메뉴 건너뛰기




Volumn 270, Issue 8, 2003, Pages 1875-1884

The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane

Author keywords

ATP synthase; GxxxG motif; Oligomerization; Subunit e; Yeast

Indexed keywords

ALANINE; CYSTEINE; DIGITONIN; FUNGAL ENZYME; GLYCINE; LEUCINE; MUTANT PROTEIN; PROTEIN; PROTEIN GXXXG; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 0038070570     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03557.x     Document Type: Article
Times cited : (116)

References (44)
  • 1
    • 0033607774 scopus 로고    scopus 로고
    • Molecular rotary motors
    • Fillingame, R.H. (1999) Molecular rotary motors. Science 286, 1687-1688.
    • (1999) Science , vol.286 , pp. 1687-1688
    • Fillingame, R.H.1
  • 2
    • 0034532649 scopus 로고    scopus 로고
    • ATP synthases in the year 2000: Evolving views about the structures of these remarkable enzyme complexes
    • Pedersen, P.L., Ko, Y.H. & Hong, S. (2000) ATP synthases in the year 2000: evolving views about the structures of these remarkable enzyme complexes. J. Bioenerg. Biomembr. 32, 325-332.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 325-332
    • Pedersen, P.L.1    Ko, Y.H.2    Hong, S.3
  • 4
    • 0037085010 scopus 로고    scopus 로고
    • The molecular mechanism of ATP synthesis by F(1)F(0)-ATP synthase
    • Senior, A.E., Nadanaciva, S. & Weber, J. (2002) The molecular mechanism of ATP synthesis by F(1)F(0)-ATP synthase. Biochim. Biophys. Acta 1553, 188-211.
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 188-211
    • Senior, A.E.1    Nadanaciva, S.2    Weber, J.3
  • 5
    • 0028114231 scopus 로고
    • Structure at 2.8 angstrom resolution of F-1-ATPase from bovine heart mitochondria
    • Abrahams, J.P., Leslie, A.G.W., Lutter, R. & Walker, J.E. (1994) Structure at 2.8 angstrom resolution of F-1-ATPase from bovine heart mitochondria. Nature 370, 621-528.
    • (1994) Nature , vol.370 , pp. 621-528
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 6
    • 0032529839 scopus 로고    scopus 로고
    • The 2.8-angstrom structure of rat liver F-1-ATPase: Configuration of a critical intermediate in ATP synthesis/hydrolysis
    • Bianchet, M.A., Hullihen, J., Pedersen, P.L. & Amzel, L.M. (1998) The 2.8-angstrom structure of rat liver F-1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis. Proc. Natl Acad. Sci. USA 95, 11065-11070.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11065-11070
    • Bianchet, M.A.1    Hullihen, J.2    Pedersen, P.L.3    Amzel, L.M.4
  • 7
    • 0033598770 scopus 로고    scopus 로고
    • Structural features of the gamma subunit of the Escherichia coli F-1 ATPase revealed by a 4.4-angstrom resolution map obtained by x-ray crystallography
    • Hausrath, A.C., Grüber, G., Matthews, B.W. & Capaldi, R.A. (1999) Structural features of the gamma subunit of the Escherichia coli F-1 ATPase revealed by a 4.4-angstrom resolution map obtained by x-ray crystallography. Proc. Natl Acad. Sci. USA 96, 13697-13702.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13697-13702
    • Hausrath, A.C.1    Grüber, G.2    Matthews, B.W.3    Capaldi, R.A.4
  • 8
    • 0033766435 scopus 로고    scopus 로고
    • Thestructure of the central stalk in bovine F1-ATPase at 2.4 Å resolution
    • Gibbons, C., Montgomery, M.G., Leslie, A.G.W. & Walker, J.E. (2000) Thestructure of the central stalk in bovine F1-ATPase at 2.4 Å resolution. Nat. Struct. Biol. 7, 1055-1061.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1055-1061
    • Gibbons, C.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 9
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A.G.W. & Walker, J.E. (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 11
    • 0031567491 scopus 로고    scopus 로고
    • Yeastmitochondrial F1F0-ATPase: The novel subunit e is identical to Tim11
    • Arnold, I., Bauer, M.F., Brunner, M., Neupert, W. & Stuart, R.A. (1997) Yeastmitochondrial F1F0-ATPase: the novel subunit e is identical to Tim11. FEBS Lett. 411, 195-200.
    • (1997) FEBS Lett. , vol.411 , pp. 195-200
    • Arnold, I.1    Bauer, M.F.2    Brunner, M.3    Neupert, W.4    Stuart, R.A.5
  • 12
    • 0032534790 scopus 로고    scopus 로고
