메뉴 건너뛰기




Volumn 271, Issue 10, 2004, Pages 1963-1970

Functional transitions of F0F1-ATPase mediated by the inhibitory peptide IF1 in yeast coupled submitochondrial particles

Author keywords

ATP synthase; Catalytic state; Inhibitory peptide latent ATPase; Protonmotive force; Yeast

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEIN INHIBITOR; ADENOSINE TRIPHOSPHATE; ATPASE INHIBITORY PROTEIN; CARBONYL CYANIDE 4 (TRIFLUOROMETHOXY)PHENYLHYDRAZONE; ENZYME INHIBITOR; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; PROTEIN; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCOUPLING PROTEIN;

EID: 2442718745     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04108.x     Document Type: Article
Times cited : (3)

References (46)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer, P.D. (1997) The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66, 717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 4
    • 0142182186 scopus 로고    scopus 로고
    • Rotary movements within the ATP synthase do not constitute an obligatory element of the catalytic mechanism
    • Berden, J.A. (2003) Rotary movements within the ATP synthase do not constitute an obligatory element of the catalytic mechanism. IUBMB Life 55, 473-481.
    • (2003) IUBMB Life , vol.55 , pp. 473-481
    • Berden, J.A.1
  • 7
    • 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 26, 1700-1705.
    • (1999) Science , vol.26 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 8
    • 0000228422 scopus 로고
    • A naturally occurring inhibitor of mitochondrial adenosine triphosphatase
    • Pullman, M.E. & Monroy, G.C. (1963) A naturally occurring inhibitor of mitochondrial adenosine triphosphatase. J. Biol. Chem. 238, 3762-3768.
    • (1963) J. Biol. Chem. , vol.238 , pp. 3762-3768
    • Pullman, M.E.1    Monroy, G.C.2
  • 10
    • 0022791949 scopus 로고
    • Regulation of the mitochondrial ATP synthase/ATPase complex
    • Schwerzmann, K. & Pedersen, P.L. (1986) Regulation of the mitochondrial ATP synthase/ATPase complex. Arch. Biochem. Biophys. 250, 1-18.
    • (1986) Arch. Biochem. Biophys. , vol.250 , pp. 1-18
    • Schwerzmann, K.1    Pedersen, P.L.2
  • 12
    • 0017743098 scopus 로고
    • Natural protein ATPase inhibitor from Candida utilis mitochondria
    • Klein, G., Satre, M. & Vignais, P. (1977) Natural protein ATPase inhibitor from Candida utilis mitochondria. FEBS Lett. 84, 129-134.
    • (1977) FEBS Lett. , vol.84 , pp. 129-134
    • Klein, G.1    Satre, M.2    Vignais, P.3
  • 13
    • 0021110084 scopus 로고
    • ATP synthesis and hydrolysis in submitochondrial particles subjected to an acid-base transition
    • Husain, I. & Harris, D.A. (1983) ATP synthesis and hydrolysis in submitochondrial particles subjected to an acid-base transition. FEBS Lett. 160, 110-114.
    • (1983) FEBS Lett. , vol.160 , pp. 110-114
    • Husain, I.1    Harris, D.A.2
  • 14
    • 0021114939 scopus 로고
    • 1-ATPase from ox heart mitochondria with its naturally occurring inhibitor protein. Studies using radio-iodinated inhibitor protein
    • 1-ATPase from ox heart mitochondria with its naturally occurring inhibitor protein. Studies using radio-iodinated inhibitor protein. Biochim. Biophys. Acta 724, 128-141.
    • (1983) Biochim. Biophys. Acta , vol.724 , pp. 128-141
    • Power, J.1    Cross, R.L.2    Harris, D.A.3
  • 15
    • 0022430817 scopus 로고
    • 1-ATPase and its naturally occurring inhibitor protein. Studies using a specific anti-inhibitor antibody
    • 1-ATPase and its naturally occurring inhibitor protein. Studies using a specific anti-inhibitor antibody. Biochim. Biophys. Acta 806, 64-74.
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 64-74
    • Husain, I.1    Jackson, P.J.2    Harris, D.A.3
  • 16
    • 0023848774 scopus 로고
    • Kinetics of the release of the mitochondrial inhibitor protein. Correlation with synthesis and hydrolysis of ATP
    • Lippe, G., Sorgato, M.C. & Harris, D.A. (1988) Kinetics of the release of the mitochondrial inhibitor protein. Correlation with synthesis and hydrolysis of ATP. Biochim. Biophys. Acta 933, 1-11.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 1-11
    • Lippe, G.1    Sorgato, M.C.2    Harris, D.A.3
  • 17
    • 0023836981 scopus 로고
