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Volumn 288, Issue 18, 2013, Pages 13156-13163

Light- and metabolism-related regulation of the chloroplast ATP synthase has distinct mechanisms and functions

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC AMINO ACIDS; ALLOSTERIC EFFECTORS; ARABIDOPSIS THALIANA; COVALENT MODIFICATIONS; DIFFERENT MECHANISMS; ELECTRON TRANSFER; METABOLIC CHANGES; PHYSIOLOGICAL CONDITION;

EID: 84877100639     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.453225     Document Type: Article
Times cited : (42)

References (42)
  • 2
    • 0141757507 scopus 로고    scopus 로고
    • Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase
    • DOI 10.1016/j.jmb.2003.08.046
    • Seelert, H., Dencher, N. A., and Müller, D. J. (2003) Fourteen protomers compose the oligomer III of the proton-rotor in spinach chloroplast ATP synthase. J. Mol. Biol. 333, 337-344 (Pubitemid 37188576)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.2 , pp. 337-344
    • Seelert, H.1    Dencher, N.A.2    Muller, D.J.3
  • 3
    • 84863474422 scopus 로고    scopus 로고
    • Mitochondrial ATP synthase: Architecture, function and pathology
    • Jonckheere, A. I., Smeitink, J. A., and Rodenburg, R. J. (2012) Mitochondrial ATP synthase: architecture, function and pathology. J. Inherit. Metab. Dis. 35, 211-225
    • (2012) J. Inherit. Metab. Dis. , vol.35 , pp. 211-225
    • Jonckheere, A.I.1    Smeitink, J.A.2    Rodenburg, R.J.3
  • 6
    • 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
  • 9
    • 1642273978 scopus 로고    scopus 로고
    • γ-ε Interactions regulate the chloroplast ATP synthase
    • Richter, M. L. (2004) γ-ε Interactions regulate the chloroplast ATP synthase. Photosynth. Res. 79, 319-329
    • (2004) Photosynth. Res. , vol.79 , pp. 319-329
    • Richter, M.L.1
  • 10
    • 0034466466 scopus 로고    scopus 로고
    • Regulation of proton flow and ATP synthesis in chloroplasts
    • DOI 10.1023/A:1005669008974
    • Evron, Y., Johnson, E. A., and McCarty, R. E. (2000) Regulation of proton flow and ATP synthesis in chloroplasts. J. Bioenerg. Biomembr. 32, 501-506 (Pubitemid 32204248)
    • (2000) Journal of Bioenergetics and Biomembranes , vol.32 , Issue.5 , pp. 501-506
    • Evron, Y.1    Johnson, E.A.2    Mccarty, R.E.3
  • 12
    • 0037716146 scopus 로고    scopus 로고
    • Molecular evolution of the modulator of chloroplast ATP synthase: Origin of the conformational change dependent regulation
    • DOI 10.1016/S0014-5793(03)00395-8
    • Hisabori, T., Ueoka-Nakanishi, H., Konno, H., and Koyama, F. (2003) Molecular evolution of the modulator of chloroplast ATP synthase: origin of the conformational change-dependent regulation. FEBS Lett. 545, 71-75 (Pubitemid 36629638)
    • (2003) FEBS Letters , vol.545 , Issue.1 , pp. 71-75
    • Hisabori, T.1    Ueoka-Nakanishi, H.2    Konno, H.3    Koyama, F.4
  • 13
    • 0000854423 scopus 로고
    • Modulation of coupling factor ATPase activity in intact chloroplasts: Reversal of thiol modulation in the dark
    • Mills, J. D., and Mitchell, P. (1982) Modulation of coupling factor ATPase activity in intact chloroplasts: reversal of thiol modulation in the dark. Biochim. Biophys. Acta 679, 75-83
    • (1982) Biochim. Biophys. Acta , vol.679 , pp. 75-83
    • Mills, J.D.1    Mitchell, P.2
  • 15
    • 58149369620 scopus 로고
    • Activation of the chloroplast ATPase measured by the electrochromic change in leaves of intact plants