    • Yeastmitochondrial F1F0-ATP synthase exists as a dimer: Identification of three dimer-specific subunits
    • Arnold, I., Pfieffer, K., Neupert, W., Stuart, R.A. & Schägger, H. (1998) Yeastmitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO J. 17, 7170-7178.
    • (1998) EMBO J. , vol.17 , pp. 7170-7178
    • Arnold, I.1    Pfieffer, K.2    Neupert, W.3    Stuart, R.A.4    Schägger, H.5
  • 13
    • 0034530609 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ATP synthase
    • Velours, J. & Arselin, G. (2000) The Saccharomyces cerevisiae ATP synthase. J. Bioenerg. Biomembr. 32, 383-390.
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 383-390
    • Velours, J.1    Arselin, G.2
  • 15
    • 0037155894 scopus 로고    scopus 로고
    • In the absence of the first membrane-spanning segment of subunit 4(b), the yeast ATP synthase is functional but does not dimerize or oligomerize
    • Soubannier, V., Vaillier, J., Paumard, P., Coulary, B., Schaeffer, J. & Velours, J. (2002) In the absence of the first membrane-spanning segment of subunit 4(b), the yeast ATP synthase is functional but does not dimerize or oligomerize. J. Biol. Chem. 277, 10739-10745.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10739-10745
    • Soubannier, V.1    Vaillier, J.2    Paumard, P.3    Coulary, B.4    Schaeffer, J.5    Velours, J.6
  • 17
    • 0029786323 scopus 로고    scopus 로고
    • Membrane topography andnear-neighbor relationships of the mitochondrial ATP synthase subunits e, f, and g
    • Belogrudov, G.I., Tomich, J.M. & Hatefi, Y. (1996) Membrane topography andnear-neighbor relationships of the mitochondrial ATP synthase subunits e, f, and g. J. Biol. Chem. 271, 20340-20345.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20340-20345
    • Belogrudov, G.I.1    Tomich, J.M.2    Hatefi, Y.3
  • 18
    • 0035795181 scopus 로고    scopus 로고
    • Stoichiometry of subunit e in rat liver mitochondrial H(+)-ATP synthase and membrane topology of its putative Ca(2+)-dependent regulatory region
    • Arakaki, N., Ueyama, Y., Hirose, M., Himeda, T., Shibata, H., Futaki, S., Kitagawa, K. & Higuti, T. (2001) Stoichiometry of subunit e in rat liver mitochondrial H(+)-ATP synthase and membrane topology of its putative Ca(2+)-dependent regulatory region. Biochim. Biophys. Acta 1504, 220-228.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 220-228
    • Arakaki, N.1    Ueyama, Y.2    Hirose, M.3    Himeda, T.4    Shibata, H.5    Futaki, S.6    Kitagawa, K.7    Higuti, T.8
  • 19
    • 0026980195 scopus 로고
    • Complete amino acid sequence of subunit e of rat liver mitochondrial H(+)-ATP synthase
    • Higuti, T., Kuroiwa, K., Kawamura, Y. & Yoshihara, Y. (1992) Complete amino acid sequence of subunit e of rat liver mitochondrial H(+)-ATP synthase. Biochemistry 31, 12451-12454.
    • (1992) Biochemistry , vol.31 , pp. 12451-12454
    • Higuti, T.1    Kuroiwa, K.2    Kawamura, Y.3    Yoshihara, Y.4
  • 20
    • 0029840353 scopus 로고    scopus 로고
    • The e subunit gene of murine F1F0-ATP synthase - Genomic sequence, chromosomal mapping and diet regulation
    • Swartz, D.A., Park, E.I., Visek, W.J. & Kaput, J. (1996) The e subunit gene of murine F1F0-ATP synthase - Genomic sequence, chromosomal mapping and diet regulation. J. Biol. Chem. 271, 20942-20948.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20942-20948
    • Swartz, D.A.1    Park, E.I.2    Visek, W.J.3    Kaput, J.4
  • 21
    • 0030901438 scopus 로고    scopus 로고
    • Regulation of ATP synthase subunit eexpression by hypoxia: Cell differentiation stage-specific control
    • Levy, F.H. & Kelly, D.P. (1997) Regulation of ATP synthase subunit eexpression by hypoxia: cell differentiation stage-specific control. Am. J. Physiol. 272, C457-C465.
    • (1997) Am. J. Physiol. , vol.272
    • Levy, F.H.1    Kelly, D.P.2
  • 22
    • 0024447422 scopus 로고
    • The role of subunit, 4, a nuclear-encoded protein of the F0 sector of yeast mitochondrial, ATP synthase, in the assembly of the whole complex
