메뉴 건너뛰기




Volumn 46, Issue 29, 2007, Pages 8680-8688

Insight into the bind-lock mechanism of the yeast mitochondrial ATP synthase inhibitory peptide

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC STATE; KINETIC RESTRICTION; NONCATALYTIC SITES; NUCLEOTIDE BINDING;

EID: 34547135425     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700522v     Document Type: Article
Times cited : (12)

References (56)
  • 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
  • 3
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell, P. (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism, Nature 191, 144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 4
    • 0017409108 scopus 로고
    • A commentary on alternative hypotheses of protonic coupling in the membrane systems catalysing oxidative and photosynthetic phosphorylation
    • Mitchell, P. (1977) A commentary on alternative hypotheses of protonic coupling in the membrane systems catalysing oxidative and photosynthetic phosphorylation, FEBS Lett. 78, 1-20.
    • (1977) FEBS Lett , vol.78 , pp. 1-20
    • Mitchell, P.1
  • 7
    • 0347504884 scopus 로고    scopus 로고
    • Structure of the mitochondrial ATP synthase by electron cryomicroscopy
    • Rubinstein, J. L, Walker J, E., and Henderson, R. (2003) Structure of the mitochondrial ATP synthase by electron cryomicroscopy, EMBO J. 22, 6182-6192.
    • (2003) EMBO J , vol.22 , pp. 6182-6192
    • Rubinstein, J.L.1    Walker, J.E.2    Henderson, R.3
  • 10
    • 0020490477 scopus 로고
    • 1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites
    • 1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites, J. Biol. Chem. 257, 2874-2881.
    • (1982) J. Biol. Chem , vol.257 , pp. 2874-2881
    • Cross, R.L.1    Nalin, C.M.2
  • 11
    • 0019889785 scopus 로고
    • 1 adenosine-5′-triphosphatase as monitored by the differential effects of inhibitors and nucleotide analogues on the 'hysteretic' behavior of the enzyme
    • 1 adenosine-5′-triphosphatase as monitored by the differential effects of inhibitors and nucleotide analogues on the 'hysteretic' behavior of the enzyme, Biochemistry 20, 6312-6318.
    • (1981) Biochemistry , vol.20 , pp. 6312-6318
    • Di Pietro, A.1    Godinot, C.2    Gautheron, D.C.3
  • 12
    • 0027507106 scopus 로고
    • 0ATP synthase. Cofactors in hydrolysis?
    • 0ATP synthase. Cofactors in hydrolysis? FEBS Lett. 316, 209-215.
    • (1993) FEBS Lett , vol.316 , pp. 209-215
    • Harris, D.A.1
  • 13
    • 0027982788 scopus 로고
    • 1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP
    • 1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP, J. Biol Chem. 269, 319-325.
    • (1994) J. Biol Chem , vol.269 , pp. 319-325
    • Jault, J.-M.1    Allison, W.S.2
  • 15
    • 0034615699 scopus 로고    scopus 로고
    • 1-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides
    • 1-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides, J. Biol. Chem. 275, 10057-10063.
    • (2000) J. Biol. Chem , vol.275 , pp. 10057-10063
    • Ren, H.1    Allison, W.S.2
  • 19
    • 0000228422 scopus 로고
    • A naturally occurring inhibitor of mitochondrial adenosine triphosphatase
    • Pullman, M. E., and 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
  • 20
    • 0019630329 scopus 로고
    • Amino acid sequence of an intrinsic inhibitor of mitochondrial ATPase from yeast
    • Matsubara, H., Hase, T., Hashimoto, T., and Tagawa, K. (1981) Amino acid sequence of an intrinsic inhibitor of mitochondrial ATPase from yeast, J. Biochem. (Tokyo) 90, 1159-1165.
    • (1981) J. Biochem. (Tokyo) , vol.90 , pp. 1159-1165
    • Matsubara, H.1    Hase, T.2    Hashimoto, T.3    Tagawa, K.4
  • 21
    • 0025237475 scopus 로고
    • Evidence for an endogenous ATPase inhibitor protein in plant mitochondria. Purification and characterization
    • Norling, B., Tourikas, C., Hamasur, B., and Glaser, E. (1990) Evidence for an endogenous ATPase inhibitor protein in plant mitochondria. Purification and characterization, Eur. J. Biochem. 188, 247-252.
    • (1990) Eur. J. Biochem , vol.188 , pp. 247-252
    • Norling, B.1    Tourikas, C.2    Hamasur, B.3    Glaser, E.4
  • 22
    • 0037126590 scopus 로고    scopus 로고
    • The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase
    • Cabezón, E., Runswick, M. J., Leslie, A. G., and Walker J. E. (2001) The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase, EMBO J. 20, 6990-6996.
    • (2001) EMBO J , vol.20 , pp. 6990-6996
    • Cabezón, E.1    Runswick, M.J.2    Leslie, A.G.3    Walker, J.E.4
  • 23
    • 0022791949 scopus 로고
    • Regulation of the mitochondrial ATP synthase/ATPase complex
    • Schwerzmann, K., and 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
  • 25
    • 0021110084 scopus 로고
    • ATP synthesis and hydrolysis in submitochondrial particles subjected to an acid-base transition. Effects of the ATPase inhibitor protein
    • Husain, I., and Harris, D. A. (1983) ATP synthesis and hydrolysis in submitochondrial particles subjected to an acid-base transition. Effects of the ATPase inhibitor protein, FEBS Lett. 160, 110-114.
    • (1983) FEBS Lett , vol.160 , pp. 110-114
    • Husain, I.1    Harris, D.A.2
  • 26
    • 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
  • 27
