메뉴 건너뛰기




Volumn 1757, Issue 3, 2006, Pages 198-205

Glycerate-3-phosphate, produced by CO2 fixation in the Calvin cycle, is critical for the synthesis of the D1 protein of photosystem II

Author keywords

Calvin cycle; CO2 fixation; D1 protein; Glycerate 3 phosphate; Photoinhibition; Photosystem II

Indexed keywords

3 PHOSPHOGLYCERIC ACID; ALDEHYDE DERIVATIVE; CARBON DIOXIDE; D1 PROTEIN; GLYCERIC ACID; PHOSPHORIBULOKINASE; PROTEIN; REACTIVE OXYGEN METABOLITE; RIBULOSE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 33646107142     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.02.002     Document Type: Article
Times cited : (79)

References (47)
  • 1
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II. Inactivation, protein damage and turnover
    • Aro E.M., Virgin I., and Andersson B. Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochim. Biophys. Acta 1143 (1993) 113-134
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 2
    • 0021473380 scopus 로고
    • Membrane protein damage and repair: removal and replacement of inactivated 32-kilodalton polypeptides in chloroplast membranes
    • Ohad I., Kyle D.J., and Arntzen C.J. Membrane protein damage and repair: removal and replacement of inactivated 32-kilodalton polypeptides in chloroplast membranes. J. Cell Biol. 99 (1984) 481-485
    • (1984) J. Cell Biol. , vol.99 , pp. 481-485
    • Ohad, I.1    Kyle, D.J.2    Arntzen, C.J.3
  • 3
    • 0027139717 scopus 로고
    • Photoinhibition and D1 protein degradation in Peas acclimated to different growth irradiances
    • Aro E.M., McCaffery S., and Anderson J.M. 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
  • 4
    • 3042679202 scopus 로고    scopus 로고
    • Environmental stress inhibits the synthesis de novo of proteins involved in the photodamage-repair cycle of photosystem II in Synechocystis sp PCC 6803
    • Allakhverdiev S.I., and Murata N. Environmental stress inhibits the synthesis de novo of proteins involved in the photodamage-repair cycle of photosystem II in Synechocystis sp PCC 6803. Biochim. Biophys. Acta 1657 (2004) 23-32
    • (2004) Biochim. Biophys. Acta , vol.1657 , pp. 23-32
    • Allakhverdiev, S.I.1    Murata, N.2
  • 6
    • 0035886704 scopus 로고    scopus 로고
    • Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery
    • Nishiyama Y., Yamamoto H., Allakhverdiev S.I., Inaba M., Yokota A., and Murata N. Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery. EMBO J. 20 (2001) 5587-5594
    • (2001) EMBO J. , vol.20 , pp. 5587-5594
    • Nishiyama, Y.1    Yamamoto, H.2    Allakhverdiev, S.I.3    Inaba, M.4    Yokota, A.5    Murata, N.6
  • 7
    • 4444313478 scopus 로고    scopus 로고
    • Singlet oxygen inhibits the repair of photosystem II by suppressing the translation elongation of the D1 protein in Synechocystis sp. PCC 6803
    • Nishiyama Y., Allakhverdiev S.I., Yamamoto H., Hayashi H., and Murata N. Singlet oxygen inhibits the repair of photosystem II by suppressing the translation elongation of the D1 protein in Synechocystis sp. PCC 6803. Biochemistry 43 (2004) 11321-11330
    • (2004) Biochemistry , vol.43 , pp. 11321-11330
    • Nishiyama, Y.1    Allakhverdiev, S.I.2    Yamamoto, H.3    Hayashi, H.4    Murata, N.5
  • 8
    • 23444459220 scopus 로고    scopus 로고
    • Inhibition of the repair of photosystem II by oxidative stress in cyanobacteria
    • Nishiyama Y., Allakhverdiev S.I., and Murata N. Inhibition of the repair of photosystem II by oxidative stress in cyanobacteria. Photosynth. Res. 84 (2005) 1-7
    • (2005) Photosynth. Res. , vol.84 , pp. 1-7
    • Nishiyama, Y.1    Allakhverdiev, S.I.2    Murata, N.3
  • 9
    • 20444405387 scopus 로고    scopus 로고
    • Two-step mechanism of photodamage to photosystem II: step one occurs at the oxygen-evolving complex and step two occurs at the photochemical reaction center
