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Volumn 128, Issue 2, 1997, Pages 159-168

Differences in the rate of dephosphorylation of thylakoid proteins during dark incubation after chilling in the light between two rice (Oriza sativa L.) varieties

Author keywords

Chlorophyll fluorescence; Low temperature; Phosphatase inhibitors; Photoinhibition; Protein dephosphorylation; Rice (Oryza saliva L.)

Indexed keywords

MEMBRANE PROTEIN;

EID: 0030825712     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(97)00161-1     Document Type: Article
Times cited : (16)

References (32)
  • 1
    • 0000362285 scopus 로고
    • The effect of light, during and subsequent to chilling, on the photosynthetic activity of two soybean cultivars, measured by in vivo chlorophyll fluorescence
    • G. Neuner, W. Larcher, The effect of light, during and subsequent to chilling, on the photosynthetic activity of two soybean cultivars, measured by in vivo chlorophyll fluorescence, Photosynthetica 25 (1991) 257-266.
    • (1991) Photosynthetica , vol.25 , pp. 257-266
    • Neuner, G.1    Larcher, W.2
  • 2
    • 0343139970 scopus 로고    scopus 로고
    • Chlorophyll fluorescence in cucumber (Cucumis sativus L.) and pea (Pisum sativum L.) leaves under chilling stress in the light and during the subsequent recovery period
    • S.B. Ha, Y.J. Eu, C.-H. Lee, Chlorophyll fluorescence in cucumber (Cucumis sativus L.) and pea (Pisum sativum L.) leaves under chilling stress in the light and during the subsequent recovery period, J. Photosci. 3 (1996) 15-21.
    • (1996) J. Photosci. , vol.3 , pp. 15-21
    • Ha, S.B.1    Eu, Y.J.2    Lee, C.-H.3
  • 3
    • 0002183167 scopus 로고    scopus 로고
    • Screening for stress tolerance by chlorophyll fluorescence
    • U. Hashimoto, P.J. Kramer, H. Nonami, B.R. Strain (Eds.), Academic Press, New York
    • R.M. Smillie, S.E. Hetherington, Screening for stress tolerance by chlorophyll fluorescence, in: U. Hashimoto, P.J. Kramer, H. Nonami, B.R. Strain (Eds.), Measurement Techniques in Plant Science, Academic Press, New York, pp. 229-261.
    • Measurement Techniques in Plant Science , pp. 229-261
    • Smillie, R.M.1    Hetherington, S.E.2
  • 4
    • 0010766355 scopus 로고
    • Assessment of chilling sensitivity by chlorophyll fluorescence analysis
    • C.Y. Wang (Ed.), CRC Press, Florida
    • J.M. Wilson, J.A. Greaves, Assessment of chilling sensitivity by chlorophyll fluorescence analysis, in: C.Y. Wang (Ed.), Chilling Injury of Horticultural Crops, CRC Press, Florida, 1990, pp 129-141.
    • (1990) Chilling Injury of Horticultural Crops , pp. 129-141
    • Wilson, J.M.1    Greaves, J.A.2
  • 5
    • 0029102413 scopus 로고
    • Methods of selection for chilling tolerance in Nepalese rice by chlorophyll fluorescence analysis
    • B.R. Sthapit, J.R. Witcombe, J.M. Wilson, Methods of selection for chilling tolerance in Nepalese rice by chlorophyll fluorescence analysis, Crop Sci. 35 (1995) 90-94.
    • (1995) Crop Sci. , vol.35 , pp. 90-94
    • Sthapit, B.R.1    Witcombe, J.R.2    Wilson, J.M.3
  • 6
    • 0342705619 scopus 로고    scopus 로고
    • Early alterations of chlorophyll fluorescence by light-chilling in cucumber (Cucumis sativus L.). Leaves and their usage as stress indicators
    • S.B. Ha, Y.J. Eu, C.-H. Lee, Early alterations of chlorophyll fluorescence by light-chilling in cucumber (Cucumis sativus L.). leaves and their usage as stress indicators, Korean J. Ecol. 19 (1996) 151-163.