    • Kramer, D. M., and Crofts, A. R. (1989) Activation of the chloroplast ATPase measured by the electrochromic change in leaves of intact plants. Biochim. Biophys. Acta 976, 28-41
    • (1989) Biochim. Biophys. Acta , vol.976 , pp. 28-41
    • Kramer, D.M.1    Crofts, A.R.2
  • 16
    • 84859762682 scopus 로고    scopus 로고
    • Thiol modulation of the chloroplast ATP synthase is dependent on the energization of thylakoid membranes
    • Konno, H., Nakane, T., Yoshida, M., Ueoka-Nakanishi, H., Hara, S., and Hisabori, T. (2012) Thiol modulation of the chloroplast ATP synthase is dependent on the energization of thylakoid membranes. Plant Cell Physiol. 4, 626-634
    • (2012) Plant Cell Physiol. , vol.4 , pp. 626-634
    • Konno, H.1    Nakane, T.2    Yoshida, M.3    Ueoka-Nakanishi, H.4    Hara, S.5    Hisabori, T.6
  • 18
    • 37549058830 scopus 로고    scopus 로고
    • A point mutation in atpC1 raises the redox potential of the Arabidopsis chloroplast ATP synthase γ subunit regulatory disulfide above the range of thioredoxin modulation
    • Wu, G., Ortiz-Flores, G., Ortiz-Lopez, A., and Ort, D. R. (2007) A point mutation in atpC1 raises the redox potential of the Arabidopsis chloroplast ATP synthase γ subunit regulatory disulfide above the range of thioredoxin modulation. J. Biol. Chem. 282, 36782-36789
    • (2007) J. Biol. Chem. , vol.282 , pp. 36782-36789
    • Wu, G.1    Ortiz-Flores, G.2    Ortiz-Lopez, A.3    Ort, D.R.4
  • 19
    • 48349125619 scopus 로고    scopus 로고
    • Mutation in the cysteine bridge domain of the γ subunit affects light regulation of the ATP synthase but not photosynthesis or growth in Arabidopsis
    • Wu, G., and Ort, D. R. (2008) Mutation in the cysteine bridge domain of the γ subunit affects light regulation of the ATP synthase but not photosynthesis or growth in Arabidopsis. Photosynth Res. 97, 185-193
    • (2008) Photosynth Res. , vol.97 , pp. 185-193
    • Wu, G.1    Ort, D.R.2
  • 23
    • 77950366997 scopus 로고    scopus 로고
    • An Arabidopsis mutant with high cyclic electron flow around photosystem I (hcef) involving the NADPH dehydrogenase complex
    • Livingston, A. K., Cruz, J. A., Kohzuma, K., Dhingra, A., and Kramer, D. M. (2010) An Arabidopsis mutant with high cyclic electron flow around photosystem I (hcef) involving the NADPH dehydrogenase complex. Plant Cell 22, 221-233
    • (2010) Plant Cell , vol.22 , pp. 221-233
    • Livingston, A.K.1    Cruz, J.A.2    Kohzuma, K.3    Dhingra, A.4    Kramer, D.M.5
  • 24
    • 78049275413 scopus 로고    scopus 로고
    • Regulation of cyclic electron flow in C plants: Differential effects of limiting photosynthesis at ribulose-1,5-bisphosphate carboxylase/oxygenase and glyceraldehyde-3-phosphate dehydrogenase
    • Livingston, A. K., Kanazawa, A., Cruz, J. A., and Kramer, D. M. (2010) Regulation of cyclic electron flow in C plants: differential effects of limiting photosynthesis at ribulose-1,5-bisphosphate carboxylase/oxygenase and glyceraldehyde-3-phosphate dehydrogenase. Plant Cell Environ. 33, 1779-1788
    • (2010) Plant Cell Environ. , vol.33 , pp. 1779-1788
    • Livingston, A.K.1    Kanazawa, A.2    Cruz, J.A.3    Kramer, D.M.4
  • 25
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of adult Arabidopsis thaliana plants by vacuum infiltration
    • Clough, S. J., and Bent, A. F. (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of adult Arabidopsis thaliana plants by vacuum infiltration. Plant J. 16, 735-743
