The multicopy subunit c of the H+-transporting F1F0 ATP synthase of Escherichia coli is thought to fold across the membrane as a hairpin of two hydrophobic α-helices. The conserved Asp61, centered in the second transmembrane helix, is essential for H+ transport. In this study, we have made sequential Cys substitutions across both transmembrane helices and used disulfide cross-link formation to determine the oligomeric arrangement of the c subunits. Cross-link formation between single Cys substitutions in helix 1 provided initial limitations on how the subunits could be arranged. Double Cys substitutions at positions 14/16, 16/18, and 21/23 in helix 1 and 70/72 in helix 2 led to the formation of cross-linked multimers upon oxidation. Double Cys substitutions in helix 1 and helix 2, at residues 14/72, 21/65, and 20/66, respectively, also formed cross-linked multimers. These results indicate that at least 10 and probably 12 subunits c interact in a front-to-back fashion to form a ring-like arrangement in F0. Helix 1 packs at the interior and helix 2 at the periphery of the ring. The model indicates that the Asp61carboxylate is centered between the helical faces of adjacent subunit c at the center of a four-helix bundle. The multicopy subunit c of the H+-transporting F1F0 ATP synthase of Escherichia coli is thought to fold across the membrane as a hairpin of two hydrophobic α-helices. The conserved Asp61, centered in the second transmembrane helix, is essential for H+ transport. In this study, we have made sequential Cys substitutions across both transmembrane helices and used disulfide cross-link formation to determine the oligomeric arrangement of the c subunits. Cross-link formation between single Cys substitutions in helix 1 provided initial limitations on how the subunits could be arranged. Double Cys substitutions at positions 14/16, 16/18, and 21/23 in helix 1 and 70/72 in helix 2 led to the formation of cross-linked multimers upon oxidation. Double Cys substitutions in helix 1 and helix 2, at residues 14/72, 21/65, and 20/66, respectively, also formed cross-linked multimers. These results indicate that at least 10 and probably 12 subunits c interact in a front-to-back fashion to form a ring-like arrangement in F0. Helix 1 packs at the interior and helix 2 at the periphery of the ring. The model indicates that the Asp61carboxylate is centered between the helical faces of adjacent subunit c at the center of a four-helix bundle. F1F0 ATP synthases catalyze the formation of ATP utilizing the energy of a transmembrane H+electrochemical gradient, generated by electron transport complexes and other ion pumping systems. Closely related ATP synthases are found in the plasma membrane of eubacteria, the inner membrane of mitochondria, and the thylakoid membrane of chloroplasts. The enzyme is a multisubunit complex with distinct extramembranous and transmembrane domains, termed F1 and F0, respectively. Ion movement through F0 is coupled to ATP synthesis/hydrolysis at sites in F1 (1Senior A.E. Physiol. Rev. 1988; 68: 177-231Crossref PubMed Scopus (454) Google Scholar, 2Fillingame R.H. Kurlwich T.A. The Bacteria. 12. Academic Press, Inc., New York1990: 345-391Google Scholar). The simplest F1 sectors, as found in Escherichia coli, consist of five subunits in an α3β3γδε stoichiometry. Homologous subunits are found in mitochondria and chloroplasts. A high resolution structure of a substantial part of bovine F1 shows the three α- and three β-subunits to alternate around a central core through which subunit γ extends and protrudes (3Abrahams J.P. Leslie A.G.W. Lutter R. Walker J.E. Nature. 1994; 370: 621-628Crossref PubMed Scopus (2734) Google Scholar). The structure fits well with the binding change mechanism proposed by Boyer and co-workers (4Boyer P.D. Annu. Rev. Biochem. 1997; 66: 717-749Crossref PubMed Scopus (1565) Google Scholar), where each of the three β-subunits alternates between the loose binding of ADP plus Pi, tight ADP plus Pibinding and ATP synthesis, and ATP release during catalytic turnover. Several recent studies now show that subunit γ rotates within the core of the hexagonally arranged α3β3complex to presumably drive the binding changes in each β-subunit (5Duncan T.M. Bulygin PubMed Scopus Google Scholar, Nature. PubMed Scopus Google Scholar, R. Nature. 1997; PubMed Scopus Google Scholar). subunit γ and to as a R. PubMed Scopus Google Scholar). The mechanism of H+ through F0 to γ subunit is coli F0 is the simplest found in of three subunits with a of 1 R.H. PubMed Google Scholar). studies that the a and subunits at the periphery of a complex of subunit c R. Biochem. PubMed Scopus Google Scholar). with a single transmembrane helix and is proposed to with subunit to a that and the F1 catalytic to F0 PubMed Scopus Google Scholar, R. 1997; PubMed Scopus Google Scholar). a is thought to fold through the membrane with five transmembrane helices and a in the H+ transport R.H. Kurlwich T.A. The Bacteria. 