Key points are not available for this paper at this time.
The F1F0-ATP synthase in mitochondria, in addition to its function in energy transduction, has a structural role in determining cristae morphology. This depends on its ability to form dimeric and higher oligomeric supracomplexes. Here we show that mutants of the dimer-specific subunits e and g, which destabilize dimeric and oligomeric F1F0-ATP synthase supracomplexes, have a decreased mitochondrial membrane potential ΔΨ. The degree of destabilization correlated with the reduction of the membrane potential. The enzymatic activities of F1F0-ATP synthase and cytochrome c oxidase, maximal respiration rate, coupling of oxidative phosphorylation, and tubular mitochondrial morphology were not affected or only to a minor extent. In mutants lacking one or two coiled-coil domains of subunit e, the reduction of the mitochondrial membrane potential was not due to loss of mitochondrial DNA, a reduced capacity of oxidative phosphorylation, or to altered cristae morphology. We propose a role for the supracomplexes of the F1F0-ATP synthase in organizing microdomains within the inner membrane, ensuring optimal bioenergetic competence of mitochondria. The F1F0-ATP synthase in mitochondria, in addition to its function in energy transduction, has a structural role in determining cristae morphology. This depends on its ability to form dimeric and higher oligomeric supracomplexes. Here we show that mutants of the dimer-specific subunits e and g, which destabilize dimeric and oligomeric F1F0-ATP synthase supracomplexes, have a decreased mitochondrial membrane potential ΔΨ. The degree of destabilization correlated with the reduction of the membrane potential. The enzymatic activities of F1F0-ATP synthase and cytochrome c oxidase, maximal respiration rate, coupling of oxidative phosphorylation, and tubular mitochondrial morphology were not affected or only to a minor extent. In mutants lacking one or two coiled-coil domains of subunit e, the reduction of the mitochondrial membrane potential was not due to loss of mitochondrial DNA, a reduced capacity of oxidative phosphorylation, or to altered cristae morphology. We propose a role for the supracomplexes of the F1F0-ATP synthase in organizing microdomains within the inner membrane, ensuring optimal bioenergetic competence of mitochondria. Mitochondria fulfill a number of fundamental functions in eukaryotic cells. A prominent one is oxidative phosphorylation. Five major multisubunit complexes cooperate to transduce the energy of nutrient-derived substrates into the energy stored in ATP. Therefore mitochondria provide the majority of the ATP to the cell. The F1F0-ATP synthase is a rotary motor using the proton motive force across the mitochondrial inner membrane to synthesize ATP. In addition to this well established function, the F1F0-ATP synthase was recently shown to have a role in determining the ultrastructure of mitochondria (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 2Arselin G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, 4Giraud M.F. Paumard P. Soubannier V. Vaillier J. Arselin G. Salin B. Schaeffer J. Brethes D. di Rago J.P. Velours J. Biochim. Biophys. Acta. 2002; 1555: 174-180Crossref PubMed Scopus (99) Google Scholar). The F1F0-ATP synthase forms dimeric and higher oligomeric supracomplexes (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 2Arselin G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, 4Giraud M.F. Paumard P. Soubannier V. Vaillier J. Arselin G. Salin B. Schaeffer J. Brethes D. di Rago J.P. Velours J. Biochim. Biophys. Acta. 2002; 1555: 174-180Crossref PubMed Scopus (99) Google Scholar, 5Arnold I. Pfeiffer K. Neupert W. Stuart R.A. Schagger H. EMBO J. 1998; 17: 7170-7178Crossref PubMed Scopus (371) Google Scholar). Blue native (BN) 2The abbreviations used are: BN, blue native; CCCP, carbonyl cyanide 3-chlorophenylhydrazone; COX, cytochrome c oxidase; DiSC3, 3,3′-dipropylthiodicarbocyanide iodide; OXPHOS, oxidative phosphorylation; mtDNA, mitochondrial DNA; TMPD, tetramethyl-p-phenylenediamine; BisTris, 2-bis(2-hydroxyethyl)amino-2-(hydroxymethyl)propane-1,3-diol. -PAGE was instrumental as a novel tool to establish the existence of such supracomplexes (5Arnold I. Pfeiffer K. Neupert W. Stuart R.A. Schagger H. EMBO J. 1998; 17: 7170-7178Crossref PubMed Scopus (371) Google Scholar). The oligomerization depends on two subunits of the membrane-inserted F0 part, subunit e (Su e) and