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Volumn 25, Issue 19, 2006, Pages 4596-4604

The regulator of the F1 motor: Inhibition of rotation of cyanobacterial F1-ATPase by the ε subunit

Author keywords

inhibition; ADP inhibition; ATP synthase; CF1; Rotation

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; BACTERIAL ENZYME; ADENOSINE TRIPHOSPHATE; DIMETHYLAMINE; GAMMA SUBUNIT, F(1) ATPASE; MOLECULAR MOTOR; MUTANT PROTEIN; N,N DIMETHYLDODECYLAMINE OXIDE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 33749404957     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601348     Document Type: Article
Times cited : (66)

References (66)
  • 4
    • 0020446907 scopus 로고
    • Modulation of the chloroplast ATPase by tight ADP binding. Effect of uncouplers and ATP
    • Bar-Zvi D, Shavit N (1982) Modulation of the chloroplast ATPase by tight ADP binding. Effect of uncouplers and ATP. J Bioenerg Biomembr 14: 467-478
    • (1982) J Bioenerg Biomembr , vol.14 , pp. 467-478
    • Bar-Zvi, D.1    Shavit, N.2
  • 5
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • Boyer PD (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
  • 6
    • 0029810877 scopus 로고    scopus 로고
    • Differences between two tight ADP binding sites of the chloroplast coupling factor 1 and their effects on ATPase activity
    • Digel JG, Kishinevsky A, Ong AM, McCarty RE (1996) Differences between two tight ADP binding sites of the chloroplast coupling factor 1 and their effects on ATPase activity. J Biol Chem 271: 19976-19982
    • (1996) J Biol Chem , vol.271 , pp. 19976-19982
    • Digel, J.G.1    Kishinevsky, A.2    Ong, A.M.3    McCarty, R.E.4
  • 9
    • 0022373065 scopus 로고
    • The role of tightly bound ADP on chloroplast ATPase
    • Feldman RI, Boyer PD (1985) The role of tightly bound ADP on chloroplast ATPase. J Biol Chem 260: 13088-13094
    • (1985) J Biol Chem , vol.260 , pp. 13088-13094
    • Feldman, R.I.1    Boyer, P.D.2
  • 10
    • 24944464164 scopus 로고    scopus 로고
    • 1-ATP synthase: The conformation of subunit ε might be determined by directionality of subunit γ rotation
    • 1-ATP synthase: the conformation of subunit ε might be determined by directionality of subunit γ rotation. FEBS Lett 579: 5114-5118
    • (2005) FEBS Lett , vol.579 , pp. 5114-5118
    • Feniouk, B.A.1    Junge, W.2
  • 11
    • 0020491269 scopus 로고
    • Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site
    • Grubmeyer C, Cross RL, Penefsky HS (1982) Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site. J Biol Chem 257: 12092-12100
    • (1982) J Biol Chem , vol.257 , pp. 12092-12100
    • Grubmeyer, C.1    Cross, R.L.2    Penefsky, H.S.3
  • 15
    • 0033407488 scopus 로고    scopus 로고
    • 1-ATPase can rotate in a unidirectional and counter-clockwise manner
    • 1-ATPase can rotate in a unidirectional and counter-clockwise manner. FEBS Lett 463: 35-38
    • (1999) FEBS Lett , vol.463 , pp. 35-38
    • Hisabori, T.1    Kondoh, A.2    Yoshida, M.3
  • 16
    • 0032568811 scopus 로고    scopus 로고
    • The formation or the reduction of a disulfide bridge on the γ subunit of chloroplast ATP synthase affects the inhibitory effect of the ε subunit
    • Hisabori T, Motohashi K, Kroth P, Strotmann H, Amano T (1998) The formation or the reduction of a disulfide bridge on the γ subunit of chloroplast ATP synthase affects the inhibitory effect of the ε subunit. J Biol Chem 273: 15901-15905
    • (1998) J Biol Chem , vol.273 , pp. 15901-15905
    • Hisabori, T.1    Motohashi, K.2    Kroth, P.3    Strotmann, H.4    Amano, T.5
  • 17
    • 0037716146 scopus 로고    scopus 로고
    • Molecular evolution of the modulator of chloroplast ATP synthase: Origin of the conformational change dependent regulation
    • Hisabori T, Ueoka-Nakanishi H, Konno H, Koyama F (2003) Molecular evolution of the modulator of chloroplast ATP synthase: origin of the conformational change dependent regulation. FEBS Lett 545: 71-75
    • (2003) FEBS Lett , vol.545 , pp. 71-75
    • Hisabori, T.1    Ueoka-Nakanishi, H.2    Konno, H.3    Koyama, F.4
  • 19
    • 0035942281 scopus 로고    scopus 로고
    • The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10
    • Jiang W, Hermolin J, Fillingame RH (2001) The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc Natl Acad Sci USA 98: 4966-4971
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4966-4971
    • Jiang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 20