    • (1996) Korean J. Ecol. , vol.19 , pp. 151-163
    • Ha, S.B.1    Eu, Y.J.2    Lee, C.-H.3
  • 7
    • 0000937802 scopus 로고
    • Practical applications of fluorometric methods to algae and higher plant research
    • Govindjee, J. Amesz, D.C. Fork (Eds.), Academic Press, New York
    • G. Renger, U. Schreiber, Practical applications of fluorometric methods to algae and higher plant research, in: Govindjee, J. Amesz, D.C. Fork (Eds.), Light Emission by Plants and Bacteria, Academic Press, New York, 1986, pp. 587-619.
    • (1986) Light Emission by Plants and Bacteria , pp. 587-619
    • Renger, G.1    Schreiber, U.2
  • 8
    • 0001138725 scopus 로고
    • Protein phosphorylation in green plant chloroplasts
    • J. Bennett, Protein phosphorylation in green plant chloroplasts, Annu. Rev. Plant Physiol. Plant Mol. Biol. 42 (1991) 281-311.
    • (1991) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.42 , pp. 281-311
    • Bennett, J.1
  • 9
    • 0026556851 scopus 로고
    • Protein phosphorylation in regulation of photosynthesis
    • J.F. Allen, Protein phosphorylation in regulation of photosynthesis, Biochim. Biophys. Acta 1098 (1992) 275-335.
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 10
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems
    • J.F. Allen, J. Bennett, K.E. Steinback, C.J. Arntzen, Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems, Nature 291 (1981) 21-25.
    • (1981) Nature , vol.291 , pp. 21-25
    • Allen, J.F.1    Bennett, J.2    Steinback, K.E.3    Arntzen, C.J.4
  • 11
    • 0343575721 scopus 로고
    • Light-induced redox changes in chloroplast cytochrome f after phosphorylation of membrane
    • P. Horton, M. Black, Light-induced redox changes in chloroplast cytochrome f after phosphorylation of membrane, FEBS Lett. 132 (1981) 75-77.
    • (1981) FEBS Lett. , vol.132 , pp. 75-77
    • Horton, P.1    Black, M.2
  • 12
    • 0028988014 scopus 로고
    • A post-translation modification of the phyotosystem II subunit CP29 protects maize from cold stress
    • Bergantino, P. Dainese, Z. Cerovic, S. Sechi, R. Bassi, A post-translation modification of the phyotosystem II subunit CP29 protects maize from cold stress, J. Biol. Chem. 270 (1995) 8474-8481.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8474-8481
    • Bergantino1    Dainese, P.2    Cerovic, Z.3    Sechi, S.4    Bassi, R.5
  • 13
    • 0002020534 scopus 로고
    • Phosphorylation of chloroplast membrane proteins partially protects aganst phoinhibition
    • P. Horton, P. Lee, Phosphorylation of chloroplast membrane proteins partially protects aganst phoinhibition, Planta 165 (1985) 37-42.
    • (1985) Planta , vol.165 , pp. 37-42
    • Horton, P.1    Lee, P.2
  • 14
    • 0342705617 scopus 로고
    • Chilling sensitivity in Oryza sativa: The role of protein phosphorylation in protection against photoinhibition
    • B.A. Moll, K.E. Steinback, Chilling sensitivity in Oryza sativa: the role of protein phosphorylation in protection against photoinhibition, Plant Physiol. 80 (1986) 420-423.
    • (1986) Plant Physiol. , vol.80 , pp. 420-423
    • Moll, B.A.1    Steinback, K.E.2
  • 15
    • 0029167906 scopus 로고
    • Regulation of D1-protein degradation during photoinhibition of photosystem II in vivo: Phosphorylation of the D1 protein in various plant groups
    • E. Rintamäki, R. Salo, E. Lehtonen, E.M. Aro, Regulation of D1-protein degradation during photoinhibition of photosystem II in vivo: phosphorylation of the D1 protein in various plant groups, Planta 195 (1995) 379-386.
