Mitochondrial adenosine triphosphatase in mit− mutants of Saccharomyces cerevisiae with defective subunit 6 of the enzyme complex

Choo, Wan Mee; Hadikusumo, Richard G.; Marzuki, Sangkot

doi:10.1016/0005-2728(85)90108-2

Cited by 25 publications

(8 citation statements)

References 42 publications

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“…Pleiotropic effects upon respiratory chain complexes have been observed in mutant strains either lacking a particular F 1 F 0 ‐ATP synthase subunit, or expressing a mutant variant of that subunit. In particular, the altered assembly of cytochrome c oxidase has been observed, as revealed by reduced levels of optically detectable cytochromes a + a 3 in cells having mutations in subunits 6, 8 and 9 of the F 1 F 0 ‐ATP synthase complex [31–33]. However, in cells lacking subunit g, no reduction in the level of cytochromes a + a 3 , or c + c 1 and b was observed.…”

Section: Discussionmentioning

confidence: 99%

Identification of subunit g of yeast mitochondrial F₁F₀‐ATP synthase, a protein required for maximal activity of cytochrome c oxidase

Boyle

Roucou

Nagley

et al. 1999

European Journal of Biochemistry

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By means of a yeast genome database search, we have identified an open reading frame located on chromosome XVI of Saccharomyces cerevisiae that encodes a protein with 53% amino acid similarity to the 11.3-kDa subunit g of bovine mitochondrial F 1 F 0 -ATP synthase. We have designated this ORF ATP20, and its product subunit g. A null mutant strain, constructed by insertion of the HIS3 gene into the coding region of ATP20, retained oxidative phosphorylation function. Assembly of F 1 F 0 -ATP synthase in the atp20-null strain was not affected in the absence of subunit g and levels of oligomycin-sensitive ATP hydrolase activity in mitochondria were normal. Immunoprecipitation of F 1 F 0 -ATP synthase from mitochondrial lysates prepared from atp20-null cells expressing a variant of subunit g with a hexahistidine motif indicated that this polypeptide was associated with other well-characterized subunits of the yeast complex. Whilst mitochondria isolated from the atp20-null strain had the same oxidative phosphorylation efficiency (ATP : O) as that of the control strain, the atp20-null strain displayed approximately a 30% reduction in both respiratory capacity and ATP synthetic rate. The absence of subunit g also reduced the activity of cytochrome c oxidase, and altered the kinetic control of this complex as demonstrated by experiments titrating ATP synthetic activity with cyanide. These results indicate that subunit g is associated with F 1 F 0 -ATP synthase and is required for maximal levels of respiration, ATP synthesis and cytochrome c oxidase activity in yeast.

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Section: Discussionmentioning

confidence: 99%

Identification of subunit g of yeast mitochondrial F₁F₀‐ATP synthase, a protein required for maximal activity of cytochrome c oxidase

Boyle

Roucou

Nagley

et al. 1999

European Journal of Biochemistry

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“…This low respiration rate was mainly the consequence of a high rho-cell content. However, it was previously observed that the absence of a functional F, had an indirect effect on the assembly and activity of the cytochrome oxidase (Choo et al, 1985 ;Paul et al, 1989). Similarly, cytochrome oxidase activities of 0.05 pmol 0, .…”

Section: Strainmentioning

confidence: 93%

The Subunit F of Mitochondrial Yeast ATP Synthase

Spannagel

Vaillier

Arselin

et al. 1997

European Journal of Biochemistry

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The subunit f of the yeast F1 F0 ATP synthase has been isolated from the purified enzyme. Amino acid composition, protein and peptide sequencing were performed. The data are in agreement with the sequence of the predicted product of the gene D9481.21 identified on the Saccharomyces cerevisiae chromosome IV. A 303‐bp open reading frame encoding a 101‐amino acid polypeptide is described. The deduced amino acid sequence from the ATP 17 gene is 6 amino acids longer than the mature protein, which displays a molecular mass of 10567 Da. The protein is basic with a short hydrophobic segment located in the C‐terminal part of the subunit. Subunit f remained associated with other F0 subunits upon sodium bromide treatment of the whole enzyme. A null mutant was constructed. The disrupted strain was unable to grow on glycerol medium and the mutation was recessive; rho− cells arose spontaneously. The null mutant mitochondria were devoid of oligomycin‐sensitive ATPase, but still contained an active F1 while the subunits f, 6 and 8 were absent.