subunit g (Su g). The presence of each subunit is mutually dependent on the other. Both subunits are present in the dimeric and oligomeric forms but not the monomeric form of the F1F0-ATP synthase. The transmembrane segment of Su e a This is to the of two Su e G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar). within this in the Su as well as of the transmembrane of subunit to a loss of higher oligomeric complexes of the F1F0-ATP synthase G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, 4Giraud M.F. Paumard P. Soubannier V. Vaillier J. Arselin G. Salin B. Schaeffer J. Brethes D. di Rago J.P. Velours J. Biochim. Biophys. Acta. 2002; 1555: 174-180Crossref PubMed Scopus (99) Google Scholar). the coiled-coil of Su e was to the of F1F0-ATP synthase V. Stuart R.A. PubMed Scopus Google Scholar). In of of of the e, g, Su or mitochondria with cristae and of inner membrane (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 2Arselin G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, 4Giraud M.F. Paumard P. Soubannier V. Vaillier J. Arselin G. Salin B. Schaeffer J. Brethes D. di Rago J.P. Velours J. Biochim. Biophys. Acta. 2002; 1555: 174-180Crossref PubMed Scopus (99) Google Scholar). The enzymatic of the F1F0-ATP synthase was not affected in that subunits or domains are for the structural function for the of ATP (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, 4Giraud M.F. Paumard P. Soubannier V. Vaillier J. Arselin G. Salin B. Schaeffer J. Brethes D. di Rago J.P. Velours J. Biochim. Biophys. Acta. 2002; 1555: 174-180Crossref PubMed Scopus (99) Google Scholar, 5Arnold I. Pfeiffer K. Neupert W. Stuart R.A. Schagger H. EMBO J. 1998; 17: 7170-7178Crossref PubMed Scopus (371) Google Scholar, P. Eur. J. Biochem. PubMed Scopus Google Scholar). for a structural role of the higher oligomeric forms of the F1F0-ATP synthase that bioenergetic such as the of respiration or the are not altered in such mutants (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, P. Eur. J. Biochem. PubMed Scopus Google Scholar). mutants have a for which a is have phosphorylation, in cytochrome c was to in the g P. Eur. J. Biochem. PubMed Scopus Google Scholar). that this reduced cytochrome c is of of (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar). is not the altered cristae morphology to the we to of F1F0-ATP synthase supracomplexes has a on the bioenergetic of oxidative phosphorylation. are as the of supracomplexes and is this to altered cristae loss of mitochondrial DNA, and of oxidative Here we that the coiled-coil domains of Su e to the of F1F0-ATP synthase supracomplexes. not to a loss of mitochondrial are for cristae morphology. mutants that show a decreased of F1F0-ATP synthase supracomplexes have a decreased membrane potential. We propose that a of F1F0-ATP synthase to higher oligomeric is for of mitochondria. used are e g and of was to on or on Mitochondria were to M.F. B. Neupert W. PubMed Scopus Google Scholar). was on with The Su was of the using the and Su and Su the and were used with the The Su was with the and the Su The were into using and the were into the e to of in the membrane potential of and were 3,3′-dipropylthiodicarbocyanide or were Biochim. Biophys. Acta. PubMed Scopus Google Scholar, Biophys. J. Full Text Full Text PDF PubMed Scopus Google Scholar). for and for of mitochondria were used to the membrane potential with of as was to the membrane potential. The of the decreased addition of was used to the membrane potential using and of and of not to a of of the membrane potential. of the membrane potential ATP was and for and was to the membrane and the of ATP was to the of ATP and was to of the to was using the Su e were in of Su e to the of the the of Su g were in that to mitochondria of were in with the for the were to a g, and were of was and a H. Biol. PubMed Google Scholar). were in for in ATP for and addition of of to ATP in the of mitochondria were in of BisTris, The was of ATP and were The were to of Biochem. PubMed Scopus Google of of was and of was c c was in and reduced with a of The was of mitochondria. The in was and as well as maximal were with of mitochondria were in of respiration and were to the respiration was respiration ATP was to maximal respiration was addition of and were using the Mitochondria were with or for to The cytochrome were the of reduced mitochondria with a were with mitochondrial B. Neupert W. PubMed Scopus Google and on a with and a using