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Volumn 28, Issue 9, 2003, Pages 467-470

Light, redox state, thylakoid-protein phosphorylation and signaling gene expression

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PROTEIN KINASE; PROTEIN KINASE STT7; THREONINE; THYLAKOID BOUND PROTEIN TSP9; UNCLASSIFIED DRUG; PROTEIN SERINE THREONINE KINASE; VEGETABLE PROTEIN;

EID: 0642276006     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(03)00173-7     Document Type: Short Survey
Times cited : (58)

References (26)
  • 2
  • 3
  • 5
    • 0035653682 scopus 로고    scopus 로고
    • Balance of power: A view of the mechanism of photosynthetic state transitions
    • Haldrup A., et al. Balance of power: a view of the mechanism of photosynthetic state transitions. Trends Plant Sci. 6:2001;301-305.
    • (2001) Trends Plant Sci. , vol.6 , pp. 301-305
    • Haldrup, A.1
  • 6
    • 0037015689 scopus 로고    scopus 로고
    • Proteolytic activity against the light-harvesting complex and the D1/D2 core proteins of Photosystem II in close association to the light-harvesting complex II trimer
    • Georgakopulos J.H., et al. Proteolytic activity against the light-harvesting complex and the D1/D2 core proteins of Photosystem II in close association to the light-harvesting complex II trimer. Biochim. Biophys. Acta. 1556:2002;53-64.
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 53-64
    • Georgakopulos, J.H.1
  • 7
    • 0001230014 scopus 로고    scopus 로고
    • Phosphatase activities in spinach thylakoid membranes - Effectors, regulation and location
    • Carlberg I., Andersson B. 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
  • 8
    • 0035028317 scopus 로고    scopus 로고
    • Non-photochemical quenching. a response to excess light energy
    • Muller P., et al. Non-photochemical quenching. A response to excess light energy. Plant Physiol. 125:2001;1558-1566.
    • (2001) Plant Physiol. , vol.125 , pp. 1558-1566
    • Muller, P.1
  • 9
    • 0035834001 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is regulated by signals initiated by both photosystems II and I
    • Trebitsh T., Danon A. Translation of chloroplast psbA mRNA is regulated by signals initiated by both photosystems II and I. Proc. Natl. Acad. Sci. U. S. A. 98:2001;12289-12294.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12289-12294
    • Trebitsh, T.1    Danon, A.2
  • 10
    • 0028865421 scopus 로고
    • Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool
    • Escoubas J.M., et al. Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool. Proc. Natl. Acad. Sci. U. S. A. 92:1995;10237-10241.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 10237-10241
    • Escoubas, J.M.1
  • 11
    • 0035965292 scopus 로고    scopus 로고
    • A novel mechanism of nuclear photosynthesis gene regulation by redox signals from the chloroplast during photosystem stoichiometry adjustment
    • Pfannschmidt T., et al. A novel mechanism of nuclear photosynthesis gene regulation by redox signals from the chloroplast during photosystem stoichiometry adjustment. J. Biol. Chem. 276:2001;36125-36130.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36125-36130
    • Pfannschmidt, T.1
  • 12
    • 0037458032 scopus 로고    scopus 로고
    • A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes
    • Carlberg I., et al. A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes. Proc. Natl. Acad. Sci. U. S. A. 100:2003;757-762.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 757-762
    • Carlberg, I.1
  • 13
    • 0037298310 scopus 로고    scopus 로고
    • Redox regulation of thylakoid protein phosphorylation
    • (Foyer, C. ed.), Mary Ann Liebert.
    • Aro, E-M. and Ohad, I. (2003) Redox regulation of thylakoid protein phosphorylation. In Antioxidants and Redox Signaling (Vol. 5) (Foyer, C. ed.), pp. 55-67, Mary Ann Liebert.
    • (2003) Antioxidants and Redox Signaling , vol.5 , pp. 55-67
    • Aro, E.-M.1    Ohad, I.2
  • 14
    • 0347579832 scopus 로고    scopus 로고
    • Light affects the accessibility of the thylakoid light harvesting complex II (LHCII) phosphorylation site to the membrane protein kinase(s)
    • Zer H., et al. Light affects the accessibility of the thylakoid light harvesting complex II (LHCII) phosphorylation site to the membrane protein kinase(s). Biochemistry. 42:2003;728-738.
    • (2003) Biochemistry , vol.42 , pp. 728-738
    • Zer, H.1
  • 15
