovine e Subunits That Is Essential for Function

The electrochemical‐proton‐gradient‐activated states of F₀F₁ ATPase in plant mitochondria as revealed by detergents

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Interconversion of high and low ATPase activity forms of ECF1 by the detergent lauryldimethylamine oxide

Cited by 126 publications

References 22 publications

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

The Yeast Vacuolar Proton-translocating ATPase Contains a Subunit Homologous to the Manduca sexta and Bovine e Subunits That Is Essential for Function

The electrochemical‐proton‐gradient‐activated states of F0F1 ATPase in plant mitochondria as revealed by detergents

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The electrochemical‐proton‐gradient‐activated states of F₀F₁ ATPase in plant mitochondria as revealed by detergents