    • Ohnishi N., Allakhverdiev S.I., Takahashi S., Higashi S., Watanabe M., Nishiyama Y., and Murata N. Two-step mechanism of photodamage to photosystem II: step one occurs at the oxygen-evolving complex and step two occurs at the photochemical reaction center. Biochemistry 44 (2005) 8494-8499
    • (2005) Biochemistry , vol.44 , pp. 8494-8499
    • Ohnishi, N.1    Allakhverdiev, S.I.2    Takahashi, S.3    Higashi, S.4    Watanabe, M.5    Nishiyama, Y.6    Murata, N.7
  • 10
    • 11144306460 scopus 로고    scopus 로고
    • Evidence for the role of the oxygen-evolving manganese complex in photoinhibition of photosystem II
    • Hakala M., Tuominen I., Keränen M., Tyystjärvi T., and Tyystjärvi E. Evidence for the role of the oxygen-evolving manganese complex in photoinhibition of photosystem II. Biochim. Biophys. Acta 1706 (2005) 68-80
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 68-80
    • Hakala, M.1    Tuominen, I.2    Keränen, M.3    Tyystjärvi, T.4    Tyystjärvi, E.5
  • 11
    • 21744452290 scopus 로고    scopus 로고
    • Interruption of the Calvin cycle inhibits the repair of photosystem II from photodamage
    • Takahashi S., and Murata N. Interruption of the Calvin cycle inhibits the repair of photosystem II from photodamage. Biochim. Biophys. Acta 1708 (2005) 352-361
    • (2005) Biochim. Biophys. Acta , vol.1708 , pp. 352-361
    • Takahashi, S.1    Murata, N.2
  • 13
    • 18744415730 scopus 로고    scopus 로고
    • Systematic analysis of the relation of electron transport and ATP synthesis to the photodamage and repair of photosystem II in Synechocystis
    • Allakhverdiev S.I., Nishiyama Y., Takahashi S., Miyairi S., Suzuki I., and Murata N. Systematic analysis of the relation of electron transport and ATP synthesis to the photodamage and repair of photosystem II in Synechocystis. Plant Physiol. 137 (2005) 263-273
    • (2005) Plant Physiol. , vol.137 , pp. 263-273
    • Allakhverdiev, S.I.1    Nishiyama, Y.2    Takahashi, S.3    Miyairi, S.4    Suzuki, I.5    Murata, N.6
  • 14
    • 0023840317 scopus 로고
    • Comparative analysis of the biogenesis of photosystem II in the wild-type and Y-1 mutant of Chlamydomonas reinhardtii
    • Malnoë P., Mayfield S.P., and Rochaix J.D. Comparative analysis of the biogenesis of photosystem II in the wild-type and Y-1 mutant of Chlamydomonas reinhardtii. J. Cell Biol. 106 (1988) 609-616
    • (1988) J. Cell Biol. , vol.106 , pp. 609-616
    • Malnoë, P.1    Mayfield, S.P.2    Rochaix, J.D.3
  • 15
    • 0028222184 scopus 로고
    • ADP-dependent phosphorylation regulates RNA-binding in vitro: implications in light-modulated translation
    • Danon A., and Mayfield S.P. ADP-dependent phosphorylation regulates RNA-binding in vitro: implications in light-modulated translation. EMBO J. 13 (1994) 2227-2235
    • (1994) EMBO J. , vol.13 , pp. 2227-2235
    • Danon, A.1    Mayfield, S.P.2
  • 16
    • 0028587976 scopus 로고
    • Light-regulated translation of chloroplast messenger RNAs through redox potential
    • Danon A., and Mayfield S.P. Light-regulated translation of chloroplast messenger RNAs through redox potential. Science 266 (1994) 1717-1719
    • (1994) Science , vol.266 , pp. 1717-1719
    • Danon, A.1    Mayfield, S.P.2
  • 17
    • 0033959891 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities
    • Trebitsh T., Levitan A., Sofer A., and Danon A. Translation of chloroplast psbA mRNA is modulated in the light by counteracting oxidizing and reducing activities. Mol. Cell. Biol. 20 (2000) 1116-1123
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1116-1123
    • Trebitsh, T.1    Levitan, A.2    Sofer, A.3    Danon, A.4
  • 18
    • 0035834001 scopus 로고    scopus 로고