12. Academic Press, Inc., New York1990: 345-391Google Scholar, PubMed Scopus Google Scholar). and studies indicate that subunit c in the membrane as a hairpin of two hydrophobic by a on the F1 binding of the membrane R.H. Kurlwich T.A. The Bacteria. 12. Academic Press, Inc., New York1990: 345-391Google Scholar, R.H. Biochem. PubMed Scopus Google Scholar). A conserved in centered in the second transmembrane helix is essential for H+ transport R.H. Kurlwich T.A. The Bacteria. 12. Academic Press, Inc., New York1990: 345-391Google Scholar, R.H. 1997; PubMed Google Scholar). The for a of the in binding on the related enzyme of PubMed Scopus Google Scholar, 1997; PubMed Scopus Google and on a coli enzyme that R.H. PubMed Scopus Google Scholar). The of to binding changes in F1 to by an between the of subunit c with subunits and γ R.H. 1997; PubMed Google Scholar, R.H. PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). Several have proposed ATP in the F1 is coupled to through F0 of subunit c to the multicopy subunit a PubMed Scopus Google Scholar, 1994; PubMed Google Scholar, 1997; PubMed Scopus Google on the of F0 subunits is essential we are to how H+ transport is coupled to ATP In this study, Cys subunit c in to determine the arrangement of subunits by disulfide The the model of subunit c as by R.H. PubMed Scopus Google Scholar). and R. in and R. in A arrangement of 12 subunits c with helix 1 in the center and helix 2 at the periphery is The subunits interact with the of subunit the of the subunit with the centered within a four-helix between adjacent subunits The model and limitations how H+ be coupled to the and of ATP within and of subunit c generated to determine by disulfide cross-link formation the arrangement of subunits in F0. The results that subunit c is in a structure with two transmembrane Double Cys substitutions that formed cross-linked multimers on formation as single Cys substitutions the for a arrangement of as in The Cys substitutions the and in helix 1 and the in helix formed by between helix 1 and helix 2 the of helices with to each other and for a The Cys substitutions that this are and The well with the proposed model of subunit c R.H. 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Scopus Google and for the of the complex Nature. Scopus Google Scholar). The arrangement proposed well with recent where F0 as a structure a central the PubMed Scopus Google Scholar, PubMed Scopus Google of the that coli and residues in other and release in the transport coupled to ATP R.H. 1997; PubMed Google 1997; PubMed Scopus Google Scholar). The essential in helix 2 of the coli be to in helix 1 with of R.H. PubMed Scopus Google Scholar). The model of subunit c shows of helix 1 in to of helix 2, the to of the is in the In the model the are within the center of a four-helix formed by the and of two adjacent The of the essential to be in an The model also be used to the of essential residues in subunit c of the F1F0 and a binding of the 1997; PubMed Scopus Google have that residues and are essential for binding in residues at positions to residues and in The conserved residues in and have at positions within the transmembrane helices of subunit c in the 1997; PubMed Scopus Google Scholar). In both is found at a to in In the model each of the center of the four-helix formed by subunits. The model also substitutions in coli subunit c R.H. PubMed Scopus Google the as a the F1F0 ATP synthases with a of The as to and Annu. Rev. 1997; PubMed Scopus Google Scholar, 1997; Google Scholar). The subunit c of is the of in the and to have by of a 1988; PubMed Scopus Google Scholar). transmembrane helices are 1 and and helices 2 and of this subunit c show with helices 1 and 2 of the subunit c of the F1F0 ATP respectively. 1 and of subunit c show a and of and to that in subunit A model proposed for this multicopy subunit on electron and PubMed Scopus Google Scholar, Biochem. PubMed Scopus Google Scholar, Biochem. PubMed Scopus Google Scholar). In the subunits each as a of to form a complex with a central The model in the the that helix 1 the of the Biochem. PubMed Scopus Google Scholar), upon Cys and is coli subunit c that the arrangement of the subunit c be that proposed with helices 1 and the inner and helices 2 and the The of the conserved in the second helix of the subunit c the of binding the H+ pumping to the of the complex PubMed Scopus Google Scholar). on the with the coli subunit c R.H. PubMed Scopus Google Scholar), have made to a enzyme of the essential helix to helix have The model that an between helix and helix 1 is to with the binding at the center of a four-helix and helix to helix the model that in the of Biochem. PubMed Scopus Google Scholar), the between helix and helix The to be by in a conserved and PubMed Scopus Google arrangement of subunit c and limitations on how movement be coupled to ATP The by of the within the core of the (5Duncan T.M. Bulygin PubMed Scopus Google Scholar, Nature. PubMed Scopus Google Scholar, R. Nature. 