메뉴 건너뛰기




Volumn 100, Issue 4, 1997, Pages 863-868

Redox signalling and the structural basis of regulation of photosynthesis by protein phosphorylation

Author keywords

Chloroplast light harvesting complex; Molecular recognition; Photosynthesis; Photosystem I; Photosystem II; Protein kinase phosphatase; Redox sensor response regulator; Redox signalling

Indexed keywords


EID: 0030869955     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-3054.1997.1000412.x     Document Type: Article
Times cited : (58)

References (40)
  • 1
    • 0000057543 scopus 로고
    • Redox conditions specify the proteins synthesised by isolated chloroplasts and mitochondria
    • Allen, C. A, Håkansson, G. & Allen, J. F. 1995. Redox conditions specify the proteins synthesised by isolated chloroplasts and mitochondria. - Redox Rep. 1: 119-123.
    • (1995) Redox Rep. , vol.1 , pp. 119-123
    • Allen, C.A.1    Håkansson, G.2    Allen, J.F.3
  • 2
    • 0026556851 scopus 로고
    • Protein phosphorylation in regulation of photosynthesis
    • Allen, J. F. 1992a. Protein phosphorylation in regulation of photosynthesis. - Biochim. Biophys. Acta 1098: 275-335.
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 3
    • 0026513229 scopus 로고
    • How does protein phosphorylation regulate photosynthesis?
    • _ 1992b. How does protein phosphorylation regulate photosynthesis? - Trends Biochem. Sci. 17: 12-17.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 12-17
  • 4
    • 0027363665 scopus 로고
    • Redox control of transcription: Sensors, response regulators, activators and repressors
    • _ 1993a. Redox control of transcription: Sensors, response regulators, activators and repressors. - FEBS Lett, 332: 203-207.
    • (1993) FEBS Lett , vol.332 , pp. 203-207
  • 5
    • 0027724036 scopus 로고
    • Control of gene expression by redox potential and the requirement for chloroplast and mitochondrial genomes
    • _ 1993b. Control of gene expression by redox potential and the requirement for chloroplast and mitochondrial genomes - J. Theor. Biol. 165: 609-631.
    • (1993) J. Theor. Biol. , vol.165 , pp. 609-631
  • 6
    • 84989674556 scopus 로고
    • Thylakoid protein phosphorylation, state 1-state 2 transitions, and photosystem stoichiometry adjustment: Redox control at multiple levels of gene expression
    • _ 1995. Thylakoid protein phosphorylation, state 1-state 2 transitions, and photosystem stoichiometry adjustment: Redox control at multiple levels of gene expression - Physiol. Plant. 93: 196-205.
    • (1995) Physiol. Plant. , vol.93 , pp. 196-205
  • 7
    • 0030596417 scopus 로고    scopus 로고
    • Separate sexes and the mitochondrial theory of ageing
    • _ 1996. Separate sexes and the mitochondrial theory of ageing - J. Theor. Biol. 180: 135-140.
    • (1996) J. Theor. Biol. , vol.180 , pp. 135-140
  • 8
    • 0029933923 scopus 로고    scopus 로고
    • Free-radical-induced mutation vs redox regulation: Costs and benefits of genes in organelles
    • _ & Raven, J. A. 1996. Free-radical-induced mutation vs redox regulation: Costs and benefits of genes in organelles. - J. Mol. Evol. 42: 482-492.
    • (1996) J. Mol. Evol. , vol.42 , pp. 482-492
    • Raven, J.A.1
  • 9
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems
    • _, Bennett, J., Steinback, K. E. & Arntzen, C. J. 1981. Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. - Nature 291: 25-29.
    • (1981) Nature , vol.291 , pp. 25-29
    • Bennett, J.1    Steinback, K.E.2    Arntzen, C.J.3
  • 10
    • 0000688722 scopus 로고
    • State transitions, photosystem stoichiometry adjustment and non-photochemical quenching in cyanobacterial cells acclimated to light absorbed by photosystem I or photosystem II
    • _, Mullineaux, C. W., Sanders, C. E. & Melis, A. 1989. State transitions, photosystem stoichiometry adjustment and non-photochemical quenching in cyanobacterial cells acclimated to light absorbed by photosystem I or photosystem II. - Photosynth. Res. 22: 157-166.
