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Volumn 1, Issue 3, 1998, Pages 217-223

Protein phosphorylation and redox sensing in chloroplast thylakoids

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE; VEGETABLE PROTEIN;

EID: 0032083023     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5266(98)80107-6     Document Type: Article
Times cited : (125)

References (9)
  • 1
    • 0003018424 scopus 로고    scopus 로고
    • State transition and photoinhibition
    • Edited by Rochaix JD, Goldschmidt-Clermont M, Merchant S. Dordrecht: Kluwer Academic Publishers; in press
    • Keren N, Ohad I: State transition and photoinhibition. In Molecular Biology of Chlamydomonas: Chloroplast and Mitochondria. Edited by Rochaix JD, Goldschmidt-Clermont M, Merchant S. Dordrecht: Kluwer Academic Publishers; 1998: in press.
    • (1998) Molecular Biology of Chlamydomonas: Chloroplast and Mitochondria
    • Keren, N.1    Ohad, I.2
  • 2
    • 0017411320 scopus 로고
    • Phosphorylation of chloroplast membrane proteins
    • Bennett J: Phosphorylation of chloroplast membrane proteins. Nature 1977, 269:344-346.
    • (1977) Nature , vol.269 , pp. 344-346
    • Bennett, J.1
  • 3
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems
    • Allen JF, Bennett J, Steinback KE, Arntzen CJ: Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. Nature 1981, 291:25-29.
    • (1981) Nature , vol.291 , pp. 25-29
    • Allen, J.F.1    Bennett, J.2    Steinback, K.E.3    Arntzen, C.J.4
  • 4
    • 0000879463 scopus 로고
    • Activation of adenosine 5′ triphosphateinduced quenching of chlorophyll fluorescence by reduced plastoquinone. Basis of state I - State II transitions in chloroplasts
    • Horton P, Black MT: Activation of adenosine 5′ triphosphateinduced quenching of chlorophyll fluorescence by reduced plastoquinone. Basis of state I - state II transitions in chloroplasts. FEBS Lett 1980, 119:141-144.
    • (1980) FEBS Lett , vol.119 , pp. 141-144
    • Horton, P.1    Black, M.T.2
  • 5
    • 0030774348 scopus 로고    scopus 로고
    • Redox-controlled thylakoid protein phosphorylation. News and views
    • Gal A, Zer H, Ohad I: Redox-controlled thylakoid protein phosphorylation. News and views. Physiol Plant 1997, 100:869-885. A review on light/redox-dependent protein phosphorylation in thylakoids with emphasis on its relation to state transitions and protein turnover. The review describes the mechanism of the redox control of the kinase(s), requirement of a dynamic membrane organisation for kinase activation and the present state of enzyme identification.
    • (1997) Physiol Plant , vol.100 , pp. 869-885
    • Gal, A.1    Zer, H.2    Ohad, I.3
  • 6
    • 0026556851 scopus 로고
    • Protein phosphorylation in regulation of photosynthesis
    • Allen JF: Protein phosphorylation in regulation of photosynthesis. Biochim Biophys Acta 1992, 1098:275-335.
    • (1992) Biochim Biophys Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 7
    • 0028894980 scopus 로고
    • Activation/deactivation cycle of redox-controlled thylakoid protein phosphorylation. Role of plastoquinol bound to the reduced cytochrome bf complex
    • Vener AV, Van Kan PJ, Gal A, Andersson B, Ohad I: Activation/deactivation cycle of redox-controlled thylakoid protein phosphorylation. Role of plastoquinol bound to the reduced cytochrome bf complex. J Biol Chem 1995, 270:25225-25232.
    • (1995) J Biol Chem , vol.270 , pp. 25225-25232
    • Vener, A.V.1    Van Kan, P.J.2    Gal, A.3    Andersson, B.4    Ohad, I.5
  • 8
    • 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 AV, van Kan PJM, Rich PR, Ohad I, Andersson B: 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 1997, 94:1585-1590. A novel mechanism for thylakoid protein phosphorylation redox control is presented. It involves a single plastoquinol molecule binding to the quinoloxidation site of the cytochrome bf complex with a reduced high potential path. The protein kinase activation and deactivation analysis included determination of the redox states of the electron transport components by low temperature electron paramagnetic resonance, laser flash photolysis, optical spectroscopy and inhibitor studies.
    • (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.