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Volumn 1657, Issue 1, 2004, Pages 23-32

Environmental stress inhibits the synthesis de novo of proteins involved in the photodamage-repair cycle of Photosystem II in Synechocystis sp. PCC 6803

Author keywords

1,4 benzoquinone; BQ; Chl; chlorophyll; D1 protein; Environmental stress; Photodamage and repair; Photosystem II; PSII; Synechocystis PCC6803

Indexed keywords

PROTEIN; PROTEIN D1; UNCLASSIFIED DRUG;

EID: 3042679202     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.03.003     Document Type: Article
Times cited : (364)

References (48)
  • 1
    • 84930712146 scopus 로고
    • On the inhibition of photosynthesis by intense light
    • Kok B. On the inhibition of photosynthesis by intense light. Biochim. Biophys. Acta. 21:1956;234-244
    • (1956) Biochim. Biophys. Acta , vol.21 , pp. 234-244
    • Kok, B.1
  • 2
    • 0003050958 scopus 로고
    • Photoinhibition of photosynthesis induced by visible light
    • Powles S.B. Photoinhibition of photosynthesis induced by visible light. Annu. Rev. Plant Physiol. 35:1994;15-44
    • (1994) Annu. Rev. Plant Physiol. , vol.35 , pp. 15-44
    • Powles, S.B.1
  • 3
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem: II. Inactivation, protein damage and turnover
    • Aro E.-M., Virgin I., 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
  • 4
    • 0021473380 scopus 로고
    • Membrane protein damage and repair: Removal and replacement of inactivated 32-kilodalton polypeptide in chloroplast membranes
    • Ohad I., Kyle D.J., Arntzen C.J. Membrane protein damage and repair: removal and replacement of inactivated 32-kilodalton polypeptide 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
  • 6
    • 0001449340 scopus 로고
    • Membrane protein damage and repair: Selective loss of a quinone protein function in chloroplast membranes
    • Kyle D.J., Ohad I., Arntzen C.J. Membrane protein damage and repair: selective loss of a quinone protein function in chloroplast membranes. Proc. Natl. Acad. Sci. U. S. A. 81:1984;4070-4074
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 4070-4074
    • Kyle, D.J.1    Ohad, I.2    Arntzen, C.J.3
  • 7
    • 0032541967 scopus 로고    scopus 로고
    • Relationship between activity, D1 loss, and Mn binding in photoinhibition of photosystem II
    • Krieger A., Rutherford A.W., Vass I., Hedeg E. Relationship between activity, D1 loss, and Mn binding in photoinhibition of photosystem II. Biochemistry. 37:1998;16262-16269
    • (1998) Biochemistry , vol.37 , pp. 16262-16269
    • Krieger, A.1    Rutherford, A.W.2    Vass, I.3    Hedeg, E.4
  • 8
    • 0025816302 scopus 로고
    • D1 protein degradation during photoinhibition of intact leaves: A modification of the D1 protein precedes degradation
    • Kettunen R., Tyystjärvi E., Aro E.-M. D1 protein degradation during photoinhibition of intact leaves: a modification of the D1 protein precedes degradation. FEBS Lett. 290:1991;153-156
    • (1991) FEBS Lett. , vol.290 , pp. 153-156
    • Kettunen, R.1    Tyystjärvi, E.2    Aro, E.-M.3
  • 9
    • 0001596491 scopus 로고    scopus 로고
    • A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II
    • Haußühl K., Andersson B., Adamska I. A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II. EMBO J. 20:2001;713-722
    • (2001) EMBO J. , vol.20 , pp. 713-722
    • Haußühl, K.1    Andersson, B.2    Adamska, I.3
  • 10
    • 0034031132 scopus 로고    scopus 로고
    • The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
