Cloning of the yeast ATP3 gene coding for the γ-subunit of F1 and characterization of atp3 mutants.

Paul, Marie-Françoise; Ackerman, Sharon H.; Yue, Jennifer; Arselin, Geneviève; Velours, Jean; Tzagoloff, Alexander

doi:10.1074/jbc.270.6.2880

Cited by 46 publications

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“…The fact that translation is reduced in ⌬atp11 and ⌬atp12 mutants, which contain aggregated forms the ␣ and ␤ subunits (5), indicates that a minimal requirement for translation activation is that the ␣ and ␤ subunits of F 1 be present as soluble proteins. A requirement of ␥ and ␦ subunit mutants for translation of Atp6p and Atp8p proved to be difficult to assess directly because of the extensive loss of ϩ mitochondrial genome in these strains (17,18). The low level of ␥ and ␦ subunits reported in the mutant (16), however, favors the notion that neither of these F 1 components is essential for translational activation.…”

Section: Discussionmentioning

confidence: 70%

“…The mutants used for growth tests were derived from crosses to MR6 (MATa ade2-1 his3-1,15 leu2-3,112 trp1-1 ura3-1 arg8::HIS3), a respiratory competent strains with an arg8 null mutation (8). The compositions of the solid and liquid YPD, YPGal, YPEG, and minimal glucose media have been described previously (18).…”

Section: Methodsmentioning

confidence: 99%

“…Mitochondrial F 1 ATPase consists of five different subunits with an ␣ 3 ␤ 3 ␥␦ stoichiometry. In contrast to the ⌬atp11, ⌬atp12, ⌬atp1, and ⌬atp2 mutants, which accumulate the ␣ and/or ␤ subunits of F 1 as bulk aggregates, , ␦, or ␥ mutants maintain both ␣ and ␤ subunits as soluble proteins (16)(17)(18).…”

Section: Are Soluble But Incompletely Assembled Forms Of F1 Sufficienmentioning

confidence: 99%

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F ₁ -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase

Rak

Tzagoloff

2009

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

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The ATP synthase of yeast mitochondria is composed of 17 different subunit polypeptides. We have screened a panel of ATP synthase mutants for impaired expression of Atp6p, Atp8p, and Atp9p, the only mitochondrially encoded subunits of ATP synthase. Our results show that translation of Atp6p and Atp8p is activated by F1 ATPase (or assembly intermediates thereof). Mutants lacking the ␣ or ␤ subunits of F1, or the Atp11p and Atp12p chaperones that promote F1 assembly, have normal levels of the bicistronic ATP8/ATP6 mRNAs but fail to synthesize Atp6p and Atp8p. F1 mutants are also unable to express ARG8 m when this normally nuclear gene is substituted for ATP6 or ATP8 in mitochondrial DNA. Translational activation by F1 is also supported by the ability of ATP22, an Atp6p-specific translation factor, to restore Atp6p and to a lesser degree Atp8p synthesis in the absence of F1. These results establish a mechanism by which expression of ATP6 and ATP8 is translationally regulated by F1 to achieve a balanced output of two compartmentally separated sets of ATP synthase genes.F1-ATPase ͉ mitochondria ͉ Saccharomyces cerevisiae ͉ translational regulation

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Section: Discussionmentioning

confidence: 70%

Section: Methodsmentioning

confidence: 99%

Section: Are Soluble But Incompletely Assembled Forms Of F1 Sufficienmentioning

confidence: 99%

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F ₁ -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase

Rak

Tzagoloff

2009

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

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“…The change in free energy of unfolding on mutation, ⌬⌬G H2O , between wild type and mutant HuAtp12 can be calculated from the difference between the ⌬G H2O values derived from Equation 4.…”

