scholarly journals Characterisation of a highly diverged mitochondrial ATP synthase peripheral stalk subunit b in Trypanosoma brucei

2021 ◽  
Author(s):  
Caroline E. Dewar ◽  
Silke Oeljeklaus ◽  
Bettina Warscheid ◽  
André Schneider
Keyword(s):  
Cell Cycle ◽  
Membrane Potential ◽  
Trypanosoma Brucei ◽  
Atp Synthase ◽  
Mitochondrial Protein ◽  
Normal Growth ◽  
Native Page ◽  
Peripheral Stalk ◽  
Mitochondrial Atp Synthase ◽  
Subunit B

The mitochondrial F1Fo ATP synthase of Trypanosoma brucei has been studied in detail. Whereas its F1 moiety is relatively highly conserved in structure and composition, the same is not the case for the Fo part and the peripheral stalk. A core subunit of the latter, the normally conserved subunit b, could not be identified in trypanosomes suggesting that it might be absent. Here we have identified a 17 kDa mitochondrial protein of the inner membrane that is essential for normal growth, efficient oxidative phosphorylation and membrane potential maintenance. Pulldown experiments and native PAGE analysis indicate that the protein is associated with the F1Fo ATP synthase. Its ablation reduces the levels of Fo subunits, but not those of F1, and disturbs the cell cycle. HHpred analysis showed that the protein has structural similarities to subunit b of other species, indicating that the Fo part of the trypanosomal ATP synthase does contain a highly diverged subunit b. Thus, the Fo part of the trypanosomal ATPase synthase may be more widely conserved than initially thought.

scholarly journals The ATP Synthase Deficiency in Human Diseases

Life ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 325
Author(s):  
Chiara Galber ◽  
Stefania Carissimi ◽  
Alessandra Baracca ◽  
Valentina Giorgio
Keyword(s):  
Oxidative Phosphorylation ◽  
Atp Synthase ◽  
Mitochondrial Protein ◽  
High Energy ◽  
Neurocognitive Disorders ◽  
Human Diseases ◽  
Age Related ◽  
Muscle Tissues ◽  
Mitochondrial Atp Synthase ◽  
Genes Encoding

Human diseases range from gene-associated to gene-non-associated disorders, including age-related diseases, neurodegenerative, neuromuscular, cardiovascular, diabetic diseases, neurocognitive disorders and cancer. Mitochondria participate to the cascades of pathogenic events leading to the onset and progression of these diseases independently of their association to mutations of genes encoding mitochondrial protein. Under physiological conditions, the mitochondrial ATP synthase provides the most energy of the cell via the oxidative phosphorylation. Alterations of oxidative phosphorylation mainly affect the tissues characterized by a high-energy metabolism, such as nervous, cardiac and skeletal muscle tissues. In this review, we focus on human diseases caused by altered expressions of ATP synthase genes of both mitochondrial and nuclear origin. Moreover, we describe the contribution of ATP synthase to the pathophysiological mechanisms of other human diseases such as cardiovascular, neurodegenerative diseases or neurocognitive disorders.

scholarly journals Structure of the mitochondrial ATP synthase from Pichia angusta determined by electron cryo-microscopy

2016 ◽  
Vol 113 (45) ◽  
pp. 12709-12714 ◽  
Author(s):  
Kutti R. Vinothkumar ◽  
Martin G. Montgomery ◽  
Sidong Liu ◽  
John E. Walker
Keyword(s):  
Atp Synthase ◽  
Catalytic Domain ◽  
Lateral Force ◽  
Membrane Domain ◽  
Subunit A ◽  
Mechanical Coupling ◽  
Peripheral Stalk ◽  
Mitochondrial Atp Synthase ◽  
A Subunit ◽  
Pichia Angusta

The structure of the intact monomeric ATP synthase from the fungus, Pichia angusta, has been solved by electron cryo-microscopy. The structure provides insights into the mechanical coupling of the transmembrane proton motive force across mitochondrial membranes in the synthesis of ATP. This mechanism requires a strong and integral stator, consisting of the catalytic α3β3-domain, peripheral stalk, and, in the membrane domain, subunit a and associated supernumerary subunits, kept in contact with the rotor turning at speeds up to 350 Hz. The stator’s integrity is ensured by robust attachment of both the oligomycin sensitivity conferral protein (OSCP) to the catalytic domain and the membrane domain of subunit b to subunit a. The ATP8 subunit provides an additional brace between the peripheral stalk and subunit a. At the junction between the OSCP and the apparently stiff, elongated α-helical b-subunit and associated d- and h-subunits, an elbow or joint allows the stator to bend to accommodate lateral movements during the activity of the catalytic domain. The stator may also apply lateral force to help keep the static a-subunit and rotating c10-ring together. The interface between the c10-ring and the a-subunit contains the transmembrane pathway for protons, and their passage across the membrane generates the turning of the rotor. The pathway has two half-channels containing conserved polar residues provided by a bundle of four α-helices inclined at ∼30° to the plane of the membrane, similar to those described in other species. The structure provides more insights into the workings of this amazing machine.

scholarly journals Near-Neighbor Relationships of the Atypical Subunits that Form the Peripheral Stalk of the Mitochondrial ATP Synthase in Chlorophycean Algae