    • Translation of chloroplast psbA mRNA is regulated by signals initiated by both photosystems II and I
    • Trebitsh T., and 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
  • 19
    • 0032516884 scopus 로고    scopus 로고
    • Light-dependent formation of the photosynthetic proton gradient regulates translation elongation in chloroplasts
    • Mühlbauer S.K., and Eichacker L.A. Light-dependent formation of the photosynthetic proton gradient regulates translation elongation in chloroplasts. J. Biol. Chem. 273 (1998) 20935-20940
    • (1998) J. Biol. Chem. , vol.273 , pp. 20935-20940
    • Mühlbauer, S.K.1    Eichacker, L.A.2
  • 20
    • 0034755289 scopus 로고    scopus 로고
    • RNA binding-proteins interact specifically with the Arabidopsis chloroplast psbA mRNA 5′ untranslated region in a redox-dependent manner
    • Shen Y., Danon A., and Christopher D.A. RNA binding-proteins interact specifically with the Arabidopsis chloroplast psbA mRNA 5′ untranslated region in a redox-dependent manner. Plant Cell Physiol. 42 (2001) 1071-1078
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1071-1078
    • Shen, Y.1    Danon, A.2    Christopher, D.A.3
  • 21
    • 0027404576 scopus 로고
    • ATP-dependent protein synthesis in isolated pea chloroplasts: evidence for accumulation of a translation intermediate of the D1 protein
    • Taniguchi M., Kuroda H., and Satoh K. ATP-dependent protein synthesis in isolated pea chloroplasts: evidence for accumulation of a translation intermediate of the D1 protein. FEBS Lett. 317 (1993) 57-61
    • (1993) FEBS Lett. , vol.317 , pp. 57-61
    • Taniguchi, M.1    Kuroda, H.2    Satoh, K.3
  • 23
    • 0003096040 scopus 로고
    • A rapid method for isolation of purified, physiologically active chloroplasts, used to study the intracellular distribution of amino acids in pea leaves
    • Mills W.R., and Joy K.W. A rapid method for isolation of purified, physiologically active chloroplasts, used to study the intracellular distribution of amino acids in pea leaves. Planta 148 (1980) 75-83
    • (1980) Planta , vol.148 , pp. 75-83
    • Mills, W.R.1    Joy, K.W.2
  • 24
    • 0001264924 scopus 로고
    • Transport of glycerate across the envelope membrane of isolated spinach chloroplasts
    • Robinson S.P. Transport of glycerate across the envelope membrane of isolated spinach chloroplasts. Plant Physiol. 70 (1982) 1032-1038
    • (1982) Plant Physiol. , vol.70 , pp. 1032-1038
    • Robinson, S.P.1
  • 25
    • 84981673172 scopus 로고
    • Criteria of intactness and the photosynthetic activity of spinach chloroplast preparations
    • Lilley R.M.C., Fitzgerald M.P., Rienits K.G., and Walker D.A. Criteria of intactness and the photosynthetic activity of spinach chloroplast preparations. New Phytol. 75 (1975) 1-10
    • (1975) New Phytol. , vol.75 , pp. 1-10
    • Lilley, R.M.C.1    Fitzgerald, M.P.2    Rienits, K.G.3    Walker, D.A.4
  • 26
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris
    • Arnon D.I. 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
  • 27
    • 0000785987 scopus 로고
    • Glycolaldehyde inhibits CO2 fixation in the cyanobacterium Synechococcus UTEX 625 without inhibiting the accumulation of inorganic carbon or the associated quenching of chlorophyll a fluorescence
    • Miller A.G., and Canvin D.T. Glycolaldehyde inhibits CO2 fixation in the cyanobacterium Synechococcus UTEX 625 without inhibiting the accumulation of inorganic carbon or the associated quenching of chlorophyll a fluorescence. Plant Physiol. 91 (1989) 1044-1049
    • (1989) Plant Physiol. , vol.91 , pp. 1044-1049
    • Miller, A.G.1    Canvin, D.T.2
  • 28
    • 0017862824 scopus 로고
    • Dicarboxylate transport across the inner membrane of chloroplast envelope