Section: Purification Of Recombinant Huatp12p Wild Type and Mutant Prmentioning

confidence: 99%

The Molecular Chaperone, Atp12p, from Homo sapiens

Hinton

Gatti

Ackerman

2004

Journal of Biological Chemistry

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Work inSaccharomyces cerevisiae has shown that Atp12p binds to unassembled ␣ subunits of F 1 and in so doing prevents the ␣ subunit from associating with itself in non-productive complexes during assembly of the F 1 moiety of the mitochondrial ATP synthase. We have developed a method to prepare recombinant Atp12p after expression of its human cDNA in bacterial cells. The molecular chaperone activity of HuAtp12p was studied using citrate synthase as a model substrate. Wild type HuAtp12p suppresses the aggregation of thermally inactivated citrate synthase. In contrast, the mutant protein HuAtp12p E240K , which harbors a lysine at the position of the highly conserved Glu-240, fails to prevent citrate synthase aggregation at 43°C. No significant differences were observed between the wild type and the mutant proteins as judged by sedimentation analysis, cysteine titration, tryptophan emission spectra, or limited proteolysis, which suggests that the E240K mutation alters the activity of HuAtp12p with minimal effects on the physical integrity of the protein. An additional important finding of this work is that the equilibrium chemical denaturation curve of HuAtp12p shows two components, the first of which is associated with protein aggregation. This result is consistent with a model for Atp12p structure in which there is a hydrophobic chaperone domain that is buried within the protein interior.

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“…In Saccharomyces cerevisiae, all five F 1 subunits are encoded by nuclear genes (5)(6)(7)(8)(9) and are synthesized in the cytoplasm and then imported into mitochondria (10). Like other nuclearencoded mitochondrial proteins, the F 1 subunits are imported to the matrix compartment as unfolded polypeptide chains.…”

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confidence: 99%

Failure to Assemble the α3 β3 Subcomplex of the ATP Synthase Leads to Accumulation of the α and β Subunits within Inclusion Bodies and the Loss of Mitochondrial Cristae in Saccharomyces cerevisiae

Lefebvre-Legendre

Salin

Schaeffer

et al. 2005

Journal of Biological Chemistry

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The F 1 component of mitochondrial ATP synthase is an oligomeric assembly of five different subunits, ␣, ␤, ␥, ␦, and ⑀. In terms of mass, the bulk of the structure (ϳ90%) is provided by the ␣ and ␤ subunits, which form an (␣ ␤) 3 hexamer with adenine nucleotide binding sites at the ␣/␤ interfaces. We report here ultrastructural and immunocytochemical analyses of yeast mutants that are unable to form the ␣ 3 ␤ 3 oligomer, either because the ␣ or the ␤ subunit is missing or because the cells are deficient for proteins that mediate F 1 assembly (e.g. Atp11p, Atp12p, or Fmc1p). The F 1 ␣ and ␤ subunits of such mutant strains are detected within large electron-dense particles in the mitochondrial matrix. The composition of the aggregated species is principally full-length F 1 ␣ and/or ␤ subunit protein that has been processed to remove the amino-terminal targeting peptide. To our knowledge this is the first demonstration of mitochondrial inclusion bodies that are formed largely of one particular protein species. We also show that yeast mutants lacking the ␣ 3 ␤ 3 oligomer are devoid of mitochondrial cristae and are severely deficient for respiratory complexes III and IV. These observations are in accord with other studies in the literature that have pointed to a central role for the ATP synthase in biogenesis of the mitochondrial inner membrane.

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Cloning of the yeast ATP3 gene coding for the γ-subunit of F1 and characterization of atp3 mutants.

Cited by 46 publications

References 0 publications

F ₁ -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase

F ₁ -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase

The Molecular Chaperone, Atp12p, from Homo sapiens

Failure to Assemble the α3 β3 Subcomplex of the ATP Synthase Leads to Accumulation of the α and β Subunits within Inclusion Bodies and the Loss of Mitochondrial Cristae in Saccharomyces cerevisiae

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Cloning of the yeast ATP3 gene coding for the γ-subunit of F1 and characterization of atp3 mutants.

Cited by 46 publications

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F 1 -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase

F 1 -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase

The Molecular Chaperone, Atp12p, from Homo sapiens

Failure to Assemble the α3 β3 Subcomplex of the ATP Synthase Leads to Accumulation of the α and β Subunits within Inclusion Bodies and the Loss of Mitochondrial Cristae in Saccharomyces cerevisiae

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F ₁ -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase

F ₁ -dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase