메뉴 건너뛰기




Volumn 288, Issue 34, 2013, Pages 24465-24479

Individual interactions of the b subunits within the stator of the escherichia coli ATP synthase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY BINDING; C-TERMINAL REGIONS; DISULFIDE BOND FORMATION; DISULFIDE CROSS-LINKING; NEAREST NEIGHBOR ANALYSIS; NON-CATALYTIC; PERIPHERAL STATOR; PROTON TRANSLOCATION;

EID: 84883140479     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.465633     Document Type: Article
Times cited : (19)

References (71)
  • 3
    • 48249108462 scopus 로고    scopus 로고
    • Unique rotor ATP synthase and its biological diversity
    • von Ballmoos, C., Cook, G. M., and Dimroth, P. (2008) Unique rotor ATP synthase and its biological diversity. Annu. Rev. Biophys. 37, 43-64
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 43-64
    • Von Ballmoos, C.1    Cook, G.M.2    Dimroth, P.3
  • 5
    • 79960112075 scopus 로고    scopus 로고
    • Structural divergence of the rotary at Pases
    • Muench, S. P., Trinick, J., and Harrison, M. A. (2011) Structural divergence of the rotary AT Pases. Q. Rev. Biophys. 44, 311-356
    • (2011) Q. Rev. Biophys. , vol.44 , pp. 311-356
    • Muench, S.P.1    Trinick, J.2    Harrison, M.A.3
  • 6
    • 57149127160 scopus 로고    scopus 로고
    • A different conformation of EGC stator subcomplex in solution and in the assembled yeast V-AT Pase: Possible implications for regulatory disassembly
    • Diepholz, M., Venzke, D., Prinz, S., Batisse, C., Flörchinger, B., Rössle, M., Svergun, D. I., Böttcher, B., and Féthière, J. (2008) A different conformation of EGC stator subcomplex in solution and in the assembled yeast V-AT Pase: Possible implications for regulatory disassembly. Structure 16, 1789-1798
    • (2008) Structure , vol.16 , pp. 1789-1798
    • Diepholz, M.1    Venzke, D.2    Prinz, S.3    Batisse, C.4    Flörchinger, B.5    Rössle, M.6    Svergun, D.I.7    Böttcher, B.8    Féthière, J.9
  • 8
    • 66449094132 scopus 로고    scopus 로고
    • O-ATP synthase from Thermoplasma acidophilum
    • O-ATP synthase from Thermoplasma acidophilum. J. Biol. Chem. 284, 12031-12040
    • (2009) J. Biol. Chem. , vol.284 , pp. 12031-12040
    • Kish-Trier, E.1    Wilkens, S.2
  • 12
    • 0027156160 scopus 로고
    • The nuclear-encoded polypeptide Cfo-II from spinach is a real, ninth subunit of chloroplast ATP synthase
    • Herrmann, R. G., Steppuhn, J., Herrmann, G. S., and Nelson, N. (1993) The nuclear-encoded polypeptide Cfo-II from spinach is a real, ninth subunit of chloroplast ATP synthase. FEBS Lett. 326, 192-198
    • (1993) FEBS Lett. , vol.326 , pp. 192-198
    • Herrmann, R.G.1    Steppuhn, J.2    Herrmann, G.S.3    Nelson, N.4
  • 13
    • 0035830452 scopus 로고    scopus 로고
    • Specific heterodimer formation by the cytoplasmic domains of the b and b′ subunits of cyanobacterial ATP synthase
    • Dunn, S. D., Kellner, E., and Lill, H. (2001) Specific heterodimer formation by the cytoplasmic domains of the b and b′ subunits of cyanobacterial ATP synthase. Biochemistry 40, 187-192
    • (2001) Biochemistry , vol.40 , pp. 187-192
    • Dunn, S.D.1    Kellner, E.2    Lill, H.3
  • 17
  • 18
    • 76049093135 scopus 로고    scopus 로고
    • The structure of the membrane extrinsic region of bovine ATP synthase
    • Rees, D. M., Leslie, A. G., and Walker, J. E. (2009) The structure of the membrane extrinsic region of bovine ATP synthase. Proc. Natl. Acad. Sci. U.S.A. 106, 21597-21601
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 21597-21601
    • Rees, D.M.1    Leslie, A.G.2    Walker, J.E.3
  • 21
    • 2642707545 scopus 로고    scopus 로고