2017 ◽  
Vol 112 (3) ◽  
pp. 2a-3a
Author(s):  
Miriam Vázquez-Acevedo ◽  
Félix Vega-DeLuna ◽  
Lorenzo Sánchez-Vásquez ◽  
Lilia Colina-Tenorio ◽  
Claire Remacle ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Near Neighbor ◽  
Peripheral Stalk ◽  
Mitochondrial Atp Synthase ◽  
Neighbor Relationships

The mitochondrial ATP synthase of Trypanosoma brucei: Developmental regulation through the life cycle

1991 ◽  
Vol 288 (2) ◽  
pp. 509-515 ◽  
Author(s):  
Noreen Williams ◽  
Stella Y.-W. Choi ◽  
William T. Ruyechan ◽  
Peter H. Frank
Keyword(s):  
Life Cycle ◽  
Trypanosoma Brucei ◽  
Atp Synthase ◽  
Developmental Regulation ◽  
Mitochondrial Atp Synthase

scholarly journals IF1, a natural inhibitor of mitochondrial ATP synthase, is not essential for the normal growth and breeding of mice

2013 ◽  
Vol 33 (5) ◽  
Author(s):  
Junji Nakamura ◽  
Makoto Fujikawa ◽  
Masasuke Yoshida
Keyword(s):  
Atp Synthase ◽  
Mouse Strain ◽  
Reactive Oxygen Species Generation ◽  
Atp Synthesis ◽  
Normal Growth ◽  
Test Results ◽  
Mitochondrial Atp Synthase ◽  
Evolutionarily Conserved ◽  
Natural Inhibitor ◽  
Synthesis Activity

IF1 is an endogenous inhibitor protein of mitochondrial ATP synthase. It is evolutionarily conserved throughout all eukaryotes and it has been proposed to play crucial roles in prevention of the wasteful reverse reaction of ATP synthase, in the metabolic shift from oxidative phosphorylation to glycolysis, in the suppression of ROS (reactive oxygen species) generation, in mitochondria morphology and in haem biosynthesis in mitochondria, which leads to anaemia. Here, we report the phenotype of a mouse strain in which IF1 gene was destroyed. Unexpectedly, individuals of this IF1-KO (knockout) mouse strain grew and bred without defect. The general behaviours, blood test results and responses to starvation of the IF1-KO mice were apparently normal. There were no abnormalities in the tissue anatomy or the autophagy. Mitochondria of the IF1-KO mice were normal in morphology, in the content of ATP synthase molecules and in ATP synthesis activity. Thus, IF1 is not an essential protein for mice despite its ubiquitous presence in eukaryotes.

scholarly journals Mitochondrial ATP Synthase Subunit d, a Component of the Peripheral Stalk, is Essential for Growth and Heat Stress Tolerance in Arabidopsis thaliana

2021 ◽  
Author(s):  
Tianxiang Liu ◽  
Jesse Arsenault ◽  
Elizabeth Vierling ◽  
Minsoo Kim
Keyword(s):  
Arabidopsis Thaliana ◽  
Heat Stress ◽  
Plant Growth ◽  
Mitochondrial Dysfunction ◽  
Stress Tolerance ◽  
Atp Synthase ◽  
Peripheral Stalk ◽  
Cellular Processes ◽  
Mitochondrial Atp Synthase ◽  
Heat Stress Tolerance

SUMMARYAs rapid changes in climate threaten global crop yields, an understanding of plant heat stress tolerance is increasingly relevant. Heat stress tolerance involves the coordinated action of many cellular processes and is particularly energy demanding. We acquired a knockout mutant and generated knockdown lines in Arabidopsis thaliana of the d subunit of mitochondrial ATP synthase (gene name: ATPQ, AT3G52300, referred to hereafter as ATPd), a subunit of the peripheral stalk, and used these to investigate the phenotypic significance of this subunit in normal growth and heat stress tolerance. Homozygous knockout mutants for ATPd could not be obtained due to gametophytic defects, while heterozygotes possess no visible phenotype. Therefore, we used RNAi to create knockdown plant lines for further studies. Proteomic analysis and blue native gels revealed that ATPd downregulation impairs only subunits of the mitochondrial ATP synthase (complex V of the electron transport chain). Knockdown plants were more sensitive to heat stress, had abnormal leaf morphology, and were severely slow growing compared to wild type. These results indicate that ATPd plays a crucial role in proper function of the mitochondrial ATP synthase holoenzyme, which, when reduced, leads to wide-ranging defects in energy-demanding cellular processes. In knockdown plants, more hydrogen peroxide accumulated and mitochondrial dysfunction stimulon (MDS) genes were activated. These data establish the essential structural role of ATPd and provide new information about complex V assembly and quality control, as well as support the importance of mitochondrial respiration in normal plant growth and heat stress tolerance.SIGNIFICANCE STATEMENTThe energy converter, mitochondrial ATP synthase, is critical for all organisms, but the functional importance of ATP synthase subunit d remains largely unknown in plants. We demonstrate the contributions of subunit d to plant growth, development, and heat stress tolerance, as well as to ATP synthase stability, ROS signaling and mitochondrial dysfunction regulation.

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