    • Lindahl M., Spetea C., Hundal T., Oppenheim A.B., Adam Z., Andersson B. The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein. Plant Cell. 12:2000;419-431
    • (2000) Plant Cell , vol.12 , pp. 419-431
    • Lindahl, M.1    Spetea, C.2    Hundal, T.3    Oppenheim, A.B.4    Adam, Z.5    Andersson, B.6
  • 11
    • 0031712075 scopus 로고    scopus 로고
    • Massive breakdown of the photosystem II polypeptides in a mutant of the cyanobacterium Synechocystis sp. PCC 6803
    • Kanervo E., Murata N., Aro E.-M. Massive breakdown of the photosystem II polypeptides in a mutant of the cyanobacterium Synechocystis sp. PCC 6803. Photosynth. Res. 57:1998;81-91
    • (1998) Photosynth. Res. , vol.57 , pp. 81-91
    • Kanervo, E.1    Murata, N.2    Aro, E.-M.3
  • 13
    • 0026734343 scopus 로고
    • Transcriptional and posttranscriptional components of psbA response to high light intensity in Synechococcus sp. strain PCC 7942
    • Kulkarni R.D., Schaefer M.R., Golden S.S. Transcriptional and posttranscriptional components of psbA response to high light intensity in Synechococcus sp. strain PCC 7942. J. Bacteriol. 174:1992;3775-3781
    • (1992) J. Bacteriol. , vol.174 , pp. 3775-3781
    • Kulkarni, R.D.1    Schaefer, M.R.2    Golden, S.S.3
  • 14
    • 0034144409 scopus 로고    scopus 로고
    • Redox control of psbA gene expression in the cyanobacterium Synechocystis sp. PCC 6803. Involvement of the cytochrome b(6)/f complex
    • Alfonso M., Perewoska I., Kirilovsky D. Redox control of psbA gene expression in the cyanobacterium Synechocystis sp. PCC 6803. Involvement of the cytochrome b(6)/f complex. Plant Physiol. 122:2000;505-516
    • (2000) Plant Physiol. , vol.122 , pp. 505-516
    • Alfonso, M.1    Perewoska, I.2    Kirilovsky, D.3
  • 15
    • 0027397937 scopus 로고
    • Adaptation of cyanobacteria to environmental stimuli: New steps towards molecular mechanisms
    • Tandeau de Marsac N., Houmard J. Adaptation of cyanobacteria to environmental stimuli: new steps towards molecular mechanisms. FEMS Microbiol. Rev. 104:1993;119-190
    • (1993) FEMS Microbiol. Rev. , vol.104 , pp. 119-190
    • Tandeau De Marsac, N.1    Houmard, J.2
  • 17
    • 3042619075 scopus 로고    scopus 로고
    • www.kazusa.or.jp/cyano.html.
  • 18
    • 0036935397 scopus 로고    scopus 로고
    • The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts
    • Sokolenko A., Pojidaeva E., Zinchenko V., Panichkin V., Glaser V.M., Herrmann R.G., Shestakov S.V. The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts. Curr. Genet. 41:2002;291-310
    • (2002) Curr. Genet. , vol.41 , pp. 291-310
    • Sokolenko, A.1    Pojidaeva, E.2    Zinchenko, V.3    Panichkin, V.4    Glaser, V.M.5    Herrmann, R.G.6    Shestakov, S.V.7
  • 19
    • 0034058872 scopus 로고    scopus 로고
    • Degradation of the photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocystis PCC 6803 varying with respect to the type and level of psbA transcript
    • Komenda J., Hassan H.A., Diner B.A., Debus R.J., Barber J., Nixon P.J. Degradation of the photosystem II D1 and D2 proteins in different strains of the cyanobacterium Synechocystis PCC 6803 varying with respect to the type and level of psbA transcript. Plant Mol. Biol. 42:2000;635-645
    • (2000) Plant Mol. Biol. , vol.42 , pp. 635-645
    • Komenda, J.1    Hassan, H.A.2    Diner, B.A.3    Debus, R.J.4    Barber, J.5    Nixon, P.J.6
  • 20
    • 0000794417 scopus 로고
    • Photoinhibition of photosynthesis in willow leaves under field conditions
    • Ogren E. Photoinhibition of photosynthesis in willow leaves under field conditions. Planta. 175:1988;229-236
    • (1988) Planta , vol.175 , pp. 229-236