    • (1989) Photosynth. Res. , vol.22 , pp. 157-166
    • Mullineaux, C.W.1    Sanders, C.E.2    Melis, A.3
  • 11
    • 0007367630 scopus 로고
    • Differential phosphorylation of the light harvesting chlorophyll-protein complex in appressed and non-appressed regions of the thylakoid membrane
    • Andersson, B., Åkerlund, H.-E., Jergil, B. & Larsson, C. 1982. Differential phosphorylation of the light harvesting chlorophyll-protein complex in appressed and non-appressed regions of the thylakoid membrane. - FEBS Lett. 149: 181-185.
    • (1982) FEBS Lett. , vol.149 , pp. 181-185
    • Andersson, B.1    Åkerlund, H.-E.2    Jergil, B.3    Larsson, C.4
  • 12
  • 13
    • 0026033985 scopus 로고
    • Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP
    • Barford, D., Hu, S.-H. & Johnson, L. N. 1991. Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP. - J. Mol. Biol. 218: 233-260.
    • (1991) J. Mol. Biol. , vol.218 , pp. 233-260
    • Barford, D.1    Hu, S.-H.2    Johnson, L.N.3
  • 14
    • 0030870674 scopus 로고    scopus 로고
    • Novel aspects of chlorophyll a/b-binding proteins
    • Bassi, R., Sandonà, D. & Croce, R. 1997. Novel aspects of chlorophyll a/b-binding proteins. - Physiol. Plant. 100: 769-779.
    • (1997) Physiol. Plant. , vol.100 , pp. 769-779
    • Bassi, R.1    Sandonà, D.2    Croce, R.3
  • 15
    • 0001138725 scopus 로고
    • Protein phosphorylation in green plant chloroplasts
    • Bennett, J. 1991. Protein phosphorylation in green plant chloroplasts. - Annu. Rev. Plant Physiol. Plant Mol. Biol. 42: 281-331.
    • (1991) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.42 , pp. 281-331
    • Bennett, J.1
  • 16
    • 0014646190 scopus 로고
    • Fluorescence and oxygen evolution from Chlorella pyrenoidosa
    • Bonaventura, C. & Myers, J. 1969. Fluorescence and oxygen evolution from Chlorella pyrenoidosa. - Biochim. Biophys. Acta 189: 366-389.
    • (1969) Biochim. Biophys. Acta , vol.189 , pp. 366-389
    • Bonaventura, C.1    Myers, J.2
  • 17
    • 0026561283 scopus 로고
    • Structural and functional characterization of the phosphorylated adipocyte lipid-binding protein (pp15)
    • Buelt, M. K., Xu, Z., Banaszak, L. J. & Bernlohr, D. A. 1992. Structural and functional characterization of the phosphorylated adipocyte lipid-binding protein (pp15). - Biochemistry 31: 3493-3499.
    • (1992) Biochemistry , vol.31 , pp. 3493-3499
    • Buelt, M.K.1    Xu, Z.2    Banaszak, L.J.3    Bernlohr, D.A.4
  • 18
    • 11944255590 scopus 로고
    • Adjustments of photosystem stoichiometry in chloroplasts improve the quantum efficiency of photosynthesis
    • Chow, W. S., Melis, A. & Anderson, J. M. 1990. Adjustments of photosystem stoichiometry in chloroplasts improve the quantum efficiency of photosynthesis. - Proc. Natl. Acad. Sci. USA 87: 7502-7506.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7502-7506
    • Chow, W.S.1    Melis, A.2    Anderson, J.M.3
  • 19
    • 0029739337 scopus 로고    scopus 로고
    • Conformational changes induced by phosphorylation in the CP29 subunit of photosystem II
    • Croce, R., Breton, J. & Bassi, R. 1996. Conformational changes induced by phosphorylation in the CP29 subunit of photosystem II. - Biochemistry 35: 11142-11148.
    • (1996) Biochemistry , vol.35 , pp. 11142-11148
    • Croce, R.1    Breton, J.2    Bassi, R.3
  • 20
    • 0029766235 scopus 로고    scopus 로고
    • State transitions or ΔpH-dependent quenching of photosystem II fluorescence in red algae
    • Delphin, E., Duval, J. C., Etienne, A. L. & Kirilovsky, D. 1996. State transitions or ΔpH-dependent quenching of photosystem II fluorescence in red algae. - Biochemistry 35: 9435-9445.
    • (1996) Biochemistry , vol.35 , pp. 9435-9445
    • Delphin, E.1    Duval, J.C.2    Etienne, A.L.3    Kirilovsky, D.4
  • 21
    • 0015372337 scopus 로고