    • 0024511018 scopus 로고
    • Energy coupling in bacterial periplasmic transport systems. Studies in intact Escherichia coli cells
    • Joshi AK, Ahmed S, Ferro-Luzzi Ames G (1989) Energy coupling in bacterial periplasmic transport systems. Studies in intact Escherichia coli cells. J Biol Chem 264: 2126-2133
    • (1989) J Biol Chem , vol.264 , pp. 2126-2133
    • Joshi, A.K.1    Ahmed, S.2    Ferro-Luzzi Ames, G.3
  • 21
    • 0029671447 scopus 로고    scopus 로고
    • 1-ATPase caused by the γ subunit generates a high affinity nucleotide binding site
    • 1-ATPase caused by the γ subunit generates a high affinity nucleotide binding site. J Biol Chem 271: 2433-2438
    • (1996) J Biol Chem , vol.271 , pp. 2433-2438
    • Kaibara, C.1    Matsui, T.2    Hisabori, T.3    Yoshida, M.4
  • 23
    • 28844477927 scopus 로고    scopus 로고
    • 1-ATPase binds ATP
    • 1-ATPase binds ATP. FEBS Lett 579: 6875-6878
    • (2005) FEBS Lett , vol.579 , pp. 6875-6878
    • Kato-Yamada, Y.1
  • 27
    • 0028829386 scopus 로고
    • ATP synthase from a cyanobacterial Synechocystis 6803 mutant containing the regulatory segment of the chloroplast γ subunit shows thiol modulation
    • Krenn BE, Aardewijn P, Van Walraven HS, Werner-Grune S, Strotmann H, Kraayenhof R (1995) ATP synthase from a cyanobacterial Synechocystis 6803 mutant containing the regulatory segment of the chloroplast γ subunit shows thiol modulation. Biochem Soc Trans 23: 757-760
    • (1995) Biochem Soc Trans , vol.23 , pp. 757-760
    • Krenn, B.E.1    Aardewijn, P.2    Van Walraven, H.S.3    Werner-Grune, S.4    Strotmann, H.5    Kraayenhof, R.6
  • 28
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt O, Grunert HP, Hahn U (1990) A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene 96: 125-128
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.P.2    Hahn, U.3
  • 35
    • 0021759513 scopus 로고
    • Role of a disulfide bond in the γ subunit in activation of the ATPase of chloroplast coupling factor 1
    • Nalin CM, McCarty RE (1984) Role of a disulfide bond in the γ subunit in activation of the ATPase of chloroplast coupling factor 1. J Biol Chem 259: 7275-7280
    • (1984) J Biol Chem , vol.259 , pp. 7275-7280
    • Nalin, C.M.1    McCarty, R.E.2
  • 36
    • 0015502107 scopus 로고
    • Partial resolution of the enzymes catalyzing photophosphorylation. XII. Purification and properties of an inhibitor isolated from chloroplast coupling factor 1
    • Nelson N, Nelson H, Racker E (1972) Partial resolution of the enzymes catalyzing photophosphorylation. XII. Purification and properties of an inhibitor isolated from chloroplast coupling factor 1. J Biol Chem 247: 7657-7662
    • (1972) J Biol Chem , vol.247 , pp. 7657-7662
    • Nelson, N.1    Nelson, H.2    Racker, E.3
  • 37
    • 0030818839 scopus 로고    scopus 로고
    • PcaK, a high-affinity permease for the aromatic compounds 4-hydroxybenzoate and protocatechuate from Pseudomonas putida
    • Nichols NN, Harwood CS (1997) PcaK, a high-affinity permease for the aromatic compounds 4-hydroxybenzoate and protocatechuate from Pseudomonas putida. J Bacteriol 179: 5056-5061
    • (1997) J Bacteriol , vol.179 , pp. 5056-5061
    • Nichols, N.N.1    Harwood, C.S.2
  • 41
    • 0037168499 scopus 로고    scopus 로고
    • The C-terminal domain of the ε subunit of the chloroplast ATP synthase is not required for ATP synthesis
    • Nowak KF, Tabidze V, McCarty RE (2002) The C-terminal domain of the ε subunit of the chloroplast ATP synthase is not required for ATP synthesis. Biochemistry 41: 15130-15134
    • (2002) Biochemistry , vol.41 , pp. 15130-15134
    • Nowak, K.F.1    Tabidze, V.2    McCarty, R.E.3
  • 43
    • 0034614475 scopus 로고    scopus 로고
    • Effect of electrostatic interactions on the binding of charged substrate to GroEL studied by highly sensitive fluorescence correlation spectroscopy
    • Pack CG, Aoki K, Taguchi H, Yoshida M, Kinjo M, Tamura M (2000) Effect of electrostatic interactions on the binding of charged substrate to GroEL studied by highly sensitive fluorescence correlation spectroscopy. Biochem Biophys Res Commun 267: 300-304
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 300-304
    • Pack, C.G.1    Aoki, K.2    Taguchi, H.3    Yoshida, M.4    Kinjo, M.5    Tamura, M.6
  • 44
    • 0033168398 scopus 로고    scopus 로고
    • Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy
