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Volumn 1767, Issue 7, 2007, Pages 998-1005

Essential arginine in subunit a and aspartate in subunit c of FoF1 ATP synthase. Effect of repositioning within Helix 4 of subunit a and Helix 2 of subunit c

Author keywords

ATP; FoF1 (EC 3.6.3.14); Proton; Synthesis; Translocation

Indexed keywords

ARGININE; ASPARTIC ACID; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 34447260787     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2007.05.007     Document Type: Article
Times cited : (18)

References (67)
  • 1
    • 0013942130 scopus 로고
    • Chemiosmotic coupling in oxidative and photosynthetic phosphorylation
    • Mitchell P. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Physiol. Rev. 41 (1966) 445-502
    • (1966) Physiol. Rev. , vol.41 , pp. 445-502
    • Mitchell, P.1
  • 2
    • 0031016071 scopus 로고    scopus 로고
    • Primary sodium ion translocating enzymes
    • Dimroth P. Primary sodium ion translocating enzymes. Biochim. Biophys. Acta 1318 (1997) 11-51
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 11-51
    • Dimroth, P.1
  • 3
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - a splendid molecular machine
    • Boyer P.D. The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66 (1997) 717-749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 8
    • 0035910414 scopus 로고    scopus 로고
    • The rotary machine in the cell, ATP synthase
    • Noji H., and Yoshida M. The rotary machine in the cell, ATP synthase. J. Biol. Chem. 276 (2001) 1665-1668
    • (2001) J. Biol. Chem. , vol.276 , pp. 1665-1668
    • Noji, H.1    Yoshida, M.2
  • 9
    • 0037064219 scopus 로고    scopus 로고
    • o rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ
    • o rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ. Biochim. Biophys. Acta 1565 (2002) 232-245
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 232-245
    • Fillingame, R.H.1    Dmitriev, O.Y.2
  • 12
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase.
    • Rastogi V.K., and Girvin M.E. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402 (1999) 263-268
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 14
    • 0033971704 scopus 로고    scopus 로고
    • Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase
    • Capaldi R.A., Schulenberg B., Murray J., and Aggeler R. Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase. J. Exp. Biol. 203 Pt. 1 (2000) 29-33
    • (2000) J. Exp. Biol. , vol.203 , Issue.PART 1 , pp. 29-33
    • Capaldi, R.A.1    Schulenberg, B.2    Murray, J.3    Aggeler, R.4
  • 15
    • 0034738113 scopus 로고    scopus 로고
    • o motor of the ATP synthase
    • o motor of the ATP synthase. Biochim. Biophys. Acta 1458 (2000) 374-386
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 374-386
    • Dimroth, P.1
  • 16
    • 0037131230 scopus 로고    scopus 로고
    • A research journey with ATP synthase
    • Boyer P.D. A research journey with ATP synthase. J. Biol. Chem. 277 (2002) 39045-39061
    • (2002) J. Biol. Chem. , vol.277 , pp. 39045-39061
    • Boyer, P.D.1
  • 17
    • 0037457911 scopus 로고    scopus 로고
    • Helix packing in subunit a of the Escherichia coli ATP synthase as determined by chemical labeling and proteolysis of the cysteine-substituted protein
    • Zhang D., and Vik S.B. Helix packing in subunit a of the Escherichia coli ATP synthase as determined by chemical labeling and proteolysis of the cysteine-substituted protein. Biochemistry 42 (2003) 331-337
    • (2003) Biochemistry , vol.42 , pp. 331-337
    • Zhang, D.1    Vik, S.B.2
  • 18
    • 0347985776 scopus 로고    scopus 로고
    • Subunit a of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent
    • Dmitriev O.Y., Altendorf K., and Fillingame R.H. Subunit a of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent. FEBS Lett. 556 (2004) 35-38
    • (2004) FEBS Lett. , vol.556 , pp. 35-38
    • Dmitriev, O.Y.1    Altendorf, K.2    Fillingame, R.H.3
  • 19
    • 0024371966 scopus 로고
    • A perspective of the binding change mechanism for ATP synthesis
    • Boyer P.D. A perspective of the binding change mechanism for ATP synthesis. FASEB J. 3 (1989) 2164-2178
    • (1989) FASEB J. , vol.3 , pp. 2164-2178
    • Boyer, P.D.1
  • 20
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F-ATPase
    • Noji H., Yasuda R., Yoshida M., and Kinosita K. Direct observation of the rotation of F-ATPase. Nature 386 (1997) 299-302
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 25
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: an electrochemical transducer with rotatory mechanics
    • Junge W., Lill H., and Engelbrecht S. ATP synthase: an electrochemical transducer with rotatory mechanics. Trends Biochem. Sci. 22 (1997) 420-423
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 26
    • 0027970177 scopus 로고