    • 3-(3,4-Dichlorophenyl)-1,1-dimethylurea (DCMU) inhibition of system II and light-induced regulatory changes in energy transfer efficiency
    • Duysens, L. N. M. 1972. 3-(3,4-Dichlorophenyl)-1,1-dimethylurea (DCMU) inhibition of system II and light-induced regulatory changes in energy transfer efficiency. - Biophys. J. 12: 858-863.
    • (1972) Biophys. J. , vol.12 , pp. 858-863
    • Duysens, L.N.M.1
  • 22
    • 0000501373 scopus 로고
    • Regulation of photosystem composition in the cyanobacterial photosynthetic system: The regulation occurs in response to the redox state of the electron pool located between the two photosystems
    • Fujita, Y., Murakami, A. & Ohki, K. 1987. Regulation of photosystem composition in the cyanobacterial photosynthetic system: The regulation occurs in response to the redox state of the electron pool located between the two photosystems. - Plant Cell Physiol. 28: 283-292.
    • (1987) Plant Cell Physiol. , vol.28 , pp. 283-292
    • Fujita, Y.1    Murakami, A.2    Ohki, K.3
  • 23
    • 0002600978 scopus 로고
    • Short-term and long-term adaptation of the photosynthetic apparatus: Homeostatic properties of thylakoids
    • D. A. Bryant, ed., Kluwer Academic Publishers, Dordrecht, ISBN 0-7923-3273-3
    • _, Murakami, A., Aizawa, K. & Ohki, K. 1994. Short-term and long-term adaptation of the photosynthetic apparatus: Homeostatic properties of thylakoids. - In The Molecular Biology of Cyanobacteria (D. A. Bryant, ed.), pp. 677-692. Kluwer Academic Publishers, Dordrecht, ISBN 0-7923-3273-3.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 677-692
    • Murakami, A.1    Aizawa, K.2    Ohki, K.3
  • 24
    • 0030774348 scopus 로고    scopus 로고
    • Redox-controlled thylakoid protein phosphorylation. News and views
    • Gal, A., Zer, H. & Ohad, I. 1997. Redox-controlled thylakoid protein phosphorylation. News and views. - Physiol. Plant. 100: 869-885.
    • (1997) Physiol. Plant. , vol.100 , pp. 869-885
    • Gal, A.1    Zer, H.2    Ohad, I.3
  • 25
    • 0025032116 scopus 로고
    • Regulation of an enzyme by phosphorylation at the active site
    • Hurley, J. H., Dean, A. M., Sohl, J. L., Koshland, D. E. Jr & Stroud, R. M. 1990. Regulation of an enzyme by phosphorylation at the active site. - Science 249: 1012-1016.
    • (1990) Science , vol.249 , pp. 1012-1016
    • Hurley, J.H.1    Dean, A.M.2    Sohl, J.L.3    Koshland Jr., D.E.4    Stroud, R.M.5
  • 26
    • 0027170374 scopus 로고
    • Adaptation of Escherchia coli to redox environments by gene expression
    • Iuchi, S. & Lin, E. C. C. 1993. Adaptation of Escherchia coli to redox environments by gene expression. - Mol. Microbiol. 9: 9-15.
    • (1993) Mol. Microbiol. , vol.9 , pp. 9-15
    • Iuchi, S.1    Lin, E.C.C.2
  • 27
    • 0027310848 scopus 로고
    • The effects of phosphorylation on the structure and function of proteins
    • Johnson, L. N. & Barford, D. 1993. The effects of phosphorylation on the structure and function of proteins. - Annu. Rev. Biophys. Biomol. Struct. 22: 199-232.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 199-232
    • Johnson, L.N.1    Barford, D.2
  • 28
    • 0000004429 scopus 로고
    • Dynamics of photosystem stoichiometry adjustment by light quality in chloroplasts
    • Kim, J. H., Click, R. E. & Melis, A. 1993. Dynamics of photosystem stoichiometry adjustment by light quality in chloroplasts. - Plant Physiol. 102: 181-190.
    • (1993) Plant Physiol. , vol.102 , pp. 181-190
    • Kim, J.H.1    Click, R.E.2    Melis, A.3
  • 29
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. 1994. Atomic model of plant light-harvesting complex by electron crystallography. - Nature 367: 614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 30
    • 0001188850 scopus 로고
    • Regulation of photosystem stoichiometry, chlorophyll a and chlorophyll b content and relation to chloroplast ultrastructure