1997; PubMed Scopus Google Scholar). led to that the oligomeric of subunit c rotates a subunit a in the membrane (5Duncan T.M. Bulygin PubMed Scopus Google Scholar, 1994; PubMed Google Scholar, 1997; PubMed Scopus Google Scholar, Nature. PubMed Scopus Google Scholar). In the the is on the of the and upon is as the of the In the arrangement the ion be in the center of the four-helix to the a in be to an and of the four-helix with ion and that is that the subunit c rotates in the have that the membrane to the and subunits in R.H. 1997; PubMed Google Scholar, Biochem. PubMed Scopus Google Scholar). In a subunit γ and the subunit are to at the of subunit changes be the of ion to the of subunit and changes in the drive movement of the complex to in a The is within the membrane F1F0 ATP synthases catalyze the formation of ATP utilizing the energy of a transmembrane H+electrochemical gradient, generated by electron transport complexes and other ion pumping systems. Closely related ATP synthases are found in the plasma membrane of eubacteria, the inner membrane of mitochondria, and the thylakoid membrane of chloroplasts. The enzyme is a multisubunit complex with distinct extramembranous and transmembrane domains, termed F1 and F0, respectively. Ion movement through F0 is coupled to ATP synthesis/hydrolysis at sites in F1 (1Senior A.E. Physiol. Rev. 1988; 68: 177-231Crossref PubMed Scopus (454) Google Scholar, 2Fillingame R.H. Kurlwich T.A. The Bacteria. 12. Academic Press, Inc., New York1990: 345-391Google Scholar). The simplest F1 sectors, as found in Escherichia coli, consist of five subunits in an α3β3γδε stoichiometry. Homologous subunits are found in mitochondria and chloroplasts. A high resolution structure of a substantial part of bovine F1 shows the three α- and three β-subunits to alternate around a central core through which subunit γ extends and protrudes (3Abrahams J.P. Leslie A.G.W. Lutter R. Walker J.E. Nature. 1994; 370: 621-628Crossref PubMed Scopus (2734) Google Scholar). The structure fits well with the binding change mechanism proposed by Boyer and co-workers (4Boyer P.D. Annu. Rev. Biochem. 1997; 66: 717-749Crossref PubMed Scopus (1565) Google Scholar), where each of the three β-subunits alternates between the loose binding of ADP plus Pi, tight ADP plus Pibinding and ATP synthesis, and ATP release during catalytic turnover. Several recent studies now show that subunit γ rotates within the core of the hexagonally arranged α3β3complex to presumably drive the binding changes in each β-subunit (5Duncan T.M. Bulygin PubMed Scopus Google Scholar, Nature. PubMed Scopus Google Scholar, R. Nature. 1997; PubMed Scopus Google Scholar). subunit γ and to as a R. PubMed Scopus Google Scholar). The mechanism of H+ through F0 to γ subunit is The coli F0 is the simplest found in of three subunits with a of 1 R.H. PubMed Google Scholar). studies that the a and subunits at the periphery of a complex of subunit c R. Biochem. PubMed Scopus Google Scholar). with a single transmembrane helix and is proposed to with subunit to a that and the F1 catalytic to F0 PubMed Scopus Google Scholar, R. 1997; PubMed Scopus Google Scholar). a is thought to fold through the membrane with five transmembrane helices and a in the H+ transport R.H. Kurlwich T.A. The Bacteria. 12. Academic Press, Inc., New York1990: 345-391Google Scholar, PubMed Scopus Google Scholar). and studies indicate that subunit c in the membrane as a hairpin of two hydrophobic by a on the F1 binding of the membrane R.H. Kurlwich T.A. The Bacteria. 12. Academic Press, Inc., New York1990: 345-391Google Scholar, R.H. Biochem. PubMed Scopus Google Scholar). A conserved in centered in the second transmembrane helix is essential for H+ transport R.H. Kurlwich T.A. The Bacteria. 12. Academic Press, Inc., New York1990: 345-391Google Scholar, R.H. 1997; PubMed Google Scholar). The for a of the in binding on the related enzyme of PubMed Scopus Google Scholar, 1997; PubMed Scopus Google and on a coli enzyme that R.H. PubMed Scopus Google Scholar). The of to binding changes in F1 to by an between the of subunit c with subunits and γ R.H. 1997; PubMed Google Scholar, R.H. PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). Several have proposed ATP in the F1 is coupled to through F0 of subunit c to the multicopy subunit a PubMed Scopus Google Scholar, 1994; PubMed Google Scholar, 1997; PubMed Scopus Google Scholar). on the of F0 subunits is essential we are to how H+ transport is coupled to ATP In this study, Cys subunit c in to determine the arrangement of subunits by disulfide The the model of subunit c as by