    • The binding and release of the inhibitor protein are governed independently by ATP and membrane potential in ox-heart submitochondrial vesicles
    • Lippe, G., Sorgato, M.C. & Harris, D.A. (1988) The binding and release of the inhibitor protein are governed independently by ATP and membrane potential in ox-heart submitochondrial vesicles. Biochim. Biophys. Acta 933, 12-21.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 12-21
    • Lippe, G.1    Sorgato, M.C.2    Harris, D.A.3
  • 18
    • 0021189305 scopus 로고
    • Release of the inhibitory action of the natural ATPase inhibitor protein on the mitochondrial ATPase
    • Beltran, C., Tuena de Gómez-Puyou, M., Gómez-Puyou, A. & Darszon, A. (1984) Release of the inhibitory action of the natural ATPase inhibitor protein on the mitochondrial ATPase. Eur. J. Biochem. 144, 151-157.
    • (1984) Eur. J. Biochem. , vol.144 , pp. 151-157
    • Beltran, C.1    De Tuena Gómez-Puyou, M.2    Gómez-Puyou, A.3    Darszon, A.4
  • 19
    • 0019889799 scopus 로고
    • Proton-adenosine-triphosphatase complex of rat liver mitochondria: Effect of energy state on its interaction with the adenosinetriphosphatase inhibitory peptide
    • Schwerzmann, K. & Pedersen, P.L. (1981) Proton-adenosine- triphosphatase complex of rat liver mitochondria: effect of energy state on its interaction with the adenosinetriphosphatase inhibitory peptide. Biochemistry 20, 6305-6311.
    • (1981) Biochemistry , vol.20 , pp. 6305-6311
    • Schwerzmann, K.1    Pedersen, P.L.2
  • 24
    • 0041819514 scopus 로고    scopus 로고
    • The structure of bovine F1-ATPase in complex with its regulatory protein IF1
    • Cabezón, E., Montgomery, M.G., Leslie, A.G.W. & Walker, J.E. (2003) The structure of bovine F1-ATPase in complex with its regulatory protein IF1. Nat. Struct. Biol. 10, 744-750.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 744-750
    • Cabezón, E.1    Montgomery, M.G.2    Leslie, A.G.W.3    Walker, J.E.4
  • 25
    • 0014961651 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXII. Interaction between mitochondrial adenosine triphosphatase inhibitor and mitochondrial adenosine triphosphatase
    • Horstman, L.L. & Racker, E. (1970) Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXII. Interaction between mitochondrial adenosine triphosphatase inhibitor and mitochondrial adenosine triphosphatase. J. Biol. Chem. 245, 1336-1344.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1336-1344
    • Horstman, L.L.1    Racker, E.2
  • 26
    • 0021876340 scopus 로고
    • Interaction between the mitochondrial ATP synthetase and ATPase inhibitor protein. Active/inactive slow pH-dependent transitions of the inhibitor protein
    • Panchenko, M.V. & Vinogradov, A.D. (1985) Interaction between the mitochondrial ATP synthetase and ATPase inhibitor protein. Active/inactive slow pH-dependent transitions of the inhibitor protein. FEBS Lett. 184, 226-230.
    • (1985) FEBS Lett. , vol.184 , pp. 226-230
    • Panchenko, M.V.1    Vinogradov, A.D.2
  • 27
    • 0025155005 scopus 로고
    • Activation of a complex of ATPase with the natural protein inhibitor in submitochondrial particles
    • Khodjaev, E.-Yu, Komarnitsky, F.B., Capozza, G., Dukhovich, V.F., Chernyak, B.V. & Papa, S. (1990) Activation of a complex of ATPase with the natural protein inhibitor in submitochondrial particles. FEBS Lett. 272, 145-148.
    • (1990) FEBS Lett. , vol.272 , pp. 145-148
    • Khodjaev, E.-Yu.1    Komarnitsky, F.B.2    Capozza, G.3    Dukhovich, V.F.4    Chernyak, B.V.5    Papa, S.6
  • 28
    • 0020649270 scopus 로고
    • pH-induced conformational change of ATPase inhibitor from yeast mitochondria. A proton magnetic resonance study
    • Fujii, S., Hashimoto, T., Yoshida, Y., Miura, R., Yamano, T. & Tagawa, K. (1983) pH-induced conformational change of ATPase inhibitor from yeast mitochondria. A proton magnetic resonance study. J. Biochem. (Tokyo) 93, 189-196.
    • (1983) J. Biochem. (Tokyo) , vol.93 , pp. 189-196
    • Fujii, S.1    Hashimoto, T.2    Yoshida, Y.3    Miura, R.4    Yamano, T.5    Tagawa, K.6
  • 29
    • 0027289039 scopus 로고
    • Factors affecting the species-homologous and species-heterologous binding of mitochondrial ATPase inhibitor, IF1, to the mitochondrial ATPase of slow and fast heart-rate hearts