    • Melis, A. & Harvey, G. W. 1980. Regulation of photosystem stoichiometry, chlorophyll a and chlorophyll b content and relation to chloroplast ultrastructure. - Biochim. Biophys. Acta 637: 138-145.
    • (1980) Biochim. Biophys. Acta , vol.637 , pp. 138-145
    • Melis, A.1    Harvey, G.W.2
  • 31
    • 0028999102 scopus 로고
    • Solution structure of the cytoplasmic domain of phospholamban: Phosphorylation leads to a local perturbation in secondary structure
    • Mortishire-Smith, R. J., Pitzenberger, S. M., Burke, C. J., Middaugh, C. R., Garsky, V. M. & Johnson, R. G. 1995. Solution structure of the cytoplasmic domain of phospholamban: Phosphorylation leads to a local perturbation in secondary structure. - Biochemistry 34: 7603-7613.
    • (1995) Biochemistry , vol.34 , pp. 7603-7613
    • Mortishire-Smith, R.J.1    Pitzenberger, S.M.2    Burke, C.J.3    Middaugh, C.R.4    Garsky, V.M.5    Johnson, R.G.6
  • 32
    • 0027146161 scopus 로고
    • 6-f complex and regulation of PSI formation
    • 6-f complex and regulation of PSI formation. - Plant Cell Physiol. 34: 1175-1180.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 1175-1180
    • Murakami, A.1    Fujita, Y.2
  • 33
    • 0014690121 scopus 로고
    • Control of excitation transfer in photosynthesis. I. Light-induced change of chlorophyll a fluorescence in Porphyridium cruentum
    • Murata, N. 1969. Control of excitation transfer in photosynthesis. I. Light-induced change of chlorophyll a fluorescence in Porphyridium cruentum. - Biochim. Biophys. Acta 172: 242-251.
    • (1969) Biochim. Biophys. Acta , vol.172 , pp. 242-251
    • Murata, N.1
  • 34
    • 0002679978 scopus 로고
    • Enhancement studies in photosynthesis
    • Myers, J. 1971. Enhancement studies in photosynthesis. - Annu. Rev. Plant Physiol. 22: 189-312.
    • (1971) Annu. Rev. Plant Physiol. , vol.22 , pp. 189-312
    • Myers, J.1
  • 36
    • 0029848094 scopus 로고    scopus 로고
    • A protein kinase in the core of photosystem II
    • Race, H. L. & Hind, G. 1996. A protein kinase in the core of photosystem II. - Biochemistry 35: 13006-13010.
    • (1996) Biochemistry , vol.35 , pp. 13006-13010
    • Race, H.L.1    Hind, G.2
  • 37
    • 0028589065 scopus 로고
    • Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli
    • Rajogopal, P., Waygood, E. B. & Klevit, R. E. 1994. Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli. - Biochemistry 33: 15271-15282.
    • (1994) Biochemistry , vol.33 , pp. 15271-15282
    • Rajogopal, P.1    Waygood, E.B.2    Klevit, R.E.3
  • 38
    • 0024334338 scopus 로고
    • Secondary structure of charge isomers of myelin basic protein before and after phosphorylation
    • Ramwani, J. J., Epand, R. M. & Moscarello, M. A. 1989. Secondary structure of charge isomers of myelin basic protein before and after phosphorylation. - Biochemistry 28: 6538-6543.
    • (1989) Biochemistry , vol.28 , pp. 6538-6543
    • Ramwani, J.J.1    Epand, R.M.2    Moscarello, M.A.3
  • 39
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock, J. B., Ninfa, A. J. & Stock, A. M. 1989. Protein phosphorylation and regulation of adaptive responses in bacteria. -Microbiol. Rev. 53: 450-490.
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 40
    • 0031019648 scopus 로고    scopus 로고
    • Plastoquinol at the quinol oxidation site of reduced cytochrome bf mediates signal transduction between light and protein phosphorylation: Thylakoid protein kinase deactivation by a single-turnover flash
    • Vener, A. V., van Kan, P. J. M., Rich, P. R., Ohad, I. & Andersson, B. 1997. Plastoquinol at the quinol oxidation site of reduced cytochrome bf mediates signal transduction between light and protein phosphorylation: Thylakoid protein kinase deactivation by a single-turnover flash. - Proc. Natl. Acad. Sci. USA 94: 1585-1590.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1585-1590
    • Vener, A.V.1    Van Kan, P.J.M.2    Rich, P.R.3    Ohad, I.4    Andersson, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.