Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
J. Bioenerg. Biomembr. 34, 389-395 (2002)[PubMed:12539966]
Animals that are copper deficient have cardiac hypertrophy where there is a dramatic increase in mitochondria. Mitochondrial biogenesis is enhanced in this model and there is an upregulation of mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2). While the cuproenzyme, cytochrome c oxidase (CCO), is an attractive candidate to explain the connection between cardiac hypertrophy in copper deficiency and subsequent mitochondrial biogenesis, studies have revealed that ATP synthase may be impacted by copper depletion. NRF-1 and NRF-2 can bind to some of the subunits of both CCO and ATP synthase to regulate gene expression. Furthermore, oxidative phosphorylation appears to occur unaltered in the copper-deficient state. Copper-deficient mitochondria appear to be less sensitive to the inhibitory effect of oligomycin compared to controls. Decreases in the delta subunit protein and beta mRNA transcript have been reported for ATP synthase as a function of copper deficiency. The limited data available suggest that copper, either indirectly or directly, alters ATP synthase function.
J. Bioenerg. Biomembr. 34, 389-395 (2002)[PubMed:12539966]
Animals that are copper deficient have cardiac hypertrophy where there is a dramatic increase in mitochondria. Mitochondrial biogenesis is enhanced in this model and there is an upregulation of mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2). While the cuproenzyme, cytochrome c oxidase (CCO), is an attractive candidate to explain the connection between cardiac hypertrophy in copper deficiency and subsequent mitochondrial biogenesis, studies have revealed that ATP synthase may be impacted by copper depletion. NRF-1 and NRF-2 can bind to some of the subunits of both CCO and ATP synthase to regulate gene expression. Furthermore, oxidative phosphorylation appears to occur unaltered in the copper-deficient state. Copper-deficient mitochondria appear to be less sensitive to the inhibitory effect of oligomycin compared to controls. Decreases in the delta subunit protein and beta mRNA transcript have been reported for ATP synthase as a function of copper deficiency. The limited data available suggest that copper, either indirectly or directly, alters ATP synthase function.
Human mitochondrial F(1)F(0) ATP synthase was isolated with a one-step immunological approach, using a monoclonal antibody against F(1) in a 96-well microplate activity assay system, to establish a method for fast high throughput screening of inhibitors, toxins, and drugs with very small amounts of enzyme. For preparative purification, mitochondria from human heart tissue as well as cultured fibroblasts were solubilized with dodecyl-beta-d-maltoside, and the F(1)F(0) was isolated with anti-F(1) monoclonal antibody coupled to protein G-agarose beads. The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection. Microscale immunocapture of F(1)F(0) from detergent-solubilized mitochondria or whole cell fibroblast extracts was performed using anti-F(1) monoclonal antibody immobilized on 96-well microplates. The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive. Moreover, IF(1) could be co-isolated with F(1)F(0) when the immunocapture procedure was carried out at pH 6.5 but was absent when the ATP synthase was isolated at pH 8.0. Immunocaptured F(1)F(0) lacking IF(1) could be inhibited by more than 90% by addition of recombinant inhibitor protein, and conversely, F(1)F(0) containing IF(1) could be activated more than 10-fold by brief exposure to pH 8.0, inducing the release of inhibitor protein. With this microplate system an ATP hydrolysis assay of complex V could be carried out with as little as 10 ng of heart mitochondria/well and as few as 3 x 10(4) cells/well from fibroblast cultures. The system is therefore suitable to screen patient-derived samples for alterations in amount or functionality of both the F(1)F(0) ATPase and IF(1).
Hydrogen ion transporting ATP synthase activity, rotational mechanismdefinition[GO:0046933]‹silver
Catalysis of protons from one side of a membrane to the other according to the reaction: ADP + phosphate = ATP + H2O, coupled with transport of H+ down a concentration gradient, by a rotational mechanism.
Catalysis of the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism.