    • Rouslin, W. & Broge, C.W. (1993) Factors affecting the species-homologous and species-heterologous binding of mitochondrial ATPase inhibitor, IF1, to the mitochondrial ATPase of slow and fast heart-rate hearts. Arch. Biochem. Biophys. 303, 443-450.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 443-450
    • Rouslin, W.1    Broge, C.W.2
  • 30
    • 0010443542 scopus 로고
    • Effect of the protonmotive force on ATP-linked processes and mobilization of the bound natural ATPase inhibitor in beef heart submitochondrial particles
    • Klein, G. & Vignais, P.V. (1983) Effect of the protonmotive force on ATP-linked processes and mobilization of the bound natural ATPase inhibitor in beef heart submitochondrial particles. J. Bioenerg. Biomembr. 15, 347-362.
    • (1983) J. Bioenerg. Biomembr. , vol.15 , pp. 347-362
    • Klein, G.1    Vignais, P.V.2
  • 31
    • 0024506165 scopus 로고
    • 1-ATPase inactivation by the natural inhibitor protein agrees with the alternating-site binding-change mechanism
    • 1-ATPase inactivation by the natural inhibitor protein agrees with the alternating-site binding-change mechanism. FEBS Lett. 246, 202-206.
    • (1989) FEBS Lett. , vol.246 , pp. 202-206
    • Milgrom, Ya.M.1
  • 33
    • 0033953115 scopus 로고    scopus 로고
    • 0 ATPase: Is ATP synthase a reversible molecular machine?
    • 0 ATPase: is ATP synthase a reversible molecular machine? J. Exp. Biol. 203, 41-49.
    • (2000) J. Exp. Biol. , vol.203 , pp. 41-49
    • Vinogradov, A.D.1
  • 37
    • 0034737931 scopus 로고    scopus 로고
    • Analysis of the nucleotide binding sites of mitochondrial ATP synthase provides evidence for a two-site catalytic mechanism
    • Berden, J.A., & Hartog, A.F. (2000) Analysis of the nucleotide binding sites of mitochondrial ATP synthase provides evidence for a two-site catalytic mechanism. Biochim. Biophys. Acta 1458, 234-251.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 234-251
    • Berden, J.A.1    Hartog, A.F.2
  • 38
    • 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
  • 39
    • 0038070088 scopus 로고    scopus 로고
    • Investigation of the role and mechanism of IF1 and STF1 proteins, twin inhibitory peptides which interact with the yeast mitochondrial ATP synthase
    • Venard, R., Brèthes, D., Giraud, M.-F., Vaillier, J., Velours, J. & Haraux, F. (2003) Investigation of the role and mechanism of IF1 and STF1 proteins, twin inhibitory peptides which interact with the yeast mitochondrial ATP synthase. Biochemistry 42, 7626-7636.
    • (2003) Biochemistry , vol.42 , pp. 7626-7636
    • Venard, R.1    Brèthes, D.2    Giraud, M.-F.3    Vaillier, J.4    Velours, J.5    Haraux, F.6
  • 41
    • 0021766207 scopus 로고
    • Interaction of the membrane-bound succinate dehydrogenase with substrate and competitive inhibitors
    • Kotlyar, A.V. & Vinogradov, A.D. (1984) Interaction of the membrane-bound succinate dehydrogenase with substrate and competitive inhibitors. Biochim. Biophys. Acta 784, 24-34.
    • (1984) Biochim. Biophys. Acta , vol.784 , pp. 24-34
    • Kotlyar, A.V.1    Vinogradov, A.D.2
  • 42
    • 50549170012 scopus 로고
    • Studies on bacterial photophosphorylation. III. A sensitive and rapid method of determination of photophosphorylation
    • Nishimura, M., Ito, T. & Chance, B. (1962) Studies on bacterial photophosphorylation. III. A sensitive and rapid method of determination of photophosphorylation. Biochim. Biophys. Acta 59, 177-182.
    • (1962) Biochim. Biophys. Acta , vol.59 , pp. 177-182
    • Nishimura, M.1    Ito, T.2    Chance, B.3
  • 44
    • 0025741748 scopus 로고
    • 1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites
    • 1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites. Eur. J. Biochem. 200, 789-795.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 789-795
    • Milgrom, Ya.M.1
  • 45
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell 10, 331-341.
    • (2001) Cell , vol.10 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.W.3
  • 46
    • 1842478082 scopus 로고    scopus 로고
    • 1-ATPase in Paracoccus denitrificans plasma membranes
    • 1-ATPase in Paracoccus denitrificans plasma membranes. J. Biol. Chem. 279, 12319-12324.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12319-12324
    • Zharova, T.V.1    Vinogradov, A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.