    • Lehner K., and Heldt H.W. Dicarboxylate transport across the inner membrane of chloroplast envelope. Biochim. Biophys. Acta 501 (1978) 531-544
    • (1978) Biochim. Biophys. Acta , vol.501 , pp. 531-544
    • Lehner, K.1    Heldt, H.W.2
  • 30
    • 27744454005 scopus 로고    scopus 로고
    • d-GLYCERATE 3-KINASE, the last unknown enzyme in the photorespiratory cycle in Arabidopsis, belongs to a novel kinase family
    • Boldt R., Edner C., Kolukisaoglu U., Hagemann M., Weckwerth W., Wienkoop S., Morgenthal K., and Bauwe H. d-GLYCERATE 3-KINASE, the last unknown enzyme in the photorespiratory cycle in Arabidopsis, belongs to a novel kinase family. Plant Cell 17 (2005) 2413-2420
    • (2005) Plant Cell , vol.17 , pp. 2413-2420
    • Boldt, R.1    Edner, C.2    Kolukisaoglu, U.3    Hagemann, M.4    Weckwerth, W.5    Wienkoop, S.6    Morgenthal, K.7    Bauwe, H.8
  • 32
    • 0001437511 scopus 로고
    • 2 in intact spinach chloroplasts: evidence for scavenging of hydrogen peroxide by peroxidase
    • 2 in intact spinach chloroplasts: evidence for scavenging of hydrogen peroxide by peroxidase. Plant Cell Physiol. 25 (1984) 1169-1179
    • (1984) Plant Cell Physiol. , vol.25 , pp. 1169-1179
    • Asada, K.1    Badger, M.R.2
  • 34
    • 0006602648 scopus 로고
    • Light-driven uptake of oxygen, carbon dioxide, and bicarbonate by the green alga Scenedesmus
    • Radmer R., and Ollinger O. Light-driven uptake of oxygen, carbon dioxide, and bicarbonate by the green alga Scenedesmus. Plant Physiol. 65 (1980) 723-729
    • (1980) Plant Physiol. , vol.65 , pp. 723-729
    • Radmer, R.1    Ollinger, O.2
  • 35
    • 23344454474 scopus 로고    scopus 로고
    • Modulation of photosynthetic electron transport in the absence of terminal electron acceptors: characterization of the rbcL deletion mutant of tobacco
    • Allahverdiyeva Y., Mamedov F., Mäenpää P., Vass I., and Aro E.M. Modulation of photosynthetic electron transport in the absence of terminal electron acceptors: characterization of the rbcL deletion mutant of tobacco. Biochim. Biophys. Acta 1709 (2005) 69-83
    • (2005) Biochim. Biophys. Acta , vol.1709 , pp. 69-83
    • Allahverdiyeva, Y.1    Mamedov, F.2    Mäenpää, P.3    Vass, I.4    Aro, E.M.5
  • 36
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons
    • Asada K. The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons. Annu. Rev. Plant Physiol. Plant Mol. Biol. 50 (1999) 601-639
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 601-639
    • Asada, K.1
  • 37
    • 0031747276 scopus 로고    scopus 로고
    • Oxygen reduction in the Mehler reaction is insufficient to protect photosystems I and II of leaves against photoinactivation
    • Wiese C., Shi L.B., and Heber U. Oxygen reduction in the Mehler reaction is insufficient to protect photosystems I and II of leaves against photoinactivation. Physiol. Plant. 102 (1998) 437-446
    • (1998) Physiol. Plant. , vol.102 , pp. 437-446
    • Wiese, C.1    Shi, L.B.2    Heber, U.3
  • 39
    • 0001569341 scopus 로고    scopus 로고
    • Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco
    • Feller U., Crafts-Brandner S.J., and Salvucci M.E. Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco. Plant Physiol. 116 (1998) 539-546
    • (1998) Plant Physiol. , vol.116 , pp. 539-546
    • Feller, U.1    Crafts-Brandner, S.J.2    Salvucci, M.E.3
  • 40
    • 0031400786 scopus 로고    scopus 로고
    • The two forms of ribulose-1,5-bisphospate carboxylase/oxygenase activase differ in sensitivity to elevated temperature
    • Crafts-Brandner S.J., van de Loo F.J., and Salvucci M.E. The two forms of ribulose-1,5-bisphospate carboxylase/oxygenase activase differ in sensitivity to elevated temperature. Plant Physiol. 114 (1997) 444-493
    • (1997) Plant Physiol. , vol.114 , pp. 444-493
    • Crafts-Brandner, S.J.1    van de Loo, F.J.2    Salvucci, M.E.3
