Assembly factors of F1Fo-ATP synthase across genomes

2005 ◽  
Vol 59 (3) ◽  
pp. 393-402 ◽  
Author(s):  
Andrea Pícková ◽  
Martin Potocký ◽  
Josef Houštěk
Keyword(s):  
Atp Synthase ◽  
F1fo Atp Synthase ◽  
Assembly Factors

scholarly journals Impact of F1Fo-ATP-synthase dimer assembly factors on mitochondrial function and organismic aging

2018 ◽  
Vol 5 (4) ◽  
pp. 198-207 ◽  
Author(s):  
Nadia G Rampello ◽  
Maria Stenger ◽  
Benedikt Westermann ◽  
Heinz D Osiewacz
Keyword(s):  
Atp Synthase ◽  
Mitochondrial Function ◽  
F1fo Atp Synthase ◽  
Assembly Factors

Deletion of the natural inhibitory protein Inh1 in Ustilago maydis has no effect on the dimeric state of the F1FO-ATP synthase but increases the ATPase activity and reduces the stability

2021 ◽  
Vol 1862 (7) ◽  
pp. 148429
Author(s):  
Romero-Aguilar Lucero ◽  
Esparza-Perusquía Mercedes ◽  
Langner Thorsten ◽  
García-Cruz Giovanni ◽  
Feldbrügge Michael ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Atp Synthase ◽  
Ustilago Maydis ◽  
Inhibitory Protein ◽  
F1fo Atp Synthase ◽  
The Stability

scholarly journals Molecular and Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System: Implications for Pathology

Life ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 242
Author(s):  
Salvatore Nesci ◽  
Fabiana Trombetti ◽  
Alessandra Pagliarani ◽  
Vittoria Ventrella ◽  
Cristina Algieri ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Atp Synthase ◽  
Mitochondrial Permeability Transition ◽  
Ros Generation ◽  
Protonmotive Force ◽  
Mitochondrial Oxidative Phosphorylation ◽  
F1fo Atp Synthase ◽  
Functional Changes ◽  
Age Related ◽  
Mitochondrial Functions

Under aerobic conditions, mitochondrial oxidative phosphorylation (OXPHOS) converts the energy released by nutrient oxidation into ATP, the currency of living organisms. The whole biochemical machinery is hosted by the inner mitochondrial membrane (mtIM) where the protonmotive force built by respiratory complexes, dynamically assembled as super-complexes, allows the F1FO-ATP synthase to make ATP from ADP + Pi. Recently mitochondria emerged not only as cell powerhouses, but also as signaling hubs by way of reactive oxygen species (ROS) production. However, when ROS removal systems and/or OXPHOS constituents are defective, the physiological ROS generation can cause ROS imbalance and oxidative stress, which in turn damages cell components. Moreover, the morphology of mitochondria rules cell fate and the formation of the mitochondrial permeability transition pore in the mtIM, which, most likely with the F1FO-ATP synthase contribution, permeabilizes mitochondria and leads to cell death. As the multiple mitochondrial functions are mutually interconnected, changes in protein composition by mutations or in supercomplex assembly and/or in membrane structures often generate a dysfunctional cascade and lead to life-incompatible diseases or severe syndromes. The known structural/functional changes in mitochondrial proteins and structures, which impact mitochondrial bioenergetics because of an impaired or defective energy transduction system, here reviewed, constitute the main biochemical damage in a variety of genetic and age-related diseases.

scholarly journals The spatio-temporal organization of mitochondrial F1FO ATP synthase in cristae depends on its activity mode

2020 ◽  
Vol 1861 (1) ◽  
pp. 148091 ◽  
Author(s):  
Kirill Salewskij ◽  
Bettina Rieger ◽  
Frances Hager ◽  
Tasnim Arroum ◽  
Patrick Duwe ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Temporal Organization ◽  
F1fo Atp Synthase ◽  
Activity Mode ◽  
Spatio Temporal

Attenuation of the hypoxia-induced protein kinase Cδ interaction with the ‘d’ subunit of F1Fo-ATP synthase in neonatal cardiac myocytes: implications for energy preservation and survival

2010 ◽  
Vol 429 (2) ◽  
pp. 335-345 ◽  
Author(s):  
Tiffany T. Nguyen ◽  
Mourad Ogbi ◽  
Qilin Yu ◽  
John A. Johnson
Keyword(s):  
Protein Kinase ◽  
Atpase Activity ◽  
Atp Synthase ◽  
Mitochondrial Targeting ◽  
F1fo Atp Synthase ◽  
Hiv Tat ◽  
F1fo Atpase ◽  
D Subunit ◽  
Mitochondrial Targeting Sequences ◽  
Protein Kinase Cδ

The F1Fo-ATP synthase provides most of the heart's energy, yet events that alter its function during injury are poorly understood. Recently, we described a potent inhibitory effect on F1Fo-ATP synthase function mediated by the interaction of PKCδ (protein kinase Cδ) with dF1Fo (‘d’ subunit of the F1Fo-ATPase/ATP synthase). We have now developed novel peptide modulators which facilitate or inhibit the PKCδ–dF1Fo interaction. These peptides include HIV-Tat (transactivator of transcription) protein transduction and mammalian mitochondrial-targeting sequences. Pre-incubation of NCMs (neonatal cardiac myocyte) with 10 nM extracellular concentrations of the mitochondrial-targeted PKCδ–dF1Fo interaction inhibitor decreased Hx (hypoxia)-induced co-IP (co-immunoprecipitation) of PKCδ with dF1Fo by 40±9%, abolished Hx-induced inhibition of F1Fo-ATPase activity, attenuated Hx-induced losses in F1Fo-derived ATP and protected against Hx- and reperfusion-induced cell death. A scrambled-sequence (inactive) peptide, which contained HIV-Tat and mitochondrial-targeting sequences, was without effect. In contrast, the cell-permeant mitochondrial-targeted PKCδ–dF1Fo facilitator peptide, which we have shown previously to induce the PKCδ–dF1Fo co-IP, was found to inhibit F1Fo-ATPase activity to an extent similar to that caused by Hx alone. The PKCδ–dF1Fo facilitator peptide also decreased ATP levels by 72±18% under hypoxic conditions in the presence of glycolytic inhibition. None of the PKCδ–dF1Fo modulatory peptides altered the inner mitochondrial membrane potential. Our studies provide the first evidence that disruption of the PKCδ–dF1Fo interaction using cell-permeant mitochondrial-targeted peptides attenuates cardiac injury resulting from prolonged oxygen deprivation.

Energy Transduction by the Two Molecular Motors of the F1Fo ATP Synthase

2011 ◽  
pp. 561-590 ◽  
Author(s):  
David Spetzler ◽  
Robert Ishmukhametov ◽  
Tassilo Hornung ◽  
James Martin ◽  
Justin York ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Molecular Motors ◽  
Energy Transduction ◽  
F1fo Atp Synthase

scholarly journals The F1Fo-ATP Synthase β Subunit Is Required for Candida albicans Pathogenicity Due to Its Role in Carbon Flexibility

2018 ◽  
Vol 9 ◽  
Author(s):  
Shui-Xiu Li ◽  
Hao-Tian Wu ◽  
Yu-Ting Liu ◽  
Yi-Ying Jiang ◽  
Yi-Shan Zhang ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Atp Synthase ◽  
Β Subunit ◽  
F1fo Atp Synthase
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