    • Ogren, E.1
  • 21
    • 0025995077 scopus 로고
    • Effects of cold-acclimation on the susceptibility of photosynthesis to photoinhibition in Scots pine and in winter and spring cereals: A fluorescence analysis
    • Oquist G., Huner N.P.A. Effects of cold-acclimation on the susceptibility of photosynthesis to photoinhibition in Scots pine and in winter and spring cereals: a fluorescence analysis. Funct. Ecol. 5:1991;91-100
    • (1991) Funct. Ecol. , vol.5 , pp. 91-100
    • Oquist, G.1    Huner, N.P.A.2
  • 22
    • 0033545998 scopus 로고    scopus 로고
    • Genetic engineering of the unsaturation of fatty acids in membrane lipids alters the tolerance of Synechocystis to salt stress
    • Allakhverdiev S.I., Nishiyama Y., Suzuki I., Tasaka Y., Murata N. Genetic engineering of the unsaturation of fatty acids in membrane lipids alters the tolerance of Synechocystis to salt stress. Proc. Natl. Acad. Sci. U. S. A. 96:1999;5862-5867
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5862-5867
    • Allakhverdiev, S.I.1    Nishiyama, Y.2    Suzuki, I.3    Tasaka, Y.4    Murata, N.5
  • 23
    • 0035028257 scopus 로고    scopus 로고
    • Unsaturated fatty acids in membrane lipids protect the photosynthetic machinery against salt-induced damage in Synechococcus
    • Allakhverdiev S.I., Kinoshita M., Inaba M., Suzuki I., Murata N. Unsaturated fatty acids in membrane lipids protect the photosynthetic machinery against salt-induced damage in Synechococcus. Plant Physiol. 125:2001;1842-1853
    • (2001) Plant Physiol. , vol.125 , pp. 1842-1853
    • Allakhverdiev, S.I.1    Kinoshita, M.2    Inaba, M.3    Suzuki, I.4    Murata, N.5
  • 24
    • 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., 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
  • 25
    • 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., 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
  • 26
    • 0029015587 scopus 로고
    • Photoinactivation of photosystem II induces changes in the photochemical reaction center II abolishing the regulatory role of the QB site in the D1 protein degradation
    • Zer H., Ohad I. Photoinactivation of photosystem II induces changes in the photochemical reaction center II abolishing the regulatory role of the QB site in the D1 protein degradation. Eur. J. Biochem. 231:1995;448-453
    • (1995) Eur. J. Biochem. , vol.231 , pp. 448-453
    • Zer, H.1    Ohad, I.2
  • 28
    • 0028131199 scopus 로고
    • Singlet oxygen and free radical production during acceptor- and donor-side-induced photoinhibition. Studies with spin trapping EPR spectroscopy
    • Hideg E., Spetea C., Vass I. Singlet oxygen and free radical production during acceptor- and donor-side-induced photoinhibition. Studies with spin trapping EPR spectroscopy. Biochim. Biophys. Acta. 1186:1994;143-152
    • (1994) Biochim. Biophys. Acta , vol.1186 , pp. 143-152
    • Hideg, E.1    Spetea, C.2    Vass, I.3
  • 29
    • 0028181717 scopus 로고
    • The isolated photosynthetic reaction center of PSII as a sensitiser for the formation of singlet oxygen; Detection and quantum yield determination using a chemical trapping technique
    • Telfer A., Bishop S.M., Phillips D., Barber J. The isolated photosynthetic reaction center of PSII as a sensitiser for the formation of singlet oxygen; detection and quantum yield determination using a chemical trapping technique. J. Biol. Chem. 269:1994;13244-13253
    • (1994) J. Biol. Chem. , vol.269 , pp. 13244-13253
    • Telfer, A.1    Bishop, S.M.2    Phillips, D.3    Barber, J.4
  • 30
    • 0029891761 scopus 로고    scopus 로고
