메뉴 건너뛰기




Volumn 318, Issue 1, 2004, Pages 17-24

Significance of the ε subunit in the thiol modulation of chloroplast ATP synthase

Author keywords

Subunit; Subunit; Chloroplast ATP synthase; FoF1; Redox regulation

Indexed keywords

PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; THIOL; ADENOSINE TRIPHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTON; RECOMBINANT PROTEIN; THIOL DERIVATIVE;

EID: 1942504227     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.03.179     Document Type: Article
Times cited : (12)

References (52)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase - A splendid molecular machine
    • Boyer P.D. The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66:1997;717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 2
    • 0025338413 scopus 로고
    • The proton-translocating ATPase of Escherichia coli
    • Senior A.E. The proton-translocating ATPase of Escherichia coli. Annu. Rev. Biophys. Biophys. Chem. 19:1990;7-41.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 7-41
    • Senior, A.E.1
  • 4
    • 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. Subunit structure of adenosine triphosphatase. Comparison of the structure in thermophilic bacterium PS3 with those in mitochondria, chloroplasts, and Escherichia coli. J. Biol. Chem. 254:1979;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
  • 5
    • 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. 271:1996;2433-2438.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2433-2438
    • Kaibara, C.1    Matsui, T.2    Hisabori, T.3    Yoshida, M.4
  • 8
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D., Leslie A.G., Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science. 286:1999;1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 10
    • 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 R.H. The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10. Proc. Natl. Acad. Sci. USA. 98:2001;4966-4971.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4966-4971
    • Jiang, W.1    Hermolin, J.2    Fillingame, R.H.3
  • 16
    • 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. 463:1999;35-38.
    • (1999) FEBS Lett. , vol.463 , pp. 35-38
    • Hisabori, T.1    Kondoh, A.2    Yoshida, M.3
  • 17
    • 0037109039 scopus 로고    scopus 로고
    • Subunit rotation of ATP synthase embedded in membranes: α or β subunit rotation relative to the c subunit ring
    • Nishio K., Iwamoto-Kihara A., Yamamoto A., Wada Y., Futai M. Subunit rotation of ATP synthase embedded in membranes: α or β subunit rotation relative to the c subunit ring. Proc. Natl. Acad. Sci. USA. 99:2002;13448-13452.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13448-13452
    • Nishio, K.1    Iwamoto-Kihara, A.2    Yamamoto, A.3    Wada, Y.4    Futai, M.5
  • 18
    • 49149147054 scopus 로고
    • Modulation of coupling factor ATPase activity in intact chloroplasts, the role of the thioredoxin system
    • Mills J.D., Mitchell P., Schürmann P. Modulation of coupling factor ATPase activity in intact chloroplasts, the role of the thioredoxin system. FEBS Lett. 112:1980;173-177.
    • (1980) FEBS Lett. , vol.112 , pp. 173-177
    • Mills, J.D.1    Mitchell, P.2    Schürmann, P.3
  • 19
    • 0021759513 scopus 로고
    • Role of a disulfide bond in the γ subunit in activation of the ATPase of chloroplast coupling factor 1
    • Nalin C.M., McCarty R.E. Role of a disulfide bond in the γ subunit in activation of the ATPase of chloroplast coupling factor 1. J. Biol. Chem. 259:1984;7275-7280.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7275-7280
    • Nalin, C.M.1    McCarty, R.E.2
  • 20
    • 0021759532 scopus 로고
    • Role of the γ subunit of chloroplast coupling factor 1 in the light-dependent activation of photophosphorylation and ATPase activity by dithiothreitol
    • Ketcham S.R., Davenport J.W., Warncke K., McCarty R.E. Role of the γ subunit of chloroplast coupling factor 1 in the light-dependent activation of photophosphorylation and ATPase activity by dithiothreitol. J. Biol. Chem. 259:1984;7286-7293.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7286-7293