  • 41
    • 2642712518 scopus 로고    scopus 로고
    • Effects of abiotic stresses on the turnover of the D1 reaction center II protein
    • Giardi M.T., Masojidek J., and Godde D. Effects of abiotic stresses on the turnover of the D1 reaction center II protein. Physiol. Plant. 101 (1997) 635-642
    • (1997) Physiol. Plant. , vol.101 , pp. 635-642
    • Giardi, M.T.1    Masojidek, J.2    Godde, D.3
  • 42
    • 0001219306 scopus 로고
    • The relationship between steady-state gas exchange of bean leaves and the levels of carbon-reduction-cycle intermediates
    • Badger M.R., Sharkey T.D., and von Caemmerer S. The relationship between steady-state gas exchange of bean leaves and the levels of carbon-reduction-cycle intermediates. Planta 160 (1984) 305-313
    • (1984) Planta , vol.160 , pp. 305-313
    • Badger, M.R.1    Sharkey, T.D.2    von Caemmerer, S.3
  • 43
    • 0001317256 scopus 로고
    • Mild water stress effects on carbon-reduction-cycle intermediates, ribulose bisphosphate carboxylase activity, and spatial homogeneity of photosynthesis in intact leaves
    • Sharkey T.D., and Seemann J.R. Mild water stress effects on carbon-reduction-cycle intermediates, ribulose bisphosphate carboxylase activity, and spatial homogeneity of photosynthesis in intact leaves. Plant Physiol. 89 (1989) 1060-1065
    • (1989) Plant Physiol. , vol.89 , pp. 1060-1065
    • Sharkey, T.D.1    Seemann, J.R.2
  • 44
    • 0032946768 scopus 로고    scopus 로고
    • The role of photorespiration during drought stress: an analysis utilizing barley mutants with reduced activities of photorespiratory enzymes
    • Wingler A., Quick W.P., Bungard R.A., Bailey K.J., Lea P.J., and Leegood R.C. The role of photorespiration during drought stress: an analysis utilizing barley mutants with reduced activities of photorespiratory enzymes. Plant Cell Environ. 22 (1999) 361-373
    • (1999) Plant Cell Environ. , vol.22 , pp. 361-373
    • Wingler, A.1    Quick, W.P.2    Bungard, R.A.3    Bailey, K.J.4    Lea, P.J.5    Leegood, R.C.6
  • 45
    • 1542351003 scopus 로고    scopus 로고
    • Repair machinery of symbiotic photosynthesis as the primary target of heat stress for reef-building corals
    • Takahashi S., Nakamura T., Sakamizu M., van Woesik R., and Yamasaki H. Repair machinery of symbiotic photosynthesis as the primary target of heat stress for reef-building corals. Plant Cell Physiol. 45 (2004) 251-255
    • (2004) Plant Cell Physiol. , vol.45 , pp. 251-255
    • Takahashi, S.1    Nakamura, T.2    Sakamizu, M.3    van Woesik, R.4    Yamasaki, H.5
  • 46
    • 0000747584 scopus 로고
    • Photoinhibition of photosynthesis in intact bean leaves: role of light and temperature, and requirement for chloroplast-protein synthesis during recovery
    • Greer D.H., Berry J.A., and Björkman O. Photoinhibition of photosynthesis in intact bean leaves: role of light and temperature, and requirement for chloroplast-protein synthesis during recovery. Planta 168 (1986) 253-260
    • (1986) Planta , vol.168 , pp. 253-260
    • Greer, D.H.1    Berry, J.A.2    Björkman, O.3
  • 47
    • 0036852140 scopus 로고    scopus 로고
    • Salt stress inhibits the repair of photodamaged photosystem II by suppressing the transcription and translation of psbA genes in Synechocystis
    • Allakhverdiev S.I., Nishiyama Y., Miyairi S., Yamamoto H., Inagaki N., Kanesaki Y., and Murata N. Salt stress inhibits the repair of photodamaged photosystem II by suppressing the transcription and translation of psbA genes in Synechocystis. Plant Physiol. 130 (2002) 1443-1453
    • (2002) Plant Physiol. , vol.130 , pp. 1443-1453
    • Allakhverdiev, S.I.1    Nishiyama, Y.2    Miyairi, S.3    Yamamoto, H.4    Inagaki, N.5    Kanesaki, Y.6    Murata, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.