    • 0040205730 scopus 로고    scopus 로고
    • Thylakoid protein phosphorylation and the thiol redox state
    • Carlberg I., et al. Thylakoid protein phosphorylation and the thiol redox state. Biochemistry. 38:1999;3197-3204.
    • (1999) Biochemistry , vol.38 , pp. 3197-3204
    • Carlberg, I.1
  • 16
    • 0033515448 scopus 로고    scopus 로고
    • TAKs, thylakoid membrane protein kinases associated with energy transduction
    • Snyders S., Kohorn B.D. TAKs, thylakoid membrane protein kinases associated with energy transduction. J. Biol. Chem. 274:1999;9137-9140.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9137-9140
    • Snyders, S.1    Kohorn, B.D.2
  • 17
    • 0032704273 scopus 로고    scopus 로고
    • Isolation of state transition mutants of Chlamydomonas reinhardtii by fluorescence video imaging
    • Kruse O., et al. Isolation of state transition mutants of Chlamydomonas reinhardtii by fluorescence video imaging. Photosynth. Res. 61:1999;43-51.
    • (1999) Photosynth. Res. , vol.61 , pp. 43-51
    • Kruse, O.1
  • 18
    • 0032719469 scopus 로고    scopus 로고
    • Isolation and characterization of photoautotrophic mutants of Chlamydomonas reinhardtii deficient in state transition
    • Fleischmann M.M., et al. Isolation and characterization of photoautotrophic mutants of Chlamydomonas reinhardtii deficient in state transition. J. Biol. Chem. 274:1999;30987-30994.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30987-30994
    • Fleischmann, M.M.1
  • 19
    • 0037423885 scopus 로고    scopus 로고
    • Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas
    • Depège N., et al. Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas. Science. 299:2003;1572-1575.
    • (2003) Science , vol.299 , pp. 1572-1575
    • Depège, N.1
  • 20
    • 0034802940 scopus 로고    scopus 로고
    • Identification of Lhcb gene family encoding the light-harvesting chlorophyll- a/b proteins of photosystem II in Chlamydomonas reinhardtii
    • Teramoto H., et al. Identification of Lhcb gene family encoding the light-harvesting chlorophyll- a/b proteins of photosystem II in Chlamydomonas reinhardtii. Plant Cell Physiol. 42:2001;849-856.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 849-856
    • Teramoto, H.1
  • 21
    • 34249918787 scopus 로고
    • The chlorophyll-a/b proteins of photosystem II in Chlamydomonas reinhardtii
    • Bassi R., Wollman F.-A. The chlorophyll-a/b proteins of photosystem II in Chlamydomonas reinhardtii. Planta. 183:1991;423-433.
    • (1991) Planta , vol.183 , pp. 423-433
    • Bassi, R.1    Wollman, F.-A.2
  • 22
    • 0031019648 scopus 로고    scopus 로고
    • Plastoquinol at the Qo-site of reduced cytochrome b/f mediates signal transduction between light and thylakoid phosphorylation: Thylakoid protein kinase deactivation by a single turnover flash
    • Vener A., et al. Plastoquinol at the Qo-site of reduced cytochrome b/f mediates signal transduction between light and thylakoid phosphorylation: thylakoid protein kinase deactivation by a single turnover flash. Proc. Natl. Acad. Sci. U. S. A. 94:1997;1585-1590.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1585-1590
    • Vener, A.1
  • 23
    • 0033152641 scopus 로고    scopus 로고
    • The Qo site of cytochrome b6f complexes controls the activation of the LHCII kinase
    • Zito F., et al. The Qo site of cytochrome b6f complexes controls the activation of the LHCII kinase. EMBO J. 18:1999;2961-2969.
    • (1999) EMBO J. , vol.18 , pp. 2961-2969
    • Zito, F.1
  • 25
    • 0034595810 scopus 로고    scopus 로고
    • A new subunit of cytochrome b6f complex undergoes reversible phosphorylation upon state transition
    • Hamel P., et al. A new subunit of cytochrome b6f complex undergoes reversible phosphorylation upon state transition. J. Biol. Chem. 275:2000;17072-17079.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17072-17079
    • Hamel, P.1
  • 26
    • 0035933863 scopus 로고    scopus 로고
    • Photoinhibition of Chlamydomonas reinhardtii in State 1 and State 2: Damages to the photosynthetic apparatus under linear and cyclic electron flow
    • Finazzi G., et al. Photoinhibition of Chlamydomonas reinhardtii in State 1 and State 2: damages to the photosynthetic apparatus under linear and cyclic electron flow. J. Biol. Chem. 276:2001;22251-22257.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22251-22257
    • Finazzi, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.