Human mitochondrial F(1)F(0) ATP synthase was isolated with a one-step immunological approach, using a monoclonal antibody against F(1) in a 96-well microplate activity assay system, to establish a method for fast high throughput screening of inhibitors, toxins, and drugs with very small amounts of enzyme. For preparative purification, mitochondria from human heart tissue as well as cultured fibroblasts were solubilized with dodecyl-beta-d-maltoside, and the F(1)F(0) was isolated with anti-F(1) monoclonal antibody coupled to protein G-agarose beads. The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection. Microscale immunocapture of F(1)F(0) from detergent-solubilized mitochondria or whole cell fibroblast extracts was performed using anti-F(1) monoclonal antibody immobilized on 96-well microplates. The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive. Moreover, IF(1) could be co-isolated with F(1)F(0) when the immunocapture procedure was carried out at pH 6.5 but was absent when the ATP synthase was isolated at pH 8.0. Immunocaptured F(1)F(0) lacking IF(1) could be inhibited by more than 90% by addition of recombinant inhibitor protein, and conversely, F(1)F(0) containing IF(1) could be activated more than 10-fold by brief exposure to pH 8.0, inducing the release of inhibitor protein. With this microplate system an ATP hydrolysis assay of complex V could be carried out with as little as 10 ng of heart mitochondria/well and as few as 3 x 10(4) cells/well from fibroblast cultures. The system is therefore suitable to screen patient-derived samples for alterations in amount or functionality of both the F(1)F(0) ATPase and IF(1).
Two types of cDNA clones encoding a precursor of the delta-subunit of the human mitochondrial F0F1 ATP synthase complex (EC 3.6.1.34) have been isolated from a human cDNA library. Both clones contain a 504 basepair open reading frame that encodes a polypeptide with a presequence 22 amino acids in length and a mature protein 146 residues in length. The difference between the two types of cDNA clones is the presence of a 296 basepair insert in the 3' untranslated region of the delta-subunit cDNA in one of the types.
The chemical reactions and pathways resulting in the formation of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
J. Bioenerg. Biomembr. 34, 389-395 (2002)[PubMed:12539966]
Animals that are copper deficient have cardiac hypertrophy where there is a dramatic increase in mitochondria. Mitochondrial biogenesis is enhanced in this model and there is an upregulation of mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2). While the cuproenzyme, cytochrome c oxidase (CCO), is an attractive candidate to explain the connection between cardiac hypertrophy in copper deficiency and subsequent mitochondrial biogenesis, studies have revealed that ATP synthase may be impacted by copper depletion. NRF-1 and NRF-2 can bind to some of the subunits of both CCO and ATP synthase to regulate gene expression. Furthermore, oxidative phosphorylation appears to occur unaltered in the copper-deficient state. Copper-deficient mitochondria appear to be less sensitive to the inhibitory effect of oligomycin compared to controls. Decreases in the delta subunit protein and beta mRNA transcript have been reported for ATP synthase as a function of copper deficiency. The limited data available suggest that copper, either indirectly or directly, alters ATP synthase function.
The chemical reactions and pathways resulting in the breakdown of ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
J. Bioenerg. Biomembr. 34, 389-395 (2002)[PubMed:12539966]
Animals that are copper deficient have cardiac hypertrophy where there is a dramatic increase in mitochondria. Mitochondrial biogenesis is enhanced in this model and there is an upregulation of mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2). While the cuproenzyme, cytochrome c oxidase (CCO), is an attractive candidate to explain the connection between cardiac hypertrophy in copper deficiency and subsequent mitochondrial biogenesis, studies have revealed that ATP synthase may be impacted by copper depletion. NRF-1 and NRF-2 can bind to some of the subunits of both CCO and ATP synthase to regulate gene expression. Furthermore, oxidative phosphorylation appears to occur unaltered in the copper-deficient state. Copper-deficient mitochondria appear to be less sensitive to the inhibitory effect of oligomycin compared to controls. Decreases in the delta subunit protein and beta mRNA transcript have been reported for ATP synthase as a function of copper deficiency. The limited data available suggest that copper, either indirectly or directly, alters ATP synthase function.
Human mitochondrial F(1)F(0) ATP synthase was isolated with a one-step immunological approach, using a monoclonal antibody against F(1) in a 96-well microplate activity assay system, to establish a method for fast high throughput screening of inhibitors, toxins, and drugs with very small amounts of enzyme. For preparative purification, mitochondria from human heart tissue as well as cultured fibroblasts were solubilized with dodecyl-beta-d-maltoside, and the F(1)F(0) was isolated with anti-F(1) monoclonal antibody coupled to protein G-agarose beads. The immunoprecipitated F(1)F(0) contained a full complement of subunits that were identified with specific antibodies against five of the subunits (alpha, beta, OSCP, d, and IF(1)) and by MALDI-TOF and/or LC/MS/MS for all subunits except subunit c, which could not be resolved by these methods because of the limits of detection. Microscale immunocapture of F(1)F(0) from detergent-solubilized mitochondria or whole cell fibroblast extracts was performed using anti-F(1) monoclonal antibody immobilized on 96-well microplates. The captured complex V displayed ATP hydrolysis activity that was fully oligomycin and inhibitor protein IF(1)-sensitive. Moreover, IF(1) could be co-isolated with F(1)F(0) when the immunocapture procedure was carried out at pH 6.5 but was absent when the ATP synthase was isolated at pH 8.0. Immunocaptured F(1)F(0) lacking IF(1) could be inhibited by more than 90% by addition of recombinant inhibitor protein, and conversely, F(1)F(0) containing IF(1) could be activated more than 10-fold by brief exposure to pH 8.0, inducing the release of inhibitor protein. With this microplate system an ATP hydrolysis assay of complex V could be carried out with as little as 10 ng of heart mitochondria/well and as few as 3 x 10(4) cells/well from fibroblast cultures. The system is therefore suitable to screen patient-derived samples for alterations in amount or functionality of both the F(1)F(0) ATPase and IF(1).