were with and of the morphology were of the of were on in a of and in to for and were with was for in and J. 21: PubMed Scopus Google for on in and with with were with and on and a of and and The but the of Su e for of of Su to a on the and oligomerization of F1F0-ATP synthase we the role of the transmembrane and of two coiled-coil domains in Su We in which one or coiled-coil domains of Su e were Su and Su and a with a transmembrane Su were in the e In we subunit e (Su and the in the e, g, and This to the for Su in e the e as on and is used as a in The of was using of Su e The of subunit e were only a reduced for Su The we to the that of the the used is the presence of Su as well as of the coiled-coil (Su and Su to of Su g to the the of the Su or the of Su e not This the of the transmembrane of Su e in the of Su g G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar). we that lacking the coiled-coil domains are and the of Su of the F1F0-ATP on the as as the of ability of the F1F0-ATP synthase to form supracomplexes depends on the presence of the dimer-specific subunits Su e and Su g (5Arnold I. Pfeiffer K. Neupert W. Stuart R.A. Schagger H. EMBO J. 1998; 17: 7170-7178Crossref PubMed Scopus (371) Google and on the in the transmembrane of Su e G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar). We that the two coiled-coil domains in Su e to the of higher oligomeric of the F1F0-ATP synthase. we mitochondria in of and complexes The F1F0-ATP synthase complexes were to with mitochondria e, g, and Su dimeric or oligomeric forms of the F1F0-ATP synthase complexes In mitochondria Su and Su a loss of dimeric or oligomeric forms was that with the of coiled-coil domains of Su e We that the coiled-coil domains of Su e to the of dimeric or oligomeric forms of the F1F0-ATP synthase the major for of this is the within the transmembrane segment of Su of Su g of the F1F0-ATP in the of Su of complexes is correlated with and we Su g is in the mutants supracomplexes. we e Su Su and Su with to and of Su g The of was in Su in Su and in Su cells. The of subunit of the F1F0-ATP was not affected in this that the of the monomeric F1F0-ATP synthase is not altered Su e is not We propose that in mutants that show F1F0-ATP synthase supracomplexes, the of dimeric and oligomeric forms of the F1F0-ATP synthase is altered and the dimer-specific subunit Su g is to mitochondrial In subunits of the monomeric F1F0-ATP synthase not to of the F1F0-ATP but to the role of subunit e in and oligomerization of F1F0-ATP synthase we oligomerization the of cells. a we the and the membrane potential across the inner membrane in of that or show destabilization of the of F1F0-ATP synthase. We the in as well as the in the of The as of the of of substrates into the is a of the of this The in the and the Su in to the Su was decreased on the was not altered not The mutants lacking one or coiled-coil domains reduced on as with but with e In the reduction in was the the were Su e This reduction in was not We that mutants that and of the F1F0-ATP synthase show a but not a of to F1F0-ATP of a reduced to in oxidative phosphorylation, we the membrane potential in mitochondria determining the of of Biochim. Biophys. Acta. PubMed Scopus Google Scholar, Biophys. J. Full Text Full Text PDF PubMed Scopus Google Scholar). addition of mitochondria and the was mitochondria in a membrane This to of the and to a in the which is to the membrane potential across the inner membrane Biochim. Biophys. Acta. PubMed Scopus Google Scholar, Biophys. J. Full Text Full Text PDF PubMed Scopus Google Scholar). addition of cytochrome c was and the membrane potential was The degree of in the is correlated with the membrane potential of the membrane potential was addition of in not in the of the F1F0-ATP synthase a reduced membrane potential only a e) and (Su that of the and In the of two of mitochondria Su and Su we on a reduction of to and that of the and the was not as as Su e was which a reduction to and a we used a lacking the dimer-specific subunit that is not for of the F1F0-ATP synthase in this reduction in membrane potential was The the coiled-coil domains were the was the reduction of the membrane of and bioenergetic of lacking Su e or Su potential of of with potential of of with not of respiration respiration of of ATP of in c of respiration of not in a we with one the membrane potential for of mitochondria. The reduction in membrane potential for in oligomerization of the