Biogenesis of mitochondrial ATPase

Sebald, Walter

doi:10.1016/0304-4173(77)90002-7

Cited by 112 publications

(15 citation statements)

References 102 publications

(127 reference statements)

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“…Additional nine other polypeptides derived from, or associated with, the Fo moiety can be distinguished. Similar results have been published by Marahiel et al [20] and Sebald [21] for FoFl ATPases from yeast mitochondria. It is not yet clear whether all additional polypeptides listed are part of the Fo moiety of the enzyme.…”

Section: Purit) Of the Preparation And Subunit Cotnpositionsupporting

confidence: 90%

See 1 more Smart Citation

Properties of the F₀F₁ ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X‐100

Schneider

Müller

Rittinghaus

et al. 1979

European Journal of Biochemistry

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A cold‐stable oligomycin‐sensitive F0F1 ATPase complex from chromatophores of Rhodospirillum rubrum FR 1 was solubilized by Triton X‐100 and purified by gel filtration. The F0F1 complex is resolved by sodium dodecyl sulfate electrophoresis into 14 polypeptides with approximate molecular weights in the range of 58000–6800; five of these polypeptides are derived from the F1 moiety of the complex which carries the catalytic centers of the enzyme. The purified F0F1 complex is homogeneous according to analytical ultracentrifugation and isoelectric focusing. The molecular weight as determined by gel filtration is about 480000 ± 30000. so20,w is 1.45 ± 0.1 S and the pI is 5.4. The amino acid composition of the F0F1 complex is compared with the data obtained for the F1 moiety of the enzyme. Quantitative data on the sensitivity to N,N′‐dicyclohexyl‐carbodiimide as well as kinetic parameters, regarding substrate specificity and dependence of ATPase activity on divalent cations, are reported.

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Section: Purit) Of the Preparation And Subunit Cotnpositionsupporting

confidence: 90%

“…An Fo complex from a thermophilic bacterium has been shown to consist of only three different polypeptides [9], whereas Fo complexes from other sources appear to contain up to 10 different subunits [20,21].…”

Section: S and The P I Is 54mentioning

confidence: 99%

Properties of the F₀F₁ ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X‐100

Schneider

Müller

Rittinghaus

et al. 1979

European Journal of Biochemistry

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“…In two of these classes, Oli-1 and Oli-3, the altered gene product is the dicyclohexylcarbodiimide-binding protein, alternatively referred to as ATPase-9. This protein is present in mammalian mitochondrial ATPase, but it must be encoded by a nuclear rather than a mitochondrial gene, as has been shown to be the case in Neurospora (27). A sequence which could encode this protein has not been located in mouse, human, or bovine mtDNA (1,3).…”

Section: Methodsmentioning

confidence: 99%

Sequence analysis of mitochondrial DNA in a mouse cell line resistant to chloramphenicol and oligomycin.

Slott¹,

Shade²,

Lansman³

1983

Mol. Cell. Biol.

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A mouse L-cell line, designated 111-OB3, is described which is resistant to two drugs, chloramphenicol and oligomycin. The cells contain two types of mitochondrial DNA molecules, in roughly equal proportions, which differ in that one is cleaved by endonuclease EcoRI at a novel site within the coding sequence for subunit 6 of the mitochondrial ATPase (ATPase-6). Sequence analysis reveals that the cleavage site was created by a single transversion which predicts a replacement of valine in the wild-type ATPase-6 by glutamic acid. The replacement occurs in a hydrophobic amino acid sequence which is highly conserved in mouse, human, and bovine proteins. The position of the replacement is similar to a substitution observed in one class of yeast mutants resistant to oligomycin. Both of the mitochondrial DNA molecules in 111-OB3 also have a single nucleotide change in the gene encoding the large (16S) rRNA. These observations are consistent with the hypothesis that oligomycin resistance in mammalian cells can be cytoplasmically determined and can result from alterations in ATPase-6. The appearance of the mutation before selection in oligomycin suggests a model for the origin of mitochondrial mutations in mammalian cells.