R.H. PubMed Scopus Google Scholar). and R. in and R. in A arrangement of 12 subunits c with helix 1 in the center and helix 2 at the periphery is The subunits interact with the of subunit the of the subunit with the centered within a four-helix between adjacent subunits The model and limitations how H+ be coupled to the and of ATP within and of subunit c generated to determine by disulfide cross-link formation the arrangement of subunits in F0. The results that subunit c is in a structure with two transmembrane Double Cys substitutions that formed cross-linked multimers on formation as single Cys substitutions the for a arrangement of as in The Cys substitutions the and in helix 1 and the in helix formed by between helix 1 and helix 2 the of helices with to each other and for a The Cys substitutions that this are and The well with the proposed model of subunit c R.H. PubMed Scopus Google In the model used as a for residues that to cross-link in the formation of cross-linked single Cys substitutions in helix 2 with the model in the of is centered around Cross-link formation in this that is to a of helix 2 to helix 1 in related to transport. also that Cys of which are at the between helices in the in of the at of the is in the of the of the change by a Cys on of the be to disulfide could for the cross-linked in the and have also studies in the of a that used to and F1F0 Biochem. PubMed Scopus Google Scholar). The of in high formation with with and also with in where in the of The structure of F0 be the structure in the high cross-linked that form in the single Cys substitutions of helix and on of an in the on the that the inner core of the in The of and in residues to of this the helix this we helix 1 as in helix 2 in the model In a this is The of the the central core are in with in the helix and indicates of to disulfide cross-link formation with of The of helix 2, the to the of the is also hydrophobic with in two faces are hydrophobic conserved PubMed Scopus Google Scholar), which is with both to the of the In other membrane the in show the Annu. Rev. Biochem. PubMed Scopus Google Scholar). and on the interior helical are by in to other residues in the which led to the that residues on of an that to the of the PubMed Scopus Google Scholar). In the of subunit c the of the in the central core is and that be and for the with are with the of the membrane T.A. R. Scopus Google and for the of the complex Nature. Scopus Google Scholar). The arrangement proposed well with recent where F0 as a structure a central the PubMed Scopus Google Scholar, PubMed Scopus Google of the that coli and residues in other and release in the transport coupled to ATP R.H. 1997; PubMed Google 1997; PubMed Scopus Google Scholar). The essential in helix 2 of the coli be to in helix 1 with of R.H. PubMed Scopus Google Scholar). The model of subunit c shows of helix 1 in to of helix 2, the to of the is in the In the model the are within the center of a four-helix formed by the and of two adjacent The of the essential to be in an The model also be used to the of essential residues in subunit c of the F1F0 and a binding of the 1997; PubMed Scopus Google have that residues and are essential for binding in residues at positions to residues and in The conserved residues in and have at positions within the transmembrane helices of subunit c in the 1997; PubMed Scopus Google Scholar). In both is found at a to in In the model each of the center of the four-helix formed by subunits. The model also substitutions in coli subunit c R.H. PubMed Scopus Google the as a the F1F0 ATP synthases with a of The as to and Annu. Rev. 1997; PubMed Scopus Google Scholar, 1997; Google Scholar). The subunit c of is the of in the and to have by of a 1988; PubMed Scopus Google Scholar). transmembrane helices are 1 and and helices 2 and of this subunit c show with helices 1 and 2 of the subunit c of the F1F0 ATP respectively. 1 and of subunit c show a and of and to that in subunit A model proposed for this multicopy subunit on electron and PubMed Scopus Google Scholar, Biochem. PubMed Scopus Google Scholar, Biochem. PubMed Scopus Google Scholar). In the subunits each as a of to form a complex with a central The model in the the that helix 1 the of the Biochem. PubMed Scopus Google Scholar), upon Cys and is coli subunit c that the arrangement of the subunit c be that proposed with helices 1 and the inner and helices 2 and the The of the conserved in the second helix of the subunit c the of binding the H+ pumping to the of the complex PubMed Scopus Google Scholar). on the with the coli subunit c R.H. PubMed Scopus Google Scholar), have made to a enzyme of the essential helix to helix have The model that an between helix and helix 1 is to with the binding at the center of a four-helix and helix to helix the model that in the of Biochem. PubMed Scopus Google Scholar), the between helix and helix The to be by in a conserved and PubMed Scopus Google arrangement of subunit c and limitations on how movement be coupled to ATP The by of the within the core of the (5Duncan T.M. Bulygin PubMed Scopus Google Scholar, Nature. PubMed Scopus Google Scholar, R. Nature. 