J. Bioenerg. Biomembr. 34, 389-395 (2002)[PubMed:12539966]
Animals that are copper deficient have cardiac hypertrophy where there is a dramatic increase in mitochondria. Mitochondrial biogenesis is enhanced in this model and there is an upregulation of mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2). While the cuproenzyme, cytochrome c oxidase (CCO), is an attractive candidate to explain the connection between cardiac hypertrophy in copper deficiency and subsequent mitochondrial biogenesis, studies have revealed that ATP synthase may be impacted by copper depletion. NRF-1 and NRF-2 can bind to some of the subunits of both CCO and ATP synthase to regulate gene expression. Furthermore, oxidative phosphorylation appears to occur unaltered in the copper-deficient state. Copper-deficient mitochondria appear to be less sensitive to the inhibitory effect of oligomycin compared to controls. Decreases in the delta subunit protein and beta mRNA transcript have been reported for ATP synthase as a function of copper deficiency. The limited data available suggest that copper, either indirectly or directly, alters ATP synthase function.
The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.
J. Bioenerg. Biomembr. 34, 389-395 (2002)[PubMed:12539966]
Animals that are copper deficient have cardiac hypertrophy where there is a dramatic increase in mitochondria. Mitochondrial biogenesis is enhanced in this model and there is an upregulation of mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2). While the cuproenzyme, cytochrome c oxidase (CCO), is an attractive candidate to explain the connection between cardiac hypertrophy in copper deficiency and subsequent mitochondrial biogenesis, studies have revealed that ATP synthase may be impacted by copper depletion. NRF-1 and NRF-2 can bind to some of the subunits of both CCO and ATP synthase to regulate gene expression. Furthermore, oxidative phosphorylation appears to occur unaltered in the copper-deficient state. Copper-deficient mitochondria appear to be less sensitive to the inhibitory effect of oligomycin compared to controls. Decreases in the delta subunit protein and beta mRNA transcript have been reported for ATP synthase as a function of copper deficiency. The limited data available suggest that copper, either indirectly or directly, alters ATP synthase function.
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a copper ion stimulus.
J. Bioenerg. Biomembr. 34, 389-395 (2002)[PubMed:12539966]
Animals that are copper deficient have cardiac hypertrophy where there is a dramatic increase in mitochondria. Mitochondrial biogenesis is enhanced in this model and there is an upregulation of mitochondrial transcription factor A (mtTFA) and nuclear respiratory factors 1 and 2 (NRF-1 and NRF-2). While the cuproenzyme, cytochrome c oxidase (CCO), is an attractive candidate to explain the connection between cardiac hypertrophy in copper deficiency and subsequent mitochondrial biogenesis, studies have revealed that ATP synthase may be impacted by copper depletion. NRF-1 and NRF-2 can bind to some of the subunits of both CCO and ATP synthase to regulate gene expression. Furthermore, oxidative phosphorylation appears to occur unaltered in the copper-deficient state. Copper-deficient mitochondria appear to be less sensitive to the inhibitory effect of oligomycin compared to controls. Decreases in the delta subunit protein and beta mRNA transcript have been reported for ATP synthase as a function of copper deficiency. The limited data available suggest that copper, either indirectly or directly, alters ATP synthase function.
Protein involved in the synthesis of adenosine 5'-triphosphate (ATP). ATP is a ribonucleotide adenosine (a purine base adenine linked to the sugar D-ribofuranose) which carries 3 phosphate groups esterified to the sugar moiety. It is the cell's source for energy and phosphate.
Protein involved in the transport of ions. Such proteins are usually transmembrane and mediate a movement of ions across cell membranes. Transport may be passive (facilitated diffusion; down the electrochemical gradient), or active (against the electrochemical gradient). Active transport requires energy which may come from light, oxidation reactions, ATP hydrolysis, or cotransport of other ions or molecules.
Protein involved in the transport of a molecule (metabolite, protein, etc), a ion or an electron across cell membranes, inside the cell or in a tissue fluid.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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