    • (1995) Planta , vol.195 , pp. 379-386
    • Rintamäki, E.1    Salo, R.2    Lehtonen, E.3    Aro, E.M.4
  • 16
    • 0030520622 scopus 로고    scopus 로고
    • Effects of chilling injury in the light on chlorophyll fluorescence and D1 protein turnover in cucumber and pea leaves
    • Y.J. Eu, S.B. Ha, C.-H. Lee, Effects of chilling injury in the light on chlorophyll fluorescence and D1 protein turnover in cucumber and pea leaves, J. Biochem. Mol. Biol. 29 (1996) 398-404.
    • (1996) J. Biochem. Mol. Biol. , vol.29 , pp. 398-404
    • Eu, Y.J.1    Ha, S.B.2    Lee, C.-H.3
  • 17
    • 0000339737 scopus 로고
    • Chlorophyll fluorescence transients
    • J.L. Harwood, J.R. Bowyer (Eds.), Academic Press, New York
    • P. Horton, J.R. Bowyer, Chlorophyll fluorescence transients, in: J.L. Harwood, J.R. Bowyer (Eds.), Methods in Plant Biochemistry, vol. 4, Academic Press, New York, 1990, pp. 259-296.
    • (1990) Methods in Plant Biochemistry , vol.4 , pp. 259-296
    • Horton, P.1    Bowyer, J.R.2
  • 18
    • 0027139717 scopus 로고
    • Photoinhibition and D1 protein degradation in peas acclimated to different growth irradiances
    • E.M. Aro, S. McCaffery, J.M. Anderson, Photoinhibition and D1 protein degradation in peas acclimated to different growth irradiances, Plant Physiol. 103 (1993) 835-843.
    • (1993) Plant Physiol. , vol.103 , pp. 835-843
    • Aro, E.M.1    McCaffery, S.2    Anderson, J.M.3
  • 19
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris
    • D.I. Arnon, Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris, Plant Physiol. 24 (1949) 1-15.
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 20
    • 0028078197 scopus 로고
    • Two mechanisms of recovery from photoinhibition in vivo: Reactivation of photosystem II related and unrelated to D1-protein turnover
    • J. Leitsch, B. Schnettger, C. Critchley, G.H. Krause, Two mechanisms of recovery from photoinhibition in vivo: Reactivation of photosystem II related and unrelated to D1-protein turnover, Planta 194 (1994) 15-21.
    • (1994) Planta , vol.194 , pp. 15-21
    • Leitsch, J.1    Schnettger, B.2    Critchley, C.3    Krause, G.H.4
  • 21
    • 0028052864 scopus 로고
    • Rapid turnover of the D1 reaction-center protein of photosystem II as a protection mechanism against photoinhibition in a moss Ceratodon purpureus (Hedw.)
    • E. Rintamäki, R. Salo, E.M. Aro, Rapid turnover of the D1 reaction-center protein of photosystem II as a protection mechanism against photoinhibition in a moss Ceratodon purpureus (Hedw.), Brid. Planta 193 (1994) 520-529.
    • (1994) Brid. Planta , vol.193 , pp. 520-529
    • Rintamäki, E.1    Salo, R.2    Aro, E.M.3
  • 22
    • 0028606359 scopus 로고
    • The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane lipids: A mechanism of chilling tolerance
    • Z. Gombos, H. Wada, N. Murata, The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane lipids: a mechanism of chilling tolerance, Proc. Natl. Acad. Sci. USA 91 (1994) 8787-8791.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8787-8791
    • Gombos, Z.1    Wada, H.2    Murata, N.3
  • 23
    • 34250085121 scopus 로고
    • Photosystem II reaction centres stay intact during low temperature photoinhibition
    • C. Ottander, T. Hundal, B. Andersson, N.P. A Huner, G. Öquist, Photosystem II reaction centres stay intact during low temperature photoinhibition, Photosynth. Res. 35 (1993) 191-200.