    • ATP synthase's second stalk comes into focus
    • Wilkens, S., and Capaldi, R. A. (1998) ATP synthase's second stalk comes into focus. Nature 393, 29
    • (1998) Nature , vol.393 , pp. 29
    • Wilkens, S.1    Capaldi, R.A.2
  • 22
    • 33748986212 scopus 로고    scopus 로고
    • ATP synthase. Subunit-subunit interaction in the stator stalk
    • Weber, J. (2006) ATP synthase. Subunit-subunit interaction in the stator stalk. Biochim. Biophys. Acta 1757, 1162-1170
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1162-1170
    • Weber, J.1
  • 29
    • 0034625459 scopus 로고    scopus 로고
    • Site-directed cross-linking of b to the α, β, and a subunits of the Escherichia coli ATP synthase
    • McLachlin, D. T., Coveny, A. M., Clark, S. M., and Dunn, S. D. (2000) Site-directed cross-linking of b to the α, β, and a subunits of the Escherichia coli ATP synthase. J. Biol. Chem. 275, 17571-17577
    • (2000) J. Biol. Chem. , vol.275 , pp. 17571-17577
    • McLachlin, D.T.1    Coveny, A.M.2    Clark, S.M.3    Dunn, S.D.4
  • 30
    • 0032511038 scopus 로고    scopus 로고
    • The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions
    • McLachlin, D. T., Bestard, J. A., and Dunn, S. D. (1998) The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions. J. Biol. Chem. 273, 15162-15168
    • (1998) J. Biol. Chem. , vol.273 , pp. 15162-15168
    • McLachlin, D.T.1    Bestard, J.A.2    Dunn, S.D.3
  • 31
    • 0034724261 scopus 로고    scopus 로고
    • Disulfide linkage of the b and δ subunits does not affect the function of the Escherichia coli ATP synthase
    • McLachlin, D. T., and Dunn, S. D. (2000) Disulfide linkage of the b and δ subunits does not affect the function of the Escherichia coli ATP synthase. Biochemistry 39, 3486-3490
    • (2000) Biochemistry , vol.39 , pp. 3486-3490
    • McLachlin, D.T.1    Dunn, S.D.2
  • 32
    • 0037188394 scopus 로고    scopus 로고
    • The "second stalk" of Escherichia coli ATP synthase. Structure of the isolated dimerization domain
    • Del Rizzo, P. A., Bi, Y., Dunn, S. D., and Shilton, B. H. (2002) The "second stalk" of Escherichia coli ATP synthase. Structure of the isolated dimerization domain. Biochemistry 41, 6875-6884
    • (2002) Biochemistry , vol.41 , pp. 6875-6884
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3    Shilton, B.H.4
  • 35
    • 0035100279 scopus 로고    scopus 로고
    • Open-and-shut cases in coiled coil assembly. α-sheets and α-cylinders
    • Walshaw, J., and Woolfson, D. N. (2001) Open-and-shut cases in coiled coil assembly. α-sheets and α-cylinders. Protein Sci. 10, 668-673
    • (2001) Protein Sci. , vol.10 , pp. 668-673
    • Walshaw, J.1    Woolfson, D.N.2
  • 36
    • 33750951013 scopus 로고    scopus 로고
    • ATP synthase b subunit dimerization domain. Aright-handed coiled coil with offset helices
    • Del Rizzo, P. A., Bi, Y., and Dunn, S. D. (2006) ATP synthase b subunit dimerization domain. Aright-handed coiled coil with offset helices. J. Mol. Biol. 364, 735-746
    • (2006) J. Mol. Biol. , vol.364 , pp. 735-746
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3
  • 37
    • 36148937536 scopus 로고    scopus 로고
    • 1 sector of Escherichia coli ATP synthase
    • 1 sector of Escherichia coli ATP synthase. J. Biol. Chem. 282, 31920-31927
    • (2007) J. Biol. Chem. , vol.282 , pp. 31920-31927
    • Wood, K.S.1    Dunn, S.D.2
  • 38
    • 67649354869 scopus 로고    scopus 로고
    • Accommodating discontinuities in dimeric left-handed coiled coils in ATP synthase external stalks