1997; PubMed Scopus Google Scholar). led to that the oligomeric of subunit c rotates a subunit a in the membrane (5Duncan T.M. Bulygin PubMed Scopus Google Scholar, 1994; PubMed Google Scholar, 1997; PubMed Scopus Google Scholar, Nature. PubMed Scopus Google Scholar). In the the is on the of the and upon is as the of the In the arrangement the ion be in the center of the four-helix to the a in be to an and of the four-helix with ion and that is that the subunit c rotates in the have that the membrane to the and subunits in R.H. 1997; PubMed Google Scholar, Biochem. PubMed Scopus Google Scholar). In a subunit γ and the subunit are to at the of subunit changes be the of ion to the of subunit and changes in the drive movement of the complex to in a The is within the membrane and of subunit c generated to determine by disulfide cross-link formation the arrangement of subunits in F0. 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Scopus Google and for the of the complex Nature. Scopus Google Scholar). The arrangement proposed well with recent where F0 as a structure a central the PubMed Scopus Google Scholar, PubMed Scopus Google Scholar). A of the that coli and residues in other and release in the transport coupled to ATP R.H. 1997; PubMed Google 1997; PubMed Scopus Google Scholar). The essential in helix 2 of the coli be to in helix 1 with of R.H. PubMed Scopus Google Scholar). The model of subunit c shows of helix 1 in to of helix 2, the to of the is in the In the model the are within the center of a four-helix formed by the and of two adjacent The of the essential to be in an The model also be used to the of essential residues in subunit c of the F1F0 and a binding of the 1997; PubMed Scopus Google have that residues and are essential for binding in residues at positions to residues and in The conserved residues in and have at positions within the transmembrane helices of subunit c in the 1997; PubMed Scopus Google Scholar). In both is found at a to in In the model each of the center of the four-helix formed by subunits. The model also substitutions in coli subunit c R.H. PubMed Scopus Google the as a the The F1F0 ATP synthases with a of The as to and Annu. Rev. 1997; PubMed Scopus Google Scholar, 1997; Google Scholar). The subunit c of is the of in the and to have by of a 1988; PubMed Scopus Google Scholar). transmembrane helices are 1 and and helices 2 and of this subunit c show with helices 1 and 2 of the subunit c of the F1F0 ATP respectively. 1 and of subunit c show a and of and to that in subunit A model proposed for this multicopy subunit on electron and PubMed Scopus Google Scholar, Biochem. PubMed Scopus Google Scholar, Biochem. PubMed Scopus Google Scholar). In the subunits each as a of to form a complex with a central The model in the the that helix 1 the of the Biochem. PubMed Scopus Google Scholar), upon Cys and is coli subunit c that the arrangement of the subunit c be that proposed with helices 1 and the inner and helices 2 and the The of the conserved in the second helix of the subunit c the of binding the H+ pumping to the of the complex PubMed Scopus Google Scholar). on the with the coli subunit c R.H. PubMed Scopus Google Scholar), have made to a enzyme of the essential helix to helix have The model that an between helix and helix 1 is to with the binding at the center of a four-helix and helix to helix the model that in the of Biochem. PubMed Scopus Google Scholar), the between helix and helix The to be by in a conserved and PubMed Scopus Google Scholar). The arrangement of subunit c and limitations on how movement be coupled to ATP The by of the within the core of the (5Duncan T.M. Bulygin PubMed Scopus Google Scholar, Nature. PubMed Scopus Google Scholar, R. Nature. 1997; PubMed Scopus Google Scholar). led to that the oligomeric of subunit c rotates a subunit a in the membrane (5Duncan T.M. Bulygin PubMed Scopus Google Scholar, 1994; PubMed Google Scholar, 1997; PubMed Scopus Google Scholar, Nature. PubMed Scopus Google Scholar). In the the is on the of the and upon is as the of the In the arrangement the ion be in the center of the four-helix to the a in be to an and of the four-helix with ion and that is that the subunit c rotates in the have that the membrane to the and subunits in R.H. 1997; PubMed Google Scholar, Biochem. PubMed Scopus Google Scholar). In a subunit γ and the subunit are to at the of subunit changes be the of ion to the of subunit and changes in the drive movement of the complex to in a The is within the membrane
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