F1F0-ATP synthase was for e was reduced to of the Su and Su the membrane potential as was reduced to and with the the to which the of were decreased were using of and oligomerization of F1F0-ATP synthase complexes of membrane potential. the reduction in membrane potential for to the was of the as well as of the used we that the degree of destabilization of this well with the degree of reduction in membrane potential. of and in of F1F0-ATP reduction in membrane potential was for such as e, g, and Su have shown reduction in bioenergetic such as the respiration rate, the or the (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 2Arselin G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. 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PubMed Scopus Google Scholar). we the mutants lacking Su e show altered mitochondrial morphology. was in and morphology was in a tubular or in with mitochondria. mutants were that in the ATP and the membrane potential were to a tubular of mitochondria We to mitochondrial morphology using the which is mitochondria in a In the e and g but not in the only and was of mitochondrial morphology this and to are that mutants have a membrane potential not only in mitochondria but in in the of Su Su and e and g were to have altered cristae morphology as (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 2Arselin G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar). We altered ultrastructure of the inner membrane is correlated with a reduction in membrane potential. The mutants e, g, Su Su and Su were on with and the ultrastructure was In the e, g, Su the of the mitochondrial inner membrane were as In in the Su and Su mitochondria in cristae morphology with Su was we mitochondria with this was a minor of we this to a of the in a cells. we that of of Su e are for of cristae in This that altered cristae morphology for the reduction in membrane potential in mitochondria. the only affected in cristae morphology in addition of that ultrastructure of mitochondria is for of mitochondrial of the F1F0-ATP or of for the reduction in membrane potential and is of oxidative phosphorylation. this in we the enzymatic activities of cytochrome c and F1F0-ATP synthase. with (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, 5Arnold I. Pfeiffer K. Neupert W. Stuart R.A. Schagger H. EMBO J. 1998; 17: 7170-7178Crossref PubMed Scopus (371) Google the of the F1F0-ATP synthase was not reduced in the e with the the coiled-coil we not a in was in two as respiration of mitochondria and of cytochrome c with mitochondria. In of the in was in the Su and Su mutants We that is not affected the oligomeric of the F1F0-ATP synthase. the e a reduction of this was which we to loss of we of and of for mutants of c a reduction in the e and a in Su and Su were mutants lacking coiled-coil domains in Su e reduction in F1F0-ATP synthase or reduction of cytochrome c and of the of the complexes of the we respiration in mitochondria using of and as The maximal of was in the presence of the the or its maximal and is the F1F0-ATP synthase In to the e that of maximal the coiled-coil mutants of Su e (Su and Su in the maximal respiration The respiration in the Su e to the loss of mitochondrial were the of the is not reduced in the Su e coiled-coil mutants to for the reduction of the membrane potential in of oxidative phosphorylation. this we is to a membrane potential in We the maximal membrane potential the of the F1F0-ATP synthase ATP of the mitochondrial The membrane potential is We for of the mutants with the This that mutants are of membrane potential the of proton across the inner mitochondrial membrane in mutants lacking Su e or Su This is that the of respiration to respiration is not reduced This is used as a for the of coupling respiration and ATP of that coupling capacity of oxidative is affected in of the mutants lacking Su e or Su The fundamental role of the F1F0-ATP synthase in the of of the ATP has and in is the role of this in determining the ultrastructure of mitochondria. of of and of the F1F0-ATP synthase was to to altered cristae morphology (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 2Arselin G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, 4Giraud M.F. Paumard P. Soubannier V. Vaillier J. Arselin G. Salin B. Schaeffer J. Brethes D. di Rago J.P. Velours J. Biochim. Biophys. 