    • Wise, J. G., and Vogel, P. D. (2009) Accommodating discontinuities in dimeric left-handed coiled coils in ATP synthase external stalks. Biophys. J. 96, 2823-2831
    • (2009) Biophys. J. , vol.96 , pp. 2823-2831
    • Wise, J.G.1    Vogel, P.D.2
  • 39
    • 0033960457 scopus 로고    scopus 로고
    • + transport to rotary catalysis in F-type ATP synthases. Structure and organization of the transmembrane rotary motor
    • + transport to rotary catalysis in F-type ATP synthases. Structure and organization of the transmembrane rotary motor. J. Exp. Biol. 203, 9-17
    • (2000) J. Exp. Biol. , vol.203 , pp. 9-17
    • Fillingame, R.H.1    Jiang, W.2    Dmitriev, O.Y.3
  • 40
    • 0034613389 scopus 로고    scopus 로고
    • 1 ATP synthase from the crosslinking of subunits b and c in the Escherichia coli enzyme
    • 1 ATP synthase from the crosslinking of subunits b and c in the Escherichia coli enzyme. J. Biol. Chem. 275, 31340-31346
    • (2000) J. Biol. Chem. , vol.275 , pp. 31340-31346
    • Jones, P.C.1    Hermolin, J.2    Jiang, W.3    Fillingame, R.H.4
  • 44
    • 0021736478 scopus 로고
    • In vivo evidence for the role of the ∈ subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli
    • Klionsky, D. J., Brusilow, W. S., and Simoni, R. D. (1984) In vivo evidence for the role of the ∈ subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J. Bacteriol. 160, 1055-1060
    • (1984) J. Bacteriol. , vol.160 , pp. 1055-1060
    • Klionsky, D.J.1    Brusilow, W.S.2    Simoni, R.D.3
  • 45
    • 0022001052 scopus 로고
    • Role of the b subunit of the Escherichia coli proton-translocating ATPase. A mutagenic analysis
    • Porter, A. C., Kumamoto, C., Aldape, K., and Simoni, R. D. (1985) Role of the b subunit of the Escherichia coli proton-translocating ATPase. A mutagenic analysis. J. Biol. Chem. 260, 8182-8187
    • (1985) J. Biol. Chem. , vol.260 , pp. 8182-8187
    • Porter, A.C.1    Kumamoto, C.2    Aldape, K.3    Simoni, R.D.4
  • 49
    • 64049091511 scopus 로고    scopus 로고
    • Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking
    • Ballhausen, B., Altendorf, K., and Deckers-Hebestreit, G. (2009) Constant c10 ring stoichiometry in the Escherichia coli ATP synthase analyzed by cross-linking. J. Bacteriol. 191, 2400-2404
    • (2009) J. Bacteriol. , vol.191 , pp. 2400-2404
    • Ballhausen, B.1    Altendorf, K.2    Deckers-Hebestreit, G.3
  • 50
  • 51
    • 0018716577 scopus 로고
    • The ATP synthetase of Escherichia coli K12. Purification of the enzyme and reconstitution of energy-transducing activities
    • Friedl, P., Friedl, C., and Schairer, H. U. (1979) The ATP synthetase of Escherichia coli K12. Purification of the enzyme and reconstitution of energy-transducing activities. Eur. J. Biochem. 100, 175-180
    • (1979) Eur. J. Biochem. , vol.100 , pp. 175-180
    • Friedl, P.1    Friedl, C.2    Schairer, H.U.3
  • 52
    • 0023147728 scopus 로고
    • A simple, non-chromatographic procedure to purify immunoglobulins from serum and ascites fluid
    • McKinney, M. M., and Parkinson, A. (1987) A simple, non-chromatographic procedure to purify immunoglobulins from serum and ascites fluid. J. Immunol. Methods 96, 271-278
    • (1987) J. Immunol. Methods , vol.96 , pp. 271-278
    • McKinney, M.M.1    Parkinson, A.2
  • 53
    • 0026694624 scopus 로고
    • O complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies
    • O complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies. J. Biol. Chem. 267, 12364-12369
    • (1992) J. Biol. Chem. , vol.267 , pp. 12364-12369
    • Deckers-Hebestreit, G.1    Simoni, R.D.2    Altendorf, K.3
  • 54
    • 46049096340 scopus 로고    scopus 로고
