ATP6/Q0085 Literature Guide Help

Other names published for ATP6: OLI2, OLI4, PHO1, F1F0 ATP synthase subunit a, Q0085

ATP6 - Function/Process (23)

ReferenceOther Genes Addressed
Forster K, et al.  (2010) Proton transport coupled ATP synthesis by the purified yeast H(+)-ATP synthase in proteoliposomes. Biochim Biophys Acta 1797(11):1828-37
Kucharczyk R, et al.  (2010) Consequences of the pathogenic T9176C mutation of human mitochondrial DNA on yeast mitochondrial ATP synthase. Biochim Biophys Acta 1797(6-7):1105-1112
Ozalp VC, et al.  (2010) Time-resolved Measurements of Intracellular ATP in the Yeast Saccharomyces cerevisiae using a New Type of Nanobiosensor. J Biol Chem 285(48):37579-88
Kucharczyk R, et al.  (2009) Introducing the human Leigh syndrome mutation T9176G into Saccharomyces cerevisiae mitochondrial DNA leads to severe defects in the incorporation of Atp6p into the ATP synthase and in the mitochondrial morphology. Hum Mol Genet 18(15):2889-98
Olsen LF, et al.  (2009) Regulation of glycolytic oscillations by mitochondrial and plasma membrane H+-ATPases. Biophys J 96(9):3850-61
Lau WC, et al.  (2008) Cryo-EM structure of the yeast ATP synthase. J Mol Biol 382(5):1256-64
Wittig I, et al.  (2008) Characterization of domain interfaces in monomeric and dimeric ATP synthase. Mol Cell Proteomics 7(5):995-1004
Corvest V, et al.  (2007) Insight into the bind-lock mechanism of the yeast mitochondrial ATP synthase inhibitory Peptide. Biochemistry 46(29):8680-8
Zeng X, et al.  (2007) The leader Peptide of yeast atp6p is required for efficient interaction with the atp9p ring of the mitochondrial ATPase. J Biol Chem 282(50):36167-76
Zeng X, et al.  (2007) The metalloprotease encoded by ATP23 has a dual function in processing and assembly of subunit 6 of mitochondrial ATPase. Mol Biol Cell 18(2):617-26
Gavin PD, et al.  (2004) Cross-linking ATP synthase complexes in vivo eliminates mitochondrial cristae. J Cell Sci 117(Pt 11):2333-43
Tzagoloff A, et al.  (2004) Atp10p assists assembly of Atp6p into the F0 unit of the yeast mitochondrial ATPase. J Biol Chem 279(19):19775-80
Chacinska A, et al.  (2000) Prion-dependent switching between respiratory competence and deficiency in the yeast nam9-1 mutant. Mol Cell Biol 20(19):7220-9
Paumard P, et al.  (2000) Environmental study of subunit i, a F(o) component of the yeast ATP synthase. Biochemistry 39(14):4199-205
Velours J, et al.  (2000) Organisation of the yeast ATP synthase F(0):a study based on cysteine mutants, thiol modification and cross-linking reagents. Biochim Biophys Acta 1458(2-3):443-56
de Jong L, et al.  (2000) Increased synthesis and decreased stability of mitochondrial translation products in yeast as a result of loss of mitochondrial (NAD(+))-dependent isocitrate dehydrogenase. FEBS Lett 483(1):62-6
Choo WM, et al.  (1985) Mitochondrial adenosine triphosphatase in mit- mutants of Saccharomyces cerevisiase with defective subunit 6 of the enzyme complex. Biochim Biophys Acta 806(2):290-304
Macino G and Tzagoloff A  (1980) Assembly of the mitochondrial membrane system: sequence analysis of a yeast mitochondrial ATPase gene containing the oli-2 and oli-4 loci. Cell 20(2):507-17
Roberts H, et al.  (1979) mit- Mutations in the oli2 region of mitochondrial DNA affecting the 20 000 dalton subunit of the mitochondrial ATPase in Saccharomyces cerevisiae. FEBS Lett 108(2):501-4
Ebner E and Schatz G  (1973) Mitochondrial assembly in respiration-deficient mutants of Saccharomyces cerevisiae. 3. A nuclear mutant lacking mitochondrial adenosine triphosphatase. J Biol Chem 248(15):5379-84
Tzagoloff A  (1971) Assembly of the mitochondrial membrane system. IV. Role of mitochondrial and cytoplasmic protein synthesis in the biosynthesis of the rutamycin-sensitive adenosine triphosphatase. J Biol Chem 246(9):3050-6
Tzagoloff A and Meagher P  (1971) Assembly of the mitochondrial membrane system. V. Properties of a dispersed preparation of the rutamycin-sensitive adenosine triphosphatase of yeast mitochondria. J Biol Chem 246(23):7328-36
Schatz G, et al.  (1967) Partial resolution of the enzymes catalyzing oxidative phosphorylation. XIV. J Biol Chem 242(10):2552-60