    • A mechanism of proton translocation by F1FO ATP synthases suggested by double mutants of the a subunit
    • Vik S.B., and Antonio B.J. A mechanism of proton translocation by F1FO ATP synthases suggested by double mutants of the a subunit. J. Biol. Chem. 269 (1994) 30364-30369
    • (1994) J. Biol. Chem. , vol.269 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 27
    • 0033609010 scopus 로고    scopus 로고
    • ATP synthase and other motor proteins
    • Junge W. ATP synthase and other motor proteins. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 4735-4737
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4735-4737
    • Junge, W.1
  • 28
    • 0018905628 scopus 로고
    • +-conduction contains a glycine instead of the carbodiimide-reactive aspartyl residue
    • +-conduction contains a glycine instead of the carbodiimide-reactive aspartyl residue. FEBS Lett. 109 (1980) 107-111
    • (1980) FEBS Lett. , vol.109 , pp. 107-111
    • Hoppe, J.1    Schairer, H.U.2    Sebald, W.3
  • 29
    • 0019926213 scopus 로고
    • An Asp-Asn substitution in the proteolipid subunit of the ATP-synthase from Escherichia coli leads to a non-functional proton channel
    • Hoppe J., Schairer H.U., Friedl P., and Sebald W. An Asp-Asn substitution in the proteolipid subunit of the ATP-synthase from Escherichia coli leads to a non-functional proton channel. FEBS Lett. 145 (1982) 21-29
    • (1982) FEBS Lett. , vol.145 , pp. 21-29
    • Hoppe, J.1    Schairer, H.U.2    Friedl, P.3    Sebald, W.4
  • 31
    • 0027483741 scopus 로고
    • 1H NMR resonance assignments and NOE analysis
    • 1H NMR resonance assignments and NOE analysis. Biochemistry 32 (1993) 12167-12177
    • (1993) Biochemistry , vol.32 , pp. 12167-12177
    • Girvin, M.E.1    Fillingame, R.H.2
  • 32
    • 0030863908 scopus 로고    scopus 로고
    • ATP synthase: a tentative structural model
    • Engelbrecht S., and Junge W. ATP synthase: a tentative structural model. FEBS Lett. 414 (1997) 485-491
    • (1997) FEBS Lett. , vol.414 , pp. 485-491
    • Engelbrecht, S.1    Junge, W.2
  • 33
    • 0035942281 scopus 로고    scopus 로고
    • The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
    • Jiang W., Hermolin J., and Fillingame R.H. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 4966-4971
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4966-4971
    • Jiang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 34
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D., Leslie A.G., and Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science 286 (1999) 1700-1705
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 37
    • 17844367330 scopus 로고    scopus 로고
    • Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus
    • Meier T., Polzer P., Diederichs K., Welte W., and Dimroth P. Structure of the rotor ring of F-Type Na+-ATPase from Ilyobacter tartaricus. Science 308 (2005) 659-662
    • (2005) Science , vol.308 , pp. 659-662
    • Meier, T.1    Polzer, P.2    Diederichs, K.3    Welte, W.4    Dimroth, P.5
  • 40
    • 0024977998 scopus 로고
    • 0ATPase of Escherichia coli. Mutagenic analysis of the a subunit
    • 0ATPase of Escherichia coli. Mutagenic analysis of the a subunit. J. Biol. Chem. 264 (1989) 3292-3300
    • (1989) J. Biol. Chem. , vol.264 , pp. 3292-3300
    • Cain, B.D.1    Simoni, R.D.2
  • 41
  • 42
    • 0032568845 scopus 로고    scopus 로고
    • o ATP synthase as determined by labeling of unique cysteine residues
    • o ATP synthase as determined by labeling of unique cysteine residues. J. Biol. Chem. 273 (1998) 16235-16240
    • (1998) J. Biol. Chem. , vol.273 , pp. 16235-16240
    • Long, J.C.1    Wang, S.2    Vik, S.B.3
  • 45
    • 0032499690 scopus 로고    scopus 로고
    • o ATP synthase of Escherichia coli defined by disulfide cross-linking
    • o ATP synthase of Escherichia coli defined by disulfide cross-linking. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6607-6612
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6607-6612
    • Jiang, W.P.1    Fillingame, R.H.2
  • 46
    • 0028880405 scopus 로고
    • The essential arginine residue at position 210 in the a subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity
    • Hatch L.P., Cox G.B., and Howitt S.M. The essential arginine residue at position 210 in the a subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity. J. Biol. Chem. 270 (1995) 29407-29412
    • (1995) J. Biol. Chem. , vol.270 , pp. 29407-29412
    • Hatch, L.P.1    Cox, G.B.2    Howitt, S.M.3
  • 48
    • 0028067602 scopus 로고
    • o ATP synthase. Effect of position 61 substitutions in helix-2 on function of Asp24 in helix-1
    • o ATP synthase. Effect of position 61 substitutions in helix-2 on function of Asp24 in helix-1. J. Biol. Chem. 269 (1994) 5473-5479
    • (1994) J. Biol. Chem. , vol.269 , pp. 5473-5479
    • Zhang, Y.1    Fillingame, R.H.2
  • 50
    • 0037458716 scopus 로고    scopus 로고
