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Volumn 45, Issue 51, 2006, Pages 15893-15902

Assembly of the stator in Escherichia coli ATP synthase. Complexation of α subunit with other F1 subunits is prerequisite for δ subunit binding to the N-terminal region of α

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; COMPLEXATION; DISSOCIATION; ESCHERICHIA COLI; MONOMERS; PROTONS; STOICHIOMETRY;

EID: 33845957386     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0619730     Document Type: Article
Times cited : (16)

References (50)
  • 1
    • 0742305298 scopus 로고    scopus 로고
    • Happy motoring with ATP synthase
    • Senior, A. E., and Weber, J. (2004) Happy motoring with ATP synthase, Nat. Struct. Mol. Biol. 11, 110-112.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 110-112
    • Senior, A.E.1    Weber, J.2
  • 4
    • 0035910414 scopus 로고    scopus 로고
    • The rotary machine in the cell, ATP synthase
    • Noji, H., and Yoshida, M. (2001) The rotary machine in the cell, ATP synthase, J. Biol. Chem. 276, 1665-1668.
    • (2001) J. Biol. Chem , vol.276 , pp. 1665-1668
    • Noji, H.1    Yoshida, M.2
  • 6
    • 33748986212 scopus 로고    scopus 로고
    • ATP synthase: Subunit-subunit interactions in the stator stalk
    • Weber, J. (2006) ATP synthase: Subunit-subunit interactions in the stator stalk, Biochim. Biophys. Acta 1757, 1162-1170.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1162-1170
    • Weber, J.1
  • 9
    • 0038584352 scopus 로고    scopus 로고
    • 3 as determined by fluorescence correlation spectroscopy
    • 3 as determined by fluorescence correlation spectroscopy, Biochemistry 38, 13759-13765.
    • (1999) Biochemistry , vol.38 , pp. 13759-13765
    • Häsler, K.1    Panke, O.2    Junge, W.3
  • 11
    • 0038190861 scopus 로고    scopus 로고
    • o-ATP synthase. Binding of δ subunit to a 22-residue peptide mimicking the N-terminal region of α subunit
    • o-ATP synthase. Binding of δ subunit to a 22-residue peptide mimicking the N-terminal region of α subunit, J. Biol. Chem. 278, 13263-13626.
    • (2003) J. Biol. Chem , vol.278 , pp. 13263-13626
    • Weber, J.1    Muharemagic, A.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 14
    • 33745713048 scopus 로고    scopus 로고
    • The peripheral stalk of the mitochondrial ATP synthase
    • Walker, J. E., and Dickson, V. K. (2006) The peripheral stalk of the mitochondrial ATP synthase, Biochim. Biophys. Acta 1757, 286-296.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 286-296
    • Walker, J.E.1    Dickson, V.K.2
  • 15
    • 0031055743 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the δ subunit of the Escherichia coli ATP synthase
    • Wilkens, S., Dunn, S. D., Chandler, J., Dahlquist, F. W., and Capaldi, R. A. (1997) Solution structure of the N-terminal domain of the δ subunit of the Escherichia coli ATP synthase, Nat. Struct. Biol. 4, 198-201.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 198-201
    • Wilkens, S.1    Dunn, S.D.2    Chandler, J.3    Dahlquist, F.W.4    Capaldi, R.A.5
  • 17
    • 0021094213 scopus 로고
    • 1-ATPase to bind the oligomycin-sensitivity conferring protein (OSCP)
    • 1-ATPase to bind the oligomycin-sensitivity conferring protein (OSCP), FEBS Lett. 184, 677-701.
    • (1983) FEBS Lett , vol.184 , pp. 677-701
    • Hundal, T.1    Norling, B.2    Ernster, L.3
  • 21
    • 3342922088 scopus 로고
    • A microcolorimetric method for the determination of inorganic phosphorus
    • Taussky, H. H., and Shorr, E. (1953) A microcolorimetric method for the determination of inorganic phosphorus, J. Biol. Chem. 202, 675-685.
    • (1953) J. Biol. Chem , vol.202 , pp. 675-685
    • Taussky, H.H.1    Shorr, E.2
  • 22
    • 0021112492 scopus 로고
    • 1 and the membrane sector of the proton ATPase of Escherichia coli
    • 1 and the membrane sector of the proton ATPase of Escherichia coli, J. Biol. Chem. 258, 9793-9800.
    • (1983) J. Biol. Chem , vol.258 , pp. 9793-9800
    • Perlin, D.S.1    Cox, D.N.2    Senior, A.E.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0021736478 scopus 로고
    • In vivo evidence for the role of the ε subunit as an inhibitor of the proton translocating ATPase of Escherichia coli
    • Klionsky, D. J., Brusilow, W. S. A., and Simoni, R. D. (1984) In vivo evidence for the role of the ε 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.A.2    Simoni, R.D.3
  • 30
    • 0023929638 scopus 로고
    • A novel method for site-specific mutagenesis
    • Vandeyar, M., Weiner, M., Hutton, C, and Batt, C. (1988) A novel method for site-specific mutagenesis, Gene 65, 129-133.
    • (1988) Gene , vol.65 , pp. 129-133
    • Vandeyar, M.1    Weiner, M.2    Hutton, C.3    Batt, C.4
  • 34
    • 0018200296 scopus 로고
    • The ε subunit of Escherichia coli coupling factor 1 is required for its binding to the cytoplasmic membrane
    • Sternweis, P. (1978) The ε subunit of Escherichia coli coupling factor 1 is required for its binding to the cytoplasmic membrane, J. Biol. Chem. 253, 3123-3128.
    • (1978) J. Biol. Chem , vol.253 , pp. 3123-3128
    • Sternweis, P.1
  • 35
    • 0023522190 scopus 로고
    • 1-ATPase enzymes suggest that a cyclical catalytic mechanism involving three catalytic sites occurs
    • 1-ATPase enzymes suggest that a cyclical catalytic mechanism involving three catalytic sites occurs, J. Biol. Chem. 262, 17450-17454.
    • (1987) J. Biol. Chem , vol.262 , pp. 17450-17454
    • Rao, R.1    Senior, A.E.2
  • 38
    • 0032511038 scopus 로고    scopus 로고
    • o-ATP synthase interact via residues in their C-terminal regions
    • o-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
  • 40
    • 0017411003 scopus 로고
    • Characterization of the purified membrane attachment (δ) subunit of the proton translocating adenosine triphosphatase from Escherichia coli
    • Sternweis, P. C., and Smith, J. B. (1977) Characterization of the purified membrane attachment (δ) subunit of the proton translocating adenosine triphosphatase from Escherichia coli, Biochemistry 16, 4020-4025.
    • (1977) Biochemistry , vol.16 , pp. 4020-4025
    • Sternweis, P.C.1    Smith, J.B.2
  • 42
    • 0027170676 scopus 로고
    • o-ATPase, a large multimeric membrane-bound enzyme
    • o-ATPase, a large multimeric membrane-bound enzyme, Mol. Microbiol. 9, 419-424.
    • (1993) Mol. Microbiol , vol.9 , pp. 419-424
    • Brusilow, W.S.A.1
  • 47
    • 0020457179 scopus 로고
    • Differential polypeptide synthesis of the proton-translocating ATPase of Escherichia coli
    • Brusilow, W. S. A., Klionsky, D. J., and Simoni, R. D. (1982) Differential polypeptide synthesis of the proton-translocating ATPase of Escherichia coli, J. Bacteriol. 151, 1363-1371.
    • (1982) J. Bacteriol , vol.151 , pp. 1363-1371
    • Brusilow, W.S.A.1    Klionsky, D.J.2    Simoni, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.