Mitochondrial proton-transporting ATP synthase complex

Primary Literature

Lerouley O, et al. (2025) An alternative mechanism by which If1 prevents ATP hydrolysis by the ATP synthase subcomplex in S. cerevisiae. EMBO Rep 26(13):3305-3326 PMID: 40490602
Buzzard E, et al. (2024) The consequence of ATP synthase dimer angle on mitochondrial morphology studied by cryo-electron tomography. Biochem J 481(3):161-75 PMID: 38164968
Panja C, et al. (2023) ATP synthase interactome analysis identifies a new subunit l as a modulator of permeability transition pore in yeast. Sci Rep 13(1):3839 PMID: 36882574
Frasch WD, et al. (2022) O ATP synthase molecular motor mechanisms. Front Microbiol 13: 965620. PMID: 36081786
Guo H and Rubinstein JL (2022) Structure of ATP synthase under strain during catalysis. Nat Commun 13(1):2232 PMID: 35468906
Naumenko N, et al. (2017) INA complex liaises the F1Fo-ATP synthase membrane motor modules. Nat Commun 8(1):1237 PMID: 29093463
Xu T, et al. (2015) Understanding structure, function, and mutations in the mitochondrial ATP synthase. Microb Cell 2(4):105-125 PMID: 25938092
Davies KM, et al. (2012) Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae. Proc Natl Acad Sci U S A 109(34):13602-7 PMID: 22864911
Pagadala V, et al. (2011) Characterization of the mitochondrial ATP synthase from yeast Saccharomyces cerevisae. J Bioenerg Biomembr 43(4):333-47 PMID: 21748405
Rak M, et al. (2011) Modular assembly of yeast mitochondrial ATP synthase. EMBO J 30(5):920-30 PMID: 21266956
Dautant A, et al. (2010) Crystal structure of the Mg·ADP-inhibited state of the yeast F1c10-ATP synthase. J Biol Chem 285(38):29502-10 PMID: 20610387
Förster 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 PMID: 20691145
Bueler SA and Rubinstein JL (2008) Location of subunit d in the peripheral stalk of the ATP synthase from Saccharomyces cerevisiae. Biochemistry 47(45):11804-10 PMID: 18937496
Lau WC, et al. (2008) Cryo-EM structure of the yeast ATP synthase. J Mol Biol 382(5):1256-64 PMID: 18722382
Rubinstein JL, et al. (2005) ATP synthase from Saccharomyces cerevisiae: location of subunit h in the peripheral stalk region. J Mol Biol 345(3):513-20 PMID: 15581895
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 PMID: 14998992
Paumard P, et al. (2000) Environmental study of subunit i, a F(o) component of the yeast ATP synthase. Biochemistry 39(14):4199-205 PMID: 10747812
Spannagel C, et al. (1998) Topography of the yeast ATP synthase F0 sector by using cysteine substitution mutants. Cross-linkings between subunits 4, 6, and f. Biochemistry 37(2):615-21 PMID: 9425084
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 PMID: 4256832
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Additional Literature

Ito T, et al. (2025) Yeast Model System Showed That Heterologously Expressed Mutant Atp9 Has a Negative Impact on Cell Growth by Causing ATP Depletion. Biol Pharm Bull 48(7):1070-1078 PMID: 40707212

Hazan Ben-Menachem R, et al. (2023) Mitochondrial-derived vesicles retain membrane potential and contain a functional ATP synthase. EMBO Rep 24(5):e56114 PMID: 36929726

Sinha SD and Wideman JG (2023) The persistent homology of mitochondrial ATP synthases. iScience 26(5):106700 PMID: 37250340

Cadena LR, et al. (2021) Mitochondrial Contact Site and Cristae Organization System and F1FO-ATP Synthase Crosstalk Is a Fundamental Property of Mitochondrial Cristae. mSphere 6(3):e0032721 PMID: 34133204

Franco LVR, et al. (2020) Atco, a yeast mitochondrial complex of Atp9 and Cox6, is an assembly intermediate of the ATP synthase. PLoS One 15(5):e0233177 PMID: 32413073

Wagner K, et al. (2009) Mitochondrial F1Fo-ATP synthase: the small subunits e and g associate with monomeric complexes to trigger dimerization. J Mol Biol 392(4):855-61 PMID: 19635484

Fronzes R, et al. (2006) The peripheral stalk participates in the yeast ATP synthase dimerization independently of e and g subunits. Biochemistry 45(21):6715-23 PMID: 16716082

Saddar S and Stuart RA (2005) The yeast F(1)F(0)-ATP synthase: analysis of the molecular organization of subunit g and the importance of a conserved GXXXG motif. J Biol Chem 280(26):24435-42 PMID: 15886192

Stephens AN, et al. (2003) The molecular neighborhood of subunit 8 of yeast mitochondrial F1F0-ATP synthase probed by cysteine scanning mutagenesis and chemical modification. J Biol Chem 278(20):17867-75 PMID: 12626501

Giraud MF, et al. (2002) Is there a relationship between the supramolecular organization of the mitochondrial ATP synthase and the formation of cristae? Biochim Biophys Acta 1555(1-3):174-80 PMID: 12206911

Arnold I, et al. (1999) ATP synthase of yeast mitochondria. Isolation of subunit j and disruption of the ATP18 gene. J Biol Chem 274(1):36-40 PMID: 9867807

Yao B and Mueller DM (1999) The role of the amino-terminal beta-barrel domain of the alpha and beta subunits in the yeast F1-ATPase. J Bioenerg Biomembr 31(2):95-104 PMID: 10449236

Velours J, et al. (1998) Topography of the yeast ATP synthase F0 sector. Biochimie 80(10):793-801 PMID: 9893937

Arnold I, et al. (1997) Yeast mitochondrial F1F0-ATPase: the novel subunit e is identical to Tim11. FEBS Lett 411(2-3):195-200 PMID: 9271204

Reviews

Eldeeb MH, et al. (2024) Mitochondrial respiratory supercomplexes of the yeast Saccharomyces cerevisiae. IUBMB Life 76(8):485-504 PMID: 38529880

Frigo E, et al. (2023) The Haves and Have-Nots: The Mitochondrial Permeability Transition Pore across Species. Cells 12(10) PMID: 37408243

Marshansky V (2022) Discovery and Study of Transmembrane Rotary Ion-Translocating Nano-Motors: F-ATPase/Synthase of Mitochondria/Bacteria and V-ATPase of Eukaryotic Cells. Biochemistry (Mosc) 87(8):702-719 PMID: 36171652

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Reviews

Mitochondrial proton-transporting ATP synthase complex Literature

Primary Literature

Additional Literature