    • Ketcham, S.R.1    Davenport, J.W.2    Warncke, K.3    McCarty, R.E.4
  • 23
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxins: Structure and function in plant cells
    • Jacquot J.P., Lancelin J.M., Meyer Y. Thioredoxins: structure and function in plant cells. New Phytol. 136:1997;543-570.
    • (1997) New Phytol. , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 24
    • 0034723368 scopus 로고    scopus 로고
    • Redox signaling in chloroplasts: Cleavage of disulfides by an iron-sulfur cluster
    • Dai S., Schwendtmayer C., Schürmann P., Ramaswamy S., Eklund H. Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster. Science. 287:2000;655-658.
    • (2000) Science , vol.287 , pp. 655-658
    • Dai, S.1    Schwendtmayer, C.2    Schürmann, P.3    Ramaswamy, S.4    Eklund, H.5
  • 25
    • 0024282473 scopus 로고
    • The γ-subunit of ATP synthase from spinach chloroplasts. Primary structure deduced from the cloned cDNA sequence
    • Miki J., Maeda M., Mukohata Y., Futai M. The γ-subunit of ATP synthase from spinach chloroplasts. Primary structure deduced from the cloned cDNA sequence. FEBS Lett. 232:1988;221-226.
    • (1988) FEBS Lett. , vol.232 , pp. 221-226
    • Miki, J.1    Maeda, M.2    Mukohata, Y.3    Futai, M.4
  • 26
    • 0030917877 scopus 로고    scopus 로고
    • The ATP synthase γ subunit provides the primary site of activation of the chloroplast enzyme: Experiments with a chloroplast-like Synechocystis 6803 mutant
    • Krenn B.E., Strotmann H., Van Walraven H.S., Scholts M.J., Kraayenhof R. The ATP synthase γ subunit provides the primary site of activation of the chloroplast enzyme: experiments with a chloroplast-like Synechocystis 6803 mutant. Biochem. J. 323:1997;841-845.
    • (1997) Biochem. J. , vol.323 , pp. 841-845
    • Krenn, B.E.1    Strotmann, H.2    Van Walraven, H.S.3    Scholts, M.J.4    Kraayenhof, R.5
  • 28
    • 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. 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. 273:1998;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
  • 31
    • 0033966205 scopus 로고    scopus 로고
    • 1 β or α and β subunits reveal the essential role of the α subunit in ATP synthesis and tentoxin sensitivity
    • 1 β or α and β subunits reveal the essential role of the α subunit in ATP synthesis and tentoxin sensitivity. J. Biol. Chem. 275:2000;906-912.
    • (2000) J. Biol. Chem. , vol.275 , pp. 906-912
    • Tucker, W.C.1    Du, Z.2    Hein, R.3    Richter, M.L.4    Gromet-Elhanan, Z.5
  • 32
    • 0034849040 scopus 로고    scopus 로고
    • 1-ATPases. Demonstration of different structural requirements for stimulation and inhibition by tentoxin
    • 1-ATPases. Demonstration of different structural requirements for stimulation and inhibition by tentoxin. Eur. J. Biochem. 268:2001;2179-2186.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2179-2186
    • Tucker, W.C.1    Du, Z.2    Gromet-Elhanan, Z.3    Richter, M.L.4
  • 35
    • 0017351393 scopus 로고
    • Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coli
    • Smith J.B., Sternweis P.C. Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coli. Biochemistry. 16:1977;306-311.
    • (1977) Biochemistry , vol.16 , pp. 306-311
    • Smith, J.B.1    Sternweis, P.C.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. Partial resolution of the enzymes catalyzing photophosphorylation. XII. Purification and properties of an inhibitor isolated from chloroplast coupling factor 1. J. Biol. Chem. 247:1972;7657-7662.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7657-7662
    • Nelson, N.1    Nelson, H.2    Racker, E.3
  • 38
    • 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. 277:2002;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
  • 39
    • 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., Simoni R.D. In vivo evidence for the role of the ε subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli. J. Bacteriol. 160:1984;1055-1060.