    • Selective and specific cleavage of the D1 and D2 proteins of photosystem II by exposure to singlet oxygen: Factors responsible for the susceptibility to cleavage of the proteins
    • Okada K., Ikeuchi M., Yamamoto N., Ono T., Miyao M. Selective and specific cleavage of the D1 and D2 proteins of photosystem II by exposure to singlet oxygen: factors responsible for the susceptibility to cleavage of the proteins. Biochim. Biophys. Acta. 1274:1996;73-79
    • (1996) Biochim. Biophys. Acta , vol.1274 , pp. 73-79
    • Okada, K.1    Ikeuchi, M.2    Yamamoto, N.3    Ono, T.4    Miyao, M.5
  • 31
    • 0028606359 scopus 로고
    • The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane lipids: A mechanism of chilling tolerance
    • Gombos Z., Wada H., Murata N. 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. U. S. A. 91:1994;8787-8791
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 8787-8791
    • Gombos, Z.1    Wada, H.2    Murata, N.3
  • 32
    • 0031177711 scopus 로고    scopus 로고
    • Membrane lipid unsaturation modulates processing of the photosystem II reaction center protein D1 at low temperatures
    • Kanervo E., Tasaka Y., Murata N., Aro E.-M. Membrane lipid unsaturation modulates processing of the photosystem II reaction center protein D1 at low temperatures. Plant Physiol. 114:1997;841-849
    • (1997) Plant Physiol. , vol.114 , pp. 841-849
    • Kanervo, E.1    Tasaka, Y.2    Murata, N.3    Aro, E.-M.4
  • 33
    • 0015076683 scopus 로고
    • Purification and properties of unicellular blue-green algae (order Chroococcales)
    • Stanier R.Y., Kunisawa R., Mandel M., Cohen-Bazire G. Purification and properties of unicellular blue-green algae (order Chroococcales). Bacteriol. Rev. 35:1971;171-205
    • (1971) Bacteriol. Rev. , vol.35 , pp. 171-205
    • Stanier, R.Y.1    Kunisawa, R.2    Mandel, M.3    Cohen-Bazire, G.4
  • 34
    • 0001322840 scopus 로고
    • Chilling susceptibility of the blue-green alga Anacystis nidulans: Effect of growth temperature
    • Ono T., Murata N. Chilling susceptibility of the blue-green alga Anacystis nidulans: effect of growth temperature. Plant Physiol. 67:1981;176-182
    • (1981) Plant Physiol. , vol.67 , pp. 176-182
    • Ono, T.1    Murata, N.2
  • 35
    • 24844436650 scopus 로고
    • Photochemical activity and components of membrane preparations from blue-green algae: Coexistence of two photosystems in relation to chlorophyll a and removal of phycocyanin
    • Arnon D.I., McSwain B.D., Tsujimoto H.Y., Wada K. Photochemical activity and components of membrane preparations from blue-green algae: coexistence of two photosystems in relation to chlorophyll a and removal of phycocyanin. Biochim. Biophys. Acta. 1143:1974;113-134
    • (1974) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Arnon, D.I.1    McSwain, B.D.2    Tsujimoto, H.Y.3    Wada, K.4
  • 36
    • 0033996023 scopus 로고    scopus 로고
    • Inactivation of photosystems I and II in response to osmotic stress in Synechococcus. Contribution of water channels
    • Allakhverdiev S.I., Sakamoto A., Nishiyama Y., Murata N. Inactivation of photosystems I and II in response to osmotic stress in Synechococcus. Contribution of water channels. Plant Physiol. 122:2000;1201-1208
    • (2000) Plant Physiol. , vol.122 , pp. 1201-1208
    • Allakhverdiev, S.I.1    Sakamoto, A.2    Nishiyama, Y.3    Murata, N.4
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0027207811 scopus 로고
    • Recognition signal for the C-terminal processing protease of D1 precursor protein in the photosystem II reaction center: An analysis using synthetic oligopeptides