    • Paul, M.F., Velours, J., Arselin de Chateaubodeau, G., Aigle, M. & Guérin, B. (1989) The role of subunit, 4, a nuclear-encoded protein of the F0 sector of yeast mitochondrial, ATP synthase, in the assembly of the whole complex. Eur. J. Biochem. 185, 163-171.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 163-171
    • Paul, M.F.1    Velours, J.2    Arselin De Chateaubodeau, G.3    Aigle, M.4    Guérin, B.5
  • 23
  • 24
    • 0030035504 scopus 로고    scopus 로고
    • Essential cysteines in 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase from Escherichia coli: Analysis by chemical modification and site-directed mutagenesis
    • Salleh, H.M., Patel, M.A. & Woodard, R.W. (1996) Essential cysteines in 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase from Escherichia coli: analysis by chemical modification and site-directed mutagenesis. Biochemistry 35, 8942-8947.
    • (1996) Biochemistry , vol.35 , pp. 8942-8947
    • Salleh, H.M.1    Patel, M.A.2    Woodard, R.W.3
  • 25
    • 0017165518 scopus 로고
    • Perméabilité de la membrane interne des mitochondries de levure: Étude des relations entre structure et activité
    • Arselin de Chateaubodeau, G., Guérin, M. & Guérin, B. (1976) Perméabilité de la membrane interne des mitochondries de levure: étude des relations entre structure et activité. Biochimie (Paris) 58, 601-610.
    • (1976) Biochimie (Paris) , vol.58 , pp. 601-610
    • Arselin De Chateaubodeau, G.1    Guérin, M.2    Guérin, B.3
  • 26
    • 0018337162 scopus 로고
    • Preparation of yeast mitochondria (Saccharomyces cerevisiae) with good P/O and respiratory control ratios
    • Guérin, B., Labbe, P. & Somlo, M. (1979) Preparation of yeast mitochondria (Saccharomyces cerevisiae) with good P/O and respiratory control ratios. Methods Enzymol. 55, 149-159.
    • (1979) Methods Enzymol. , vol.55 , pp. 149-159
    • Guérin, B.1    Labbe, P.2    Somlo, M.3
  • 28
    • 0018485375 scopus 로고
    • Phosphate transport and ATP synthesis in yeast mitochondria: Effect of a new inhibitor: The tribenzylphosphate
    • Rigoulet, M. & Guérin, B. (1979) Phosphate transport and ATP synthesis in yeast mitochondria: effect of a new inhibitor: the tribenzylphosphate. FEBS Lett. 102, 18-22.
    • (1979) FEBS Lett. , vol.102 , pp. 18-22
    • Rigoulet, M.1    Guérin, B.2
  • 29
    • 0017103173 scopus 로고
    • Continuous monitoring of ATP-converting reactions by purified firefly luciferase
    • Lundin, A., Richardsson, A. & Thore, A. (1976) Continuous monitoring of ATP-converting reactions by purified firefly luciferase. Anal. Biochem. 75, 611-620.
    • (1976) Anal. Biochem. , vol.75 , pp. 611-620
    • Lundin, A.1    Richardsson, A.2    Thore, A.3
  • 30
    • 0343471411 scopus 로고    scopus 로고
    • Control of oxidative-phosphorylation in rat liver mitochondria: Effect of ionic media
    • Devin, A., Guérin, B. & Rigoulet, M. (1997) Control of oxidative-phosphorylation in rat liver mitochondria: effect of ionic media. Biochim. Biophys. Acta 1319, 293-300.
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 293-300
    • Devin, A.1    Guérin, B.2    Rigoulet, M.3
  • 31
    • 0035896628 scopus 로고    scopus 로고
    • Bovine coupling factor 6, with just 14.5% shared identity, replaces subunit h in the yeast ATP synthase
    • Velours, J., Vaillier, J., Paumard, P., Soubannier, V., Lai-Zhang, J. & Mueller, D.M. (2001) Bovine coupling factor 6, with just 14.5% shared identity, replaces subunit h in the yeast ATP synthase. J. Biol. Chem. 276, 8602-8607.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8602-8607
    • Velours, J.1    Vaillier, J.2    Paumard, P.3    Soubannier, V.4    Lai-Zhang, J.5    Mueller, D.M.6
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide 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
  • 33
    • 0029808314 scopus 로고    scopus 로고
    • ATP synthase of yeast mitochondria. Isolation of the subunit h and disruption of the ATP14 gene
    • Arselin, G., Vaillier, J., Graves, P.V. & Velours, J. (1996) ATP synthase of yeast mitochondria. Isolation of the subunit h and disruption of the ATP14 gene. J. Biol. Chem. 271, 20284-20290.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20284-20290
    • Arselin, G.1    Vaillier, J.2    Graves, P.V.3    Velours, J.4
  • 34