    • 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., and 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
  • 28
    • 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
  • 29
    • 0023848774 scopus 로고
    • Kinetics of the release of the mitochondrial inhibitor protein. Correlation with synthesis and hydrolysis of ATP
    • Lippe, G., Sorgato, M. C., and 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
  • 30
    • 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., and 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
  • 31
    • 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., and 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
  • 32
    • 0019880885 scopus 로고
    • Electrochemical gradient induced displacement of the natural ATPase inhibitor protein from mitochondrial ATPase as directed by antibodies against the inhibitor protein
    • Dreyfus, G., Gómez-Puyou, A., and de Gómez-Puyou, M. T. (1981) Electrochemical gradient induced displacement of the natural ATPase inhibitor protein from mitochondrial ATPase as directed by antibodies against the inhibitor protein, Biochem. Biophys. Res. Commun. 100, 400-406.
    • (1981) Biochem. Biophys. Res. Commun , vol.100 , pp. 400-406
    • Dreyfus, G.1    Gómez-Puyou, A.2    de Gómez-Puyou, M.T.3
  • 33
    • 0021189305 scopus 로고
    • Release of the inhibitory action of the natural ATPase inhibitor protein on the mitochondrial ATPase
    • Beltran, C., de Gómez-Puyou, M. T., Gómez-Puyou, A., and 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 Gómez-Puyou, M.T.2    Gómez-Puyou, A.3    Darszon, A.4
  • 37
    • 0017743098 scopus 로고
    • Natural protein ATPase inhibitor from Candida utilis mitochondria. Binding properties of the radiolabeled inhibitor
    • Klein, G., Satre, M., and Vignais, P. (1977) Natural protein ATPase inhibitor from Candida utilis mitochondria. Binding properties of the radiolabeled inhibitor, FEBS Lett. 84, 129-134.
    • (1977) FEBS Lett , vol.84 , pp. 129-134
    • Klein, G.1    Satre, M.2    Vignais, P.3
  • 38
    • 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, Y.M.1
  • 40
    • 0027451387 scopus 로고
    • 1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites
    • 1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites, J. Biol. Chem. 268, 23179-23185.
    • (1993) J. Biol. Chem , vol.268 , pp. 23179-23185
    • Milgrom, Y.M.1    Cross, R.L.2
  • 43
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure
    • Gietz, R. D., Schiestl, R. H., Willems, A. R., and Woods, R. A. (1995) Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure, Yeast 11, 355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 44
    • 0022899463 scopus 로고
    • 1-ATPase from the yeast Schizosaccharomyces pombe. Involvement of α- and γ-subunits in the enzyme activity
    • 1-ATPase from the yeast Schizosaccharomyces pombe. Involvement of α- and γ-subunits in the enzyme activity, J. Biol. Chem. 261, 7151-7159.
    • (1986) J. Biol. Chem , vol.261 , pp. 7151-7159
    • Falson, P.1    Di Pietro, A.2    Gautheron, D.C.3
  • 46
    • 0027317040 scopus 로고
    • 1-ATPase provides a direct probe of nucleotide binding: Maximal ATP hydrolysis occurs with three sites occupied
    • 1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied, J. Biol. Chem. 268, 20126-20133.
    • (1993) J. Biol. Chem , vol.268 , pp. 20126-20133
    • Weber, J.1    Wilke-Mounts, S.2    Lee, R.S.3    Grell, E.4    Senior, A.E.5
  • 47
    • 0032564377 scopus 로고    scopus 로고
    • 1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP
    • 1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP, Biochemistry 37, 16151-16164.
    • (1998) Biochemistry , vol.37 , pp. 16151-16164
    • Dou, C.1    Fortes, P.A.2    Allison, W.S.3
  • 50
    • 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, Y.M.1
  • 52
    • 25444452953 scopus 로고    scopus 로고
    • 1-ATPase correlates with the filling of the second of three catalytic sites
    • 1-ATPase correlates with the filling of the second of three catalytic sites, Proc. Natl. Acad. Sci. U.S.A. 102, 13831-13836.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 13831-13836
    • Milgrom, Y.M.1    Cross, R.L.2
  • 53
    • 33646702831 scopus 로고    scopus 로고
    • 1-ATPase does not hydolyze ATP at a significant rate until the substrate binds to the catalytic site of the lowest affinity
    • 1-ATPase does not hydolyze ATP at a significant rate until the substrate binds to the catalytic site of the lowest affinity, Biochemistry 45, 6222-6230.
    • (2006) Biochemistry , vol.45 , pp. 6222-6230
    • Ren, H.1    Bandyopadhyay, S.2    Allison, W.S.3
  • 54
    • 0023130388 scopus 로고
    • 1-ATPase turnover during ATP hydrolysis by the single catalytic site
    • 1-ATPase turnover during ATP hydrolysis by the single catalytic site, FEBS Lett. 212, 63-67.
    • (1987) FEBS Lett , vol.212 , pp. 63-67
    • Milgrom, Y.M.1    Murataliev, M.B.2
  • 55
    • 0031435815 scopus 로고    scopus 로고
    • 1-ATPase exhibits strong positive catalytic cooperativity
    • 1-ATPase exhibits strong positive catalytic cooperativity, J. Biol. Chem. 272, 32211-32214.
    • (1997) J. Biol. Chem , vol.272 , pp. 32211-32214
    • Milgrom, Y.M.1    Cross, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.