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 26
    • 0347723943 scopus 로고    scopus 로고
    • Inactivation of the Chloroplast ATP Synthase γ Subunit Results in High Non-photochemical Fluorescence Quenching and Altered Nuclear Gene Expression in Arabidopsis thaliana
    • DOI 10.1074/jbc.M308435200
    • Dal Bosco, C., Lezhneva, L., Biehl, A., Leister, D., Strotmann, H., Wanner, G., and Meurer, J. (2004) Inactivation of the chloroplast ATP synthase γ subunit results in high nonphotochemical fluorescence quenching and altered nuclear gene expression in Arabidopsis thaliana. J. Biol. Chem. 279, 1060-1069 (Pubitemid 38082627)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 1060-1069
    • Dal, B.C.1    Lezhneva, L.2    Bieh, A.3    Leister, D.4    Strotmann, H.5    Wanner, G.6    Meurer, J.7
  • 27
    • 0036789921 scopus 로고    scopus 로고
    • In vivo modulation of nonphotochemical exciton quenching (NPQ) by regulation of the chloroplast ATP synthase
    • Kanazawa, A., and Kramer, D. M. (2002) In vivo modulation of nonphotochemical exciton quenching (NPQ) by regulation of the chloroplast ATP synthase. Proc. Natl. Acad. Sci. U.S.A. 99, 12789-12794
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12789-12794
    • Kanazawa, A.1    Kramer, D.M.2
  • 28
    • 13944268323 scopus 로고    scopus 로고
    • Plasticity in light reactions of photosynthesis for energy production and photoprotection
    • DOI 10.1093/jxb/eri022, Light Stress in Plants: Mechanisms and Interactions
    • Cruz, J. A., Avenson, T. J., Kanazawa, A., Takizawa, K., Edwards, G. E., and Kramer, D. M. (2005) Plasticity in light reactions of photosynthesis for energy production and photoprotection. J. Exp. Bot. 56, 395-406 (Pubitemid 40263287)
    • (2005) Journal of Experimental Botany , vol.56 , Issue.411 , pp. 395-406
    • Cruz, J.A.1    Avenson, T.J.2    Kanazawa, A.3    Takizawa, K.4    Edwards, G.E.5    Kramer, D.M.6
  • 31
    • 84877120994 scopus 로고    scopus 로고
    • The chloroplast ATP synthase features the characteristic redox regulation machinery
    • in press
    • Hisabori, T., Sunamura, E. I., Kim, Y., and Konno, H. (2013) The chloroplast ATP synthase features the characteristic redox regulation machinery. Antioxid. Redox Signal., in press
    • (2013) Antioxid. Redox Signal.
    • Hisabori, T.1    Sunamura, E.I.2    Kim, Y.3    Konno, H.4
  • 32
    • 34547451124 scopus 로고    scopus 로고
    • Determining the limitations and regulation of photosynthetic energy transduction in leaves
    • DOI 10.1111/j.1365-3040.2007.01680.x
    • Baker, N. R., Harbinson, J., and Kramer, D. M. (2007) Determining the limitations and regulation of photosynthetic energy transduction in leaves. Plant Cell Environ. 30, 1107-1125 (Pubitemid 47174272)
    • (2007) Plant, Cell and Environment , vol.30 , Issue.9 , pp. 1107-1125
    • Baker, N.R.1    Harbinson, J.2    Kramer, D.M.3
  • 33
    • 0001078981 scopus 로고
    • Regulation of coupling factor in field-grown sunflower: A Redox model relating coupling factor activity to the activities of other thioredoxin-dependent chloroplast enzymes
    • Kramer, D. M., Wise, R. R., Frederick, J. R., Alm, D. M., Hesketh, J. D., Ort, D. R., and Crofts, A. R. (1990) Regulation of coupling factor in field-grown sunflower: A Redox model relating coupling factor activity to the activities of other thioredoxin-dependent chloroplast enzymes. Photosynth. Res. 26, 213-222