    • (1984) J. Bacteriol. , vol.160 , pp. 1055-1060
    • Klionsky, D.J.1    Brusilow, W.S.2    Simoni, R.D.3
  • 40
    • 0028067602 scopus 로고
    • o ATP synthase. Effect of position 61 substitutions in helix-2 on function of Asp24 in helix-1
    • o ATP synthase. Effect of position 61 substitutions in helix-2 on function of Asp24 in helix-1. J. Biol. Chem. 269:1994;5473-5479.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5473-5479
    • Zhang, Y.1    Fillingame, R.H.2
  • 41
    • 0033166052 scopus 로고    scopus 로고
    • Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the γ-subunit of chloroplast ATP synthase
    • Stumpp M.T., Motohashi K., Hisabori T. Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the γ-subunit of chloroplast ATP synthase. Biochem. J. 341:1999;157-163.
    • (1999) Biochem. J. , vol.341 , pp. 157-163
    • Stumpp, M.T.1    Motohashi, K.2    Hisabori, T.3
  • 42
    • 0029175508 scopus 로고
    • Ferredoxin: Thioredoxin system
    • Schürmann P. Ferredoxin: thioredoxin system. Methods Enzymol. 252:1995;274-283.
    • (1995) Methods Enzymol. , vol.252 , pp. 274-283
    • Schürmann, P.1
  • 43
    • 0030671552 scopus 로고    scopus 로고
    • Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
    • Kobayashi T., Kishigami S., Sone M., Inokuchi H., Mogi T., Ito K. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells. Proc. Natl. Acad. Sci. USA. 94:1997;11857-11862.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11857-11862
    • Kobayashi, T.1    Kishigami, S.2    Sone, M.3    Inokuchi, H.4    Mogi, T.5    Ito, K.6
  • 44
    • 0018368188 scopus 로고
    • Preparation and properties of complex V
    • see also pp. 819-321
    • Stiggall D.L., Galante Y.M., Hatefi Y. Preparation and properties of complex V. Methods Enzymol. 55:1979;308-315. see also pp. 819-321.
    • (1979) Methods Enzymol. , vol.55 , pp. 308-315
    • Stiggall, D.L.1    Galante, Y.M.2    Hatefi, Y.3
  • 45
    • 0029671418 scopus 로고    scopus 로고
    • 1 ATP synthase from thermophilic Bacillus PS3 reconstituted into liposomes with bacteriorhodopsin. 1. Factors defining the optimal reconstitution of ATP synthases with bacteriorhodopsin
    • 1 ATP synthase from thermophilic Bacillus PS3 reconstituted into liposomes with bacteriorhodopsin. 1. Factors defining the optimal reconstitution of ATP synthases with bacteriorhodopsin. Eur. J. Biochem. 235:1996;769-778.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 769-778
    • Pitard, B.1    Richard, P.2    Dunach, M.3    Girault, G.4    Rigaud, J.L.5
  • 47
    • 0023645804 scopus 로고
    • Energy-dependent changes in the conformation of the ε subunit of the chloroplast ATP synthase
    • Richter M.L., McCarty R.E. Energy-dependent changes in the conformation of the ε subunit of the chloroplast ATP synthase. J. Biol. Chem. 262:1987;15037-15040.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15037-15040
    • Richter, M.L.1    McCarty, R.E.2
  • 49
    • 0037133033 scopus 로고    scopus 로고
    • The carboxyl terminus of the ε subunit of the chloroplast ATP synthase is exposed during illumination
    • Johnson E.A., McCarty R.E. The carboxyl terminus of the ε subunit of the chloroplast ATP synthase is exposed during illumination. Biochemistry. 41:2002;2446-2451.
    • (2002) Biochemistry , vol.41 , pp. 2446-2451
    • Johnson, E.A.1    McCarty, R.E.2
  • 50
    • 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. 278:2003;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
  • 51
    • 0021770639 scopus 로고
    • Preparation of the ε subunit and ε subunit-deficient chloroplast coupling factor 1 in reconstitutively active forms
    • Richter M.L., Patrie W.J., McCarty R.E. Preparation of the ε subunit and ε subunit-deficient chloroplast coupling factor 1 in reconstitutively active forms. J. Biol. Chem. 259:1984;7371-7373.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7371-7373
    • Richter, M.L.1    Patrie, W.J.2    McCarty, R.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.