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This reduction well with the of destabilization of the F1F0-ATP synthase This is the in in of such mutants the of membrane is We that destabilization of the F1F0-ATP synthase to a reduced capacity of the inner mitochondrial membrane to a membrane potential. mutants of Su e that of the two coiled-coil domains (Su and Su to the mutants of Su e or Su g in two not show loss of mitochondrial DNA, and were to form cristae coiled-coil domains to the of dimeric and oligomeric F1F0-ATP synthase complexes as This is with that the of subunit Su e to a destabilization of dimeric F1F0-ATP synthase complexes and only to a minor loss of mitochondrial V. Stuart R.A. PubMed Scopus Google Scholar). Here we show that the Su and Su have a reduced membrane potential. A loss of and of the F1F0-ATP synthase is to to loss of membrane potential in the on cristae morphology or is loss of is only in that show in the ultrastructure of cristae the that the membrane potential the ultrastructure of mitochondria a role in the of to cells. in the membrane potential was but not the of the is reduced activities of the are not to for the in or membrane potential. we that minor in activities of the in COX, to We this as the maximal respiration the are affected in on the membrane potential is as of the is for was that has to reduced to as as to the membrane potential H. D. P. J. H. J. J. Biochem. J. PubMed Google Scholar). was that the of oxidative in to of a on a A. Mueller D.M. PubMed Scopus Google Scholar). This of was in a number of in in mitochondria but in J.P. Biochim. Biophys. Acta. PubMed Scopus Google Scholar, G. G. A. PubMed Scopus Google Scholar, A. J. J. J. Google Scholar). a reduced cytochrome c was as a for the of a lacking Su g on a P. Eur. J. Biochem. PubMed Scopus Google Scholar). of the of have the of Su g P. Eur. J. Biochem. PubMed Scopus Google and (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google of were P. Eur. J. Biochem. PubMed Scopus Google that and reduced cytochrome c was not due to loss of mitochondrial but was due to cytochrome c In Velours and (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google to the This to this In of were in the g and e loss of mitochondrial with This the reduction of with In the mutants lacking one or coiled-coil domains of Su e not show a loss of mitochondrial a reduction in the Su e Su g to a major extent. In of this we and (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 2Arselin G. Giraud M.F. Dautant A. Vaillier J. Brethes D. Coulary-Salin B. Schaeffer J. Velours J. Eur. J. Biochem. 2003; 270: 1875-1884Crossref PubMed Scopus (112) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, 5Arnold I. Pfeiffer K. Neupert W. Stuart R.A. Schagger H. EMBO J. 1998; 17: 7170-7178Crossref PubMed Scopus (371) Google not for reduced respiration in mutants of Su g and Su e that not loss of that bioenergetic such as the respiration and the are not altered in mutants that dimeric and oligomeric F1F0-ATP synthase (1Paumard P. Vaillier J. Coulary B. Schaeffer J. Soubannier V. Mueller D.M. Brethes D. di Rago J.P. Velours J. EMBO J. 2002; 21: 221-230Crossref PubMed Scopus (617) Google Scholar, 3Soubannier V. Vaillier J. Paumard P. Coulary B. Schaeffer J. Velours J. J. Biol. Chem. 2002; 277: 10739-10745Abstract Full Text Full Text PDF PubMed Scopus (70) Google Scholar, P. Eur. J. Biochem. PubMed Scopus Google Scholar). In mutants was to a membrane potential addition of ATP to mitochondria. the of mutants were that of This of the inner is for a of enzymatic activities of the or of oxidative destabilization of F1F0-ATP synthase supracomplexes. a reduction in the membrane potential is This is a of a role of oligomeric in bioenergetic of mitochondria. the of a higher of complexes in A role of higher of complexes of the was and to the H. Pfeiffer K. EMBO J. PubMed Scopus Google Scholar, H. Biochim. Biophys. Acta. 2002; 1555: PubMed Scopus Google Scholar). We the that of F1F0-ATP synthase supracomplexes to in or of the inner mitochondrial in membrane is the of of the dimer-specific subunit g destabilization of F1F0-ATP synthase supracomplexes. This in the of microdomains within the inner mitochondrial In the of the the and the F1F0-ATP synthase to each are which with of This in to a reduced the or to a of a of the membrane potential In such a proton the or a of the membrane potential In this the of the F1F0-ATP synthase the the and in a membrane potential. We and for We and for and Velours for the Su with
Bornhövd et al. (Wed,) studied this question.