    • (1990) Photosynth. Res. , vol.26 , pp. 213-222
    • Kramer, D.M.1    Wise, R.R.2    Frederick, J.R.3    Alm, D.M.4    Hesketh, J.D.5    Ort, D.R.6    Crofts, A.R.7
  • 34
    • 34848863975 scopus 로고    scopus 로고
    • The thylakoid proton motive force in vivo. Quantitative, non-invasive probes, energetics, and regulatory consequences of light-induced pmf
    • DOI 10.1016/j.bbabio.2007.07.006, PII S0005272807001557
    • Takizawa, K., Cruz, J. A., Kanazawa, A., and Kramer, D. M. (2007) The thylakoid proton motive force in vivo: quantitative, noninvasive probes, energetics, and regulatory consequences of light-induced pmf. Biochim. Biophys. Acta 1767, 1233-1244 (Pubitemid 47498308)
    • (2007) Biochimica et Biophysica Acta - Bioenergetics , vol.1767 , Issue.10 , pp. 1233-1244
    • Takizawa, K.1    Cruz, J.A.2    Kanazawa, A.3    Kramer, D.M.4
  • 35
    • 0028110654 scopus 로고
    • Mutants of chloroplast coupling factor reduction in Arabidopsis
    • Gabrys, H., Kramer, D. M., Crofts, A. R., and Ort, D. R. (1994) Mutants of chloroplast coupling factor reduction in Arabidopsis. Plant Physiol. 104, 769-776
    • (1994) Plant Physiol. , vol.104 , pp. 769-776
    • Gabrys, H.1    Kramer, D.M.2    Crofts, A.R.3    Ort, D.R.4
  • 37
    • 0000256686 scopus 로고
    • Influence of the redox state and the activation of the chloroplast ATP synthase on proton transport-coupled ATP synthesis hydrolysis
    • Junesch, U., and Gräber, P. (1987) Influence of the redox state and the activation of the chloroplast ATP synthase on proton transport-coupled ATP synthesis hydrolysis. Biochim. Biophys. Acta 893, 275-288
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 275-288
    • Junesch, U.1    Gräber, P.2
  • 38
    • 0001236117 scopus 로고
    • Stromal phosphate concentration is low during feedback limited photosynthesis
    • Sharkey, T. D., and Vanderveer, P. J. (1989) Stromal phosphate concentration is low during feedback limited photosynthesis. Plant Physiol. 91, 679-684
    • (1989) Plant Physiol. , vol.91 , pp. 679-684
    • Sharkey, T.D.1    Vanderveer, P.J.2
  • 39
    • 0000103630 scopus 로고
    • Low oxygen inhibition of photosynthesis is caused by inhibition of starch synthesis
    • Sharkey, T. D., and Vassey, T. L. (1989) Low oxygen inhibition of photosynthesis is caused by inhibition of starch synthesis. Plant Physiol. 90, 385-387
    • (1989) Plant Physiol. , vol.90 , pp. 385-387
    • Sharkey, T.D.1    Vassey, T.L.2
  • 41
    • 66649127498 scopus 로고    scopus 로고
    • Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks
    • Reiland, S., Messerli, G., Baerenfaller, K., Gerrits, B., Endler, A., Grossmann, J., Gruissem, W., and Baginsky, S. (2009) Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks. Plant Physiol. 150, 889-903
    • (2009) Plant Physiol. , vol.150 , pp. 889-903
    • Reiland, S.1    Messerli, G.2    Baerenfaller, K.3    Gerrits, B.4    Endler, A.5    Grossmann, J.6    Gruissem, W.7    Baginsky, S.8
  • 42
    • 33747331173 scopus 로고    scopus 로고
    • Multiple phosphorylation sites in the β subunit of thylakoid ATP synthase
    • del Riego, G., Casano, L. M., Martín, M., and Sabater, B. (2006) Multiple phosphorylation sites in the β subunit of thylakoid ATP synthase. Photosynth. Res. 89, 11-18
    • (2006) Photosynth. Res. , vol.89 , pp. 11-18
    • Del Riego, G.1    Casano, L.M.2    Martín, M.3    Sabater, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.