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H. & von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 35
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schägger, H., Cramer, W.A. & von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 36
    • 0016747666 scopus 로고
    • A highly stable adenosine Triphosphatase from a thermophillie bacterium. Purification, properties, and reconstitution
    • Yoshida, M., Sone, N., Hirata, H. & Kagawa, Y. (1975) A highly stable adenosine Triphosphatase from a thermophillie bacterium. Purification, properties, and reconstitution. J. Biol. Chem. 250, 7910-7916.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7910-7916
    • Yoshida, M.1    Sone, N.2    Hirata, H.3    Kagawa, Y.4
  • 37
    • 0030589133 scopus 로고    scopus 로고
    • Separation by blue native and colorless native polyacrylamide gel electrophoresis of the oxidative phosphorylation complexes of yeast mitochondria solubilized by different detergents: Specific staining of the different complexes
    • Grandier-Vazeille, X. & Guérin, M. (1996) Separation by blue native and colorless native polyacrylamide gel electrophoresis of the oxidative phosphorylation complexes of yeast mitochondria solubilized by different detergents: specific staining of the different complexes. Anal. Biochem. 242, 248-254.
    • (1996) Anal. Biochem. , vol.242 , pp. 248-254
    • Grandier-Vazeille, X.1    Guérin, M.2
  • 38
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: The GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions
    • Senes, A., Gerstein, M. & Engelman, D.M. (2000) Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions. J. Mol. Biol. 296, 921-936.
    • (2000) J. Mol. Biol. , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 39
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ, W.P. & Engelman, D.M. (2000) The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296, 911-919.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 40
    • 0029893893 scopus 로고    scopus 로고
    • Ala-insertion scanning mutagenesis of the glycophorin A transmembrane helix: A rapid way to map helix-helix interactions in integral membrane proteins
    • Mingarro, I., Whitley, P., Lemmon, M.A. & von Heijne, G. (1996) Ala-insertion scanning mutagenesis of the glycophorin A transmembrane helix: a rapid way to map helix-helix interactions in integral membrane proteins. Protein Sci. 7, 1339-1341.
    • (1996) Protein Sci. , vol.7 , pp. 1339-1341
    • Mingarro, I.1    Whitley, P.2    Lemmon, M.A.3    Von Heijne, G.4
  • 41
    • 2242447081 scopus 로고    scopus 로고
    • Subunite of the yeast F1F0ATP synthase forms homodimers
    • Brunner, S., Everard-Gigot, V. & Stuart, R.A. (2002) Subunit e of the yeast F1F0ATP synthase forms homodimers. J. Biol. Chem. 277, 48484-48489.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48484-48489
    • Brunner, S.1    Everard-Gigot, V.2    Stuart, R.A.3
  • 42
    • 0024392222 scopus 로고
    • An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques
    • Allen, R.D., Schroeder, C.C. & Fok, A.K. (1989) An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques. J. Cell. Biol. 108, 2233-2240.
    • (1989) J. Cell. Biol. , vol.108 , pp. 2233-2240
    • Allen, R.D.1    Schroeder, C.C.2    Fok, A.K.3
  • 43
    • 0029200315 scopus 로고
    • Membrane tubulation and proton pumps
    • Allen, R.D. (1995) Membrane tubulation and proton pumps. Protoplasma 189, 1-8.
    • (1995) Protoplasma , vol.189 , pp. 1-8
    • Allen, R.D.1
  • 44
    • 0032508964 scopus 로고    scopus 로고
    • Evidence of a subunit 4 (subunit b) dimer in favor of the proximity of ATP synthase complexes in yeast inner mitochondrial membrane
    • Spannagel, C., Vaillier, J., Arselin, G., Graves, P.V., Grandier-Vazeille, X. & Velours, J. (1998) Evidence of a subunit 4 (subunit b) dimer in favor of the proximity of ATP synthase complexes in yeast inner mitochondrial membrane. Biochim. Biophys. Acta 1414, 260-264.
    • (1998) Biochim. Biophys. Acta , vol.1414 , pp. 260-264
    • Spannagel, C.1    Vaillier, J.2    Arselin, G.3    Graves, P.V.4    Grandier-Vazeille, X.5    Velours, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.