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“…A proton ionophore, CCCP (10 1íM), also stimulates efflux by 70% . DCCD (50-100 1íM), an inhibitor of proton ATPases (12)(13)(14), enhances efflux by 70-80% . Kinetic studies show that stimulation of efflux by DCCD (501íM) and CCCP (10 gM) is complete within 10 min of incubation (data not shown) .…”

Section: Calcium Content Of P Chabaudi-infected Rat Erythrocytesmentioning

confidence: 99%

Calcium transport of Plasmodium chabaudi-infected erythrocytes.

Tanabe¹,

Mikkelsen²,

Wallach³

1982

The Journal of Cell Biology

117

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The calcium content and transport processes of Plasmodium chabaudi-infected rat erythrocytes were analyzed by atomic absorption spectroscopy and "Ca" flux measurements . Infected erythrocytes, after fractionation on metrizamide gradients according to stage of parasite development, exhibited progressively increasing levels of Ca 2+ with schizont and gametocytes containing 10-to 20-fold greater calcium levels than normal cells (0.54 ± 0.25 nmol/108 cells) . 45Ca 2 + flux experiments showed both increased influx and decreased efflux in infected erythrocytes . Tris/NH 4C1 lysis of normal erythrocytes preloaded with 45 Ca 2+ with the Ca 2+ ionophore A23187 released >90% of cell calcium after incubation in ethyleneglycol bis(aminoethylether) N, N'-tetraacetic acid containing buffer, whereas lysis of the infected erythrocyte membrane resulted in release of 10-20% cell Cat+ , with the remaining portion associated with the isolated parasite fraction . This information together with the effects of various metabolic inhibitors indicates the presence of a parasite Ca' compartment in P. chabaudi-infected erythrocytes .Dicyclohexylcarbodiimide (DCCD) an inhibitor of proton ATPases of chloroplasts, bacteria, yeast, and mitochondria, and the proton ionophore, carbonyl cyanide m-chlorophenylhydrazone (CCCP), inhibited Ca 2+ influx and stimulated efflux from infected cells . These results combined with evidence for a DCCD-and CCCP-sensitive membrane potential in P. chabaudiinfected cells (Mikkelsen et al ., accompanying manuscript) suggest that Ca 2+ transport of intraerythrocytic parasites is coupled to a proton-motive force across the Plasmodia plasma membrane .The calcium ion is an essential component of many cellular regulatory processes, and cells expend considerable energy to maintain low levels of free cytoplasmic Cat+ . In the case of enucleated erythrocytes, low cytoplasmic Ca' concentrations are achieved by a combination of plasma membrane Ca" binding, low membrane Ca' permeability, and active extrusion by Ca 2+' Mg t +-ATPase pump (1, 2). Elevation of intracellular Ca 2+ results in decreased membrane deformability, altered monovalent cation transport, and modification of membrane protein structure, e.g . spectrin degradation (1, 3) . Malaria is a blood-borne disease in which the asexual development of the parasite Plasmodium occurs within the host erythrocyte. Few investigators have addressed the general issue of ion transport in Plasmodium-infected erythrocytes, although increased osmotic fragility is a common observation of Plasmodium-infected erythrocytes . Dunn (4) has shown increased sodium and decreased potassium intracellular levels resulting in part from decreased Na', K+-ATPase activity of parasitized erythrocytes . No information is available concerning Ca" levels and intracellular Ca" distribution in infected cells or the relative contributions of erythrocyte and parasite Ca' transport processes of infected cells. Such information may indicate mechanisms by which the parasite modifies its intracellu...

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Biogenesis of mitochondrial ATPase

Cited by 112 publications

References 102 publications

Properties of the F₀F₁ ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X‐100

Properties of the F₀F₁ ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X‐100

Sequence analysis of mitochondrial DNA in a mouse cell line resistant to chloramphenicol and oligomycin.

Calcium transport of Plasmodium chabaudi-infected erythrocytes.

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Biogenesis of mitochondrial ATPase

Cited by 112 publications

References 102 publications

Properties of the F0F1 ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X‐100

Properties of the F0F1 ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X‐100

Sequence analysis of mitochondrial DNA in a mouse cell line resistant to chloramphenicol and oligomycin.

Calcium transport of Plasmodium chabaudi-infected erythrocytes.

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Properties of the F₀F₁ ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X‐100

Properties of the F₀F₁ ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X‐100