    • The stoichiometry of subunit c of Escherichia coli ATP synthase is independent of its rate of synthesis
    • Krebstakies, T., Aldag, I., Altendorf, K., Greie, J.-C., and Deckers-Hebestreit, G. (2008) The stoichiometry of subunit c of Escherichia coli ATP synthase is independent of its rate of synthesis. Biochemistry 47, 6907-6916
    • (2008) Biochemistry , vol.47 , pp. 6907-6916
    • Krebstakies, T.1    Aldag, I.2    Altendorf, K.3    Greie, J.-C.4    Deckers-Hebestreit, G.5
  • 55
    • 0016642871 scopus 로고
    • A simple technique for eliminating interference by detergents in the Lowry method of protein determination
    • Dulley, J. R., and Grieve, P. A. (1975) A simple technique for eliminating interference by detergents in the Lowry method of protein determination. Anal. Biochem. 64, 136-141
    • (1975) Anal. Biochem. , vol.64 , pp. 136-141
    • Dulley, J.R.1    Grieve, P.A.2
  • 56
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 60
    • 84875255512 scopus 로고    scopus 로고
    • Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking
    • DeLeon-Rangel, J., Ishmukhametov, R. R., Jiang, W., Fillingame, R. H., and Vik, S. B. (2013) Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking. FEBS Lett. 587, 892-897
    • (2013) FEBS Lett. , vol.587 , pp. 892-897
    • Deleon-Rangel, J.1    Ishmukhametov, R.R.2    Jiang, W.3    Fillingame, R.H.4    Vik, S.B.5
  • 61
    • 0023825124 scopus 로고
    • Improved silver staining procedure for fast staining in phast system development unit. I. Staining of sodium dodecyl sulfate gels
    • Heukeshoven, J., and Dernick, R. (1988) Improved silver staining procedure for fast staining in Phast System development unit. I. Staining of sodium dodecyl sulfate gels. Electrophoresis 9, 28-32
    • (1988) Electrophoresis , vol.9 , pp. 28-32
    • Heukeshoven, J.1    Dernick, R.2
  • 63
    • 79958858245 scopus 로고    scopus 로고
    • Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation
    • Cingolani, G., and Duncan, T. M. (2011) Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation. Nat. Struct. Mol. Biol. 18, 701-707
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 701-707
    • Cingolani, G.1    Duncan, T.M.2
  • 64
    • 78650063081 scopus 로고    scopus 로고
    • + transport from each side of the membrane
    • + transport from each side of the membrane. J. Biol. Chem. 285, 39811-39818
    • (2010) J. Biol. Chem. , vol.285 , pp. 39811-39818
    • Dong, H.1    Fillingame, R.H.2
  • 65
    • 0037809269 scopus 로고    scopus 로고
    • Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from. Escherichia coli
    • Zhang, D., and Vik, S. B. (2003) Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from. Escherichia coli. J. Biol. Chem. 278, 12319-12324
    • (2003) J. Biol. Chem. , vol.278 , pp. 12319-12324
    • Zhang, D.1    Vik, S.B.2
  • 66
    • 0022835820 scopus 로고
    • O portion of the Escherichia coli proton translocating ATPase
    • O portion of the Escherichia coli proton translocating ATPase. J. Biol. Chem. 261, 10037-10042
    • (1986) J. Biol. Chem. , vol.261 , pp. 10037-10042
    • Kumamoto, C.A.1    Simoni, R.D.2
  • 69
    • 0034353296 scopus 로고    scopus 로고
    • O-ATP synthase. Stalking mind and imagination
    • O-ATP synthase. Stalking mind and imagination. J. Bioenerg. Biomembr. 32, 333-339
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 333-339
    • Wilkens, S.1
  • 71
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A., and von Heijne, G. (2000) How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25, 429-434
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.