    • Aqueous access channels in subunit a of rotary ATP synthase
    • Angevine C.M., and Fillingame R.H. Aqueous access channels in subunit a of rotary ATP synthase. J. Biol. Chem. 278 (2003) 6066-6074
    • (2003) J. Biol. Chem. , vol.278 , pp. 6066-6074
    • Angevine, C.M.1    Fillingame, R.H.2
  • 52
    • 0021736478 scopus 로고
    • In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
    • Klionsky D.J., Brusilow W.S.A., and Simoni R.D. In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J. Bacteriol. 160 (1984) 1055-1060
    • (1984) J. Bacteriol. , vol.160 , pp. 1055-1060
    • Klionsky, D.J.1    Brusilow, W.S.A.2    Simoni, R.D.3
  • 53
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner M.P., Costa G.L., Schoettlin W., Cline J., Mathur E., and Bauer J.C. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151 (1994) 119-123
    • (1994) Gene , vol.151 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6
  • 54
    • 0037188741 scopus 로고    scopus 로고
    • 1-ATPase: The C-terminal end of subunit γ is not required for ATP hydrolysis-driven rotation
    • 1-ATPase: The C-terminal end of subunit γ is not required for ATP hydrolysis-driven rotation. J. Biol. Chem. 277 (2002) 23308-23313
    • (2002) J. Biol. Chem. , vol.277 , pp. 23308-23313
    • Müller, M.1    Pänke, O.2    Junge, W.3    Engelbrecht, S.4
  • 56
    • 0017390556 scopus 로고
    • A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250
    • Sedmak J.J., and Grossberg S.E. A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Anal. Biochem. 79 (1977) 544-552
    • (1977) Anal. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 58
    • 0015100514 scopus 로고
    • Oxidative phosphorylation in Escherichia coli K12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase
    • Butlin J.D., Cox G.B., and Gibson F. Oxidative phosphorylation in Escherichia coli K12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase. Biochem. J. 124 (1971) 75-81
    • (1971) Biochem. J. , vol.124 , pp. 75-81
    • Butlin, J.D.1    Cox, G.B.2    Gibson, F.3
  • 59
    • 0018337520 scopus 로고
    • Membrane adenosine triphosphatases of prokaryotic cells
    • Downie J.A., Gibson F., and Cox G.B. Membrane adenosine triphosphatases of prokaryotic cells. Annu. Rev. Biochem. 48 (1979) 103-131
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 103-131
    • Downie, J.A.1    Gibson, F.2    Cox, G.B.3
  • 61
    • 0031791392 scopus 로고    scopus 로고
    • atp Mutants of Escherichia coli fail to grow on succinate due to a transport deficiency
    • Boogerd F.C., Boe L., Michelsen O., and Jensen P.R. atp Mutants of Escherichia coli fail to grow on succinate due to a transport deficiency. J. Bacteriol. 180 (1998) 5855-5859
    • (1998) J. Bacteriol. , vol.180 , pp. 5855-5859
    • Boogerd, F.C.1    Boe, L.2    Michelsen, O.3    Jensen, P.R.4
  • 62
    • 0025323480 scopus 로고
    • 1-ATPase by lauryldimethylamine oxide and ethylene-glycol - relationship of ATPase activity to the interaction of the ε-subunit and β-subunit
    • 1-ATPase by lauryldimethylamine oxide and ethylene-glycol - relationship of ATPase activity to the interaction of the ε-subunit and β-subunit. Biochemistry 29 (1990) 4335-4340
    • (1990) Biochemistry , vol.29 , pp. 4335-4340
    • Dunn, S.D.1    Tozer, R.G.2    Zadorozny, V.D.3
  • 63
    • 0035110954 scopus 로고    scopus 로고
    • o ATPase subunit c and cytoplasmic pH regulation
    • o ATPase subunit c and cytoplasmic pH regulation. J. Bacteriol. 183 (2001) 1524-1530
    • (2001) J. Bacteriol. , vol.183 , pp. 1524-1530
    • Jones, P.C.1
  • 64
    • 0345255628 scopus 로고    scopus 로고
    • Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane
    • Angevine C.M., Herold K.A., and Fillingame R.H. Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13179-13183
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13179-13183
    • Angevine, C.M.1    Herold, K.A.2    Fillingame, R.H.3
  • 65
    • 33845989502 scopus 로고    scopus 로고
    • Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle
    • Schwem B.E., and Fillingame R.H. Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle. J. Biol. Chem. 281 (2006) 37861-37867
    • (2006) J. Biol. Chem. , vol.281 , pp. 37861-37867
    • Schwem, B.E.1    Fillingame, R.H.2
  • 66
    • 34247877574 scopus 로고    scopus 로고
    • Aqueous access pathways in ATP synthase subunit a: reactivity of cysteine substituted into transmembrane helices 1, 3 and 5
    • Angevine C.M., Herold K.A., Vincent O.D., and Fillingame R.H. Aqueous access pathways in ATP synthase subunit a: reactivity of cysteine substituted into transmembrane helices 1, 3 and 5. J. Biol. Chem. 282 (2007) 9001-9007
    • (2007) J. Biol. Chem. , vol.282 , pp. 9001-9007
    • Angevine, C.M.1    Herold, K.A.2    Vincent, O.D.3    Fillingame, R.H.4


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