    • (1993) Photosynth. Res. , vol.35 , pp. 191-200
    • Ottander, C.1    Hundal, T.2    Andersson, B.3    Huner, N.P.A.4    Öquist, G.5
  • 24
    • 0029930771 scopus 로고    scopus 로고
    • Differential D1 dephosphorylation in functional and photodamaed photosystm II centers
    • E. Rintamäki, R. Kettunen, E.M. Aro, Differential D1 dephosphorylation in functional and photodamaed photosystm II centers, J. Biol. Chem. 271 (1996) 14870-14875.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14870-14875
    • Rintamäki, E.1    Kettunen, R.2    Aro, E.M.3
  • 26
    • 0024503509 scopus 로고
    • The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase
    • G. Camici, G. Manao, G. Cappugi, A. Modesti, M. Stefani, G. Ramponi, The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase, J. Biol. Chem. 264 (1989) 2560-2567.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2560-2567
    • Camici, G.1    Manao, G.2    Cappugi, G.3    Modesti, A.4    Stefani, M.5    Ramponi, G.6
  • 27
    • 0026038524 scopus 로고
    • Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase
    • D.A. Pot, T.A. Woodford, E. Remboutsika, R.S. Haun, J.E. Dixon, Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase, J. Biol. Chem. 266 (1991) 19688-19696.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19688-19696
    • Pot, D.A.1    Woodford, T.A.2    Remboutsika, E.3    Haun, R.S.4    Dixon, J.E.5
  • 28
    • 0028310415 scopus 로고
    • Identification of an essential cysteine residue in pyridoxal phosphatase from human erythrocytes
    • G. Gao, M.L. Fonda, Identification of an essential cysteine residue in pyridoxal phosphatase from human erythrocytes, J. Biol. Chem. 269 (1994) 8234-8239.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8234-8239
    • Gao, G.1    Fonda, M.L.2
  • 29
    • 0000562995 scopus 로고
    • Assessing modulation of stromal and thylakoid light-harvesting complex-II phosphatase activities with phosphopeptide substrates
    • M.F. Hammer, G. Sarath, J.C. Osterman, J. Markwell, Assessing modulation of stromal and thylakoid light-harvesting complex-II phosphatase activities with phosphopeptide substrates, Photosynth. Res. 44 (1995) 107-115.
    • (1995) Photosynth. Res. , vol.44 , pp. 107-115
    • Hammer, M.F.1    Sarath, G.2    Osterman, J.C.3    Markwell, J.4
  • 30
    • 0001230014 scopus 로고    scopus 로고
    • Phosphatase activities in spinach thylakoid membranes-effectors, regulation and location
    • I. Carlberg, B. Andersson, Phosphatase activities in spinach thylakoid membranes-effectors, regulation and location, Photosynth. Res. 47 (1996) 145-156.
    • (1996) Photosynth. Res. , vol.47 , pp. 145-156
    • Carlberg, I.1    Andersson, B.2
  • 31
    • 0028041218 scopus 로고
    • Regulation of thylakoid protein phosphorylation in intact chloroplasts by the activity of kinases and phosphatases
    • V. Ebbert, D. Godde, Regulation of thylakoid protein phosphorylation in intact chloroplasts by the activity of kinases and phosphatases, Biochim. Biophys. Acta 1187 (1994) 335-346.
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 335-346
    • Ebbert, V.1    Godde, D.2
  • 32
    • 0001139454 scopus 로고
    • Photoinhibition at chilling temperature
    • S. Somersalo, G.H. Krause, Photoinhibition at chilling temperature, Planta 177 (1989) 409-416.
    • (1989) Planta , vol.177 , pp. 409-416
    • Somersalo, S.1    Krause, G.H.2


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