    • Pack CG, Nishimura G, Tamura M, Aoki K, Taguchi H, Yoshida M, Kinjo M (1999) Analysis of interaction between chaperonin GroEL and its substrate using fluorescence correlation spectroscopy. Cytometry 36: 247-253
    • (1999) Cytometry , vol.36 , pp. 247-253
    • Pack, C.G.1    Nishimura, G.2    Tamura, M.3    Aoki, K.4    Taguchi, H.5    Yoshida, M.6    Kinjo, M.7
  • 46
    • 0021770639 scopus 로고
    • Preparation of the ε subunit and ε subunit-deficient chloroplast coupling factor 1 in reconstitutively active forms
    • Richter ML, Patrie WJ, McCarty RE (1984) Preparation of the ε subunit and ε subunit-deficient chloroplast coupling factor 1 in reconstitutively active forms. J Biol Chem 259: 7371-7373
    • (1984) J Biol Chem , vol.259 , pp. 7371-7373
    • Richter, M.L.1    Patrie, W.J.2    McCarty, R.E.3
  • 47
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • Sabbert D, Engelbrecht S, Junge W (1996) Intersubunit rotation in active F-ATPase. Nature 381: 623-625
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 48
    • 0033201448 scopus 로고    scopus 로고
    • o complex of Escherichia coli. Cross-linking studies show the same structure in situ as when isolated
    • o complex of Escherichia coli. Cross-linking studies show the same structure in situ as when isolated. J Biol Chem 274: 28351-28355
    • (1999) J Biol Chem , vol.274 , pp. 28351-28355
    • Schulenberg, B.1    Capaldi, R.A.2
  • 50
    • 0025338413 scopus 로고
    • The proton-translocating ATPase of Escherichia coli
    • Senior AE (1990) The proton-translocating ATPase of Escherichia coli. Annu Rev Biophys Biophys Chem 19: 7-41
    • (1990) Annu Rev Biophys Biophys Chem , vol.19 , pp. 7-41
    • Senior, A.E.1
  • 54
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D, Leslie AG, Walker JE (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.2    Walker, J.E.3
  • 55
    • 0345306622 scopus 로고    scopus 로고
    • 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ε subunit in response to proton motive force and ADP/ATP balance
    • 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ε subunit in response to proton motive force and ADP/ATP balance. J Biol Chem 278: 46840-46846
    • (2003) J Biol Chem , vol.278 , pp. 46840-46846
    • Suzuki, T.1    Murakami, T.2    Iino, R.3    Suzuki, J.4    Ono, S.5    Shirakihara, Y.6    Yoshida, M.7
  • 56
    • 0037066772 scopus 로고    scopus 로고
    • o of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring
    • o of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring. J Biol Chem 277: 13281-13285
    • (2002) J Biol Chem , vol.277 , pp. 13281-13285
    • Suzuki, T.1    Ueno, H.2    Mitome, N.3    Suzuki, J.4    Yoshida, M.5
  • 59
    • 0020482467 scopus 로고
    • Kinetic mechanism of mitochondrial adenosine triphosphatase. ADP-specific inhibition as revealed by the steady-state kinetics
    • Vasilyeva EA, Minkov IB, Fitin AF, Vinogradov AD (1982) Kinetic mechanism of mitochondrial adenosine triphosphatase. ADP-specific inhibition as revealed by the steady-state kinetics. Biochem J 202: 9-14
    • (1982) Biochem J , vol.202 , pp. 9-14
    • Vasilyeva, E.A.1    Minkov, I.B.2    Fitin, A.F.3    Vinogradov, A.D.4
  • 61
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps. Cell 93: 1117-1124
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita Jr., K.3    Yoshida, M.4
  • 64
    • 0018668935 scopus 로고
    • Subunit structure of adenosine triphosphatase. Comparison of the structure in thermophilic bacterium PS3 with those in mitochondria, chloroplasts, and Escherichia coli
    • Yoshida M, Sone N, Hirata H, Kagawa Y, Ui N (1979) Subunit structure of adenosine triphosphatase. Comparison of the structure in thermophilic bacterium PS3 with those in mitochondria, chloroplasts, and Escherichia coli. J Biol Chem 254: 9525-9533
    • (1979) J Biol Chem , vol.254 , pp. 9525-9533
    • Yoshida, M.1    Sone, N.2    Hirata, H.3    Kagawa, Y.4    Ui, N.5
  • 65
    • 0024285004 scopus 로고
    • Relationship of tightly bound ADP and ATP to control and catalysis by chloroplast ATP synthase
    • Zhou JM, Xue ZX, Du ZY, Melese T, Boyer PD (1988) Relationship of tightly bound ADP and ATP to control and catalysis by chloroplast ATP synthase. Biochemistry 27: 5129-5135
    • (1988) Biochemistry , vol.27 , pp. 5129-5135
    • Zhou, J.M.1    Xue, Z.X.2    Du, Z.Y.3    Melese, T.4    Boyer, P.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.