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“…Although the pathway of the F0F1 assembly has not been extensively studied in mammals, many experiments have been performed using yeast mutants lacking one or several F0F1 subunits. It was reported that, in yeast, subunit 6 was not essential for the binding of F1 subunits to components of the F0 factor (33). The assembly of F0F1 subunits involved the sequential addition of subunits 9 (DCCD-binding protein), 8, and 6 to a membrane-bound F1, and two other proteins, subunits b and OSCP, were not found in the complex when the F0 sector was not properly assembled (34,35).…”

Section: Discussionmentioning

confidence: 99%

Functional F1-ATPase Essential in Maintaining Growth and Membrane Potential of Human Mitochondrial DNA-depleted ρ° Cells

Buchet

Godinot

1998

Journal of Biological Chemistry

219

175

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F1-ATPase assembly has been studied in human °c ells devoid of mitochondrial DNA (mtDNA). Since, in these cells, oxidative phosphorylation cannot provide ATP, their growth relies on glycolysis. Despite the absence of the mtDNA-coded F0 subunits 6 and 8, °cells possessed normal levels of F1-ATPase ␣ and ␤ subunits. This F1-ATPase was functional and azide-or aurovertinsensitive but oligomycin-insensitive. In addition, aurovertin decreased cell growth in °cells and also reduced their mitochondrial membrane potential, as measured by rhodamine 123 fluorescence. Therefore, a functional F1-ATPase was important to maintain the mitochondrial membrane potential and the growth of these °c ells. Bongkrekic acid, a specific adenine nucleotide translocator (ANT) inhibitor, also reduced °cell growth and mitochondrial membrane potential. In conclusion, °cells need both a functional F1-ATPase and a functional ANT to maintain their mitochondrial membrane potential, which is necessary for their growth. ATP hydrolysis catalyzed by F1 must provide ADP 3؊ at a sufficient rate to maintain a rapid exchange with the glycolytic ATP 4؊ by ANT, this electrogenic exchange inducing a mitochondrial membrane potential efficient enough to sustain cell growth. However, since the effects of bongkrekic acid and of aurovertin were additive, other electrogenic pumps should cooperate with this pathway.The biogenesis of mitochondrial proteins is controlled by both nuclear and mitochondrial genomes. The proteins coded by the mtDNA are subunits of enzyme complexes involved in oxidative phosphorylation. Since all these complexes also contain proteins coded by the nuclear genome, mechanisms regulating the coordinated expression and assembly of the subunits of nuclear and mitochondrial origin must exist. In yeast cells, nuclear DNA-coded components continue to be synthesized and imported into mitochondria, even when the synthesis of mtDNA-coded subunits is blocked (cf. for review, Refs. 1 and 2). The groups of Schatz and co-workers (3) and Neupert (4) have shown that a mitochondrial membrane potential is a key requirement for protein import into mitochondria (5). In normal cells, the mitochondrial membrane potential is mainly maintained by transmembrane proton pumping occurring during electron transfer or during ATP hydrolysis catalyzed by the ATPase-ATP synthase. In °cells depleted of mtDNA, these complexes cannot be functional since all complexes involved in proton pumping contain mtDNA-coded subunits (6). However, proteins of nuclear origin are imported into the °cell mitochondria (7). Therefore, the mitochondrial membrane potential must be maintained by other electrogenic pumps. In yeast, it has been suggested that the adenine nucleotide translocator (ANT) 1 mediates an exchange of ATP 4Ϫ synthesized in the cytosol during glycolysis for ADP 3Ϫ to maintain this mitochondrial membrane potential (8). However, the exact mechanism that maintains this potential has not been thoroughly investigated. Since the mtDNA-coded subunits are essential components for ...

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Mitochondrial adenosine triphosphatase in mit− mutants of Saccharomyces cerevisiae with defective subunit 6 of the enzyme complex

Cited by 25 publications

References 42 publications

Identification of subunit g of yeast mitochondrial F₁F₀‐ATP synthase, a protein required for maximal activity of cytochrome c oxidase

Identification of subunit g of yeast mitochondrial F₁F₀‐ATP synthase, a protein required for maximal activity of cytochrome c oxidase

The Subunit F of Mitochondrial Yeast ATP Synthase

Functional F1-ATPase Essential in Maintaining Growth and Membrane Potential of Human Mitochondrial DNA-depleted ρ° Cells

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Mitochondrial adenosine triphosphatase in mit− mutants of Saccharomyces cerevisiae with defective subunit 6 of the enzyme complex

Cited by 25 publications

References 42 publications

Identification of subunit g of yeast mitochondrial F1F0‐ATP synthase, a protein required for maximal activity of cytochrome c oxidase

Identification of subunit g of yeast mitochondrial F1F0‐ATP synthase, a protein required for maximal activity of cytochrome c oxidase

The Subunit F of Mitochondrial Yeast ATP Synthase

Functional F1-ATPase Essential in Maintaining Growth and Membrane Potential of Human Mitochondrial DNA-depleted ρ° Cells

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Identification of subunit g of yeast mitochondrial F₁F₀‐ATP synthase, a protein required for maximal activity of cytochrome c oxidase

Identification of subunit g of yeast mitochondrial F₁F₀‐ATP synthase, a protein required for maximal activity of cytochrome c oxidase