    • Taguchi F., Yamamoto Y., Inagaki N., Satoh K. Recognition signal for the C-terminal processing protease of D1 precursor protein in the photosystem II reaction center: an analysis using synthetic oligopeptides. FEBS Lett. 326:1993;227-231
    • (1993) FEBS Lett. , vol.326 , pp. 227-231
    • Taguchi, F.1    Yamamoto, Y.2    Inagaki, N.3    Satoh, K.4
  • 39
    • 0029921367 scopus 로고    scopus 로고
    • The rate constant of photoinhibition, measured in lincomycin-treated leaves, is directly proportional to light intensity
    • Tyystjärvi E., Aro E.-M. The rate constant of photoinhibition, measured in lincomycin-treated leaves, is directly proportional to light intensity. Proc. Natl. Acad. Sci. U. S. A. 93:1996;2213-2218
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 2213-2218
    • Tyystjärvi, E.1    Aro, E.-M.2
  • 40
    • 0035119817 scopus 로고    scopus 로고
    • Photoinactivation of photosystem II complexes and photoprotection by non-functional neighbours in Capsicum annuum L. leaves
    • Lee H.Y., Hong Y.N., Chow W.S. Photoinactivation of photosystem II complexes and photoprotection by non-functional neighbours in Capsicum annuum L. leaves. Planta. 212:2001;332-342
    • (2001) Planta , vol.212 , pp. 332-342
    • Lee, H.Y.1    Hong, Y.N.2    Chow, W.S.3
  • 41
    • 84914603936 scopus 로고
    • Salinity-stress enhances photoinhibition of photosystem II in Chlamydomonas reinhardtii
    • Neale P.J., Melis A. Salinity-stress enhances photoinhibition of photosystem II in Chlamydomonas reinhardtii. J. Plant Physiol. 134:1989;619-622
    • (1989) J. Plant Physiol. , vol.134 , pp. 619-622
    • Neale, P.J.1    Melis, A.2
  • 42
    • 0033427597 scopus 로고    scopus 로고
    • Effects of salt stress on PSII function and photoinhibition in the cyanobacterium Spirulina platensis
    • Lu C.-M., Zhang J.-H. Effects of salt stress on PSII function and photoinhibition in the cyanobacterium Spirulina platensis. J. Plant Physiol. 155:1999;740-745
    • (1999) J. Plant Physiol. , vol.155 , pp. 740-745
    • Lu, C.-M.1    Zhang, J.-H.2
  • 44
    • 0035040683 scopus 로고    scopus 로고
    • Regulation of translation elongation in cyanobacteria: Membrane targeting of the ribosome nascent-chain complexes controls the synthesis of D1 protein
    • Tyystjärvi T., Herranen M., Aro E.-M. Regulation of translation elongation in cyanobacteria: membrane targeting of the ribosome nascent-chain complexes controls the synthesis of D1 protein. Mol. Microbiol. 40:2001;1-10
    • (2001) Mol. Microbiol. , vol.40 , pp. 1-10
    • Tyystjärvi, T.1    Herranen, M.2    Aro, E.-M.3
  • 45
    • 0000854319 scopus 로고
    • Construction of an obligate photoheterotrophic mutant of the cyanobacterium Synechocystis sp. PCC 6803
    • Jansson C., Debus R.J., Osiewacz H.D., Gurevitz M., McIntosh L. Construction of an obligate photoheterotrophic mutant of the cyanobacterium Synechocystis sp. PCC 6803. Plant Physiol. 85:1987;1021-1025
    • (1987) Plant Physiol. , vol.85 , pp. 1021-1025
    • Jansson, C.1    Debus, R.J.2    Osiewacz, H.D.3    Gurevitz, M.4    McIntosh, L.5
  • 46
    • 0024869570 scopus 로고
    • Influence of light on accumulation of photosynthesis-specific transcripts in the cyanobacterium Synechocystis 6803
    • Mohamed A., Jansson C. Influence of light on accumulation of photosynthesis-specific transcripts in the cyanobacterium Synechocystis 6803. Plant Mol. Biol. 13:1989;693-700
    • (1989) Plant Mol. Biol. , vol.13 , pp. 693-700
    • Mohamed, A.1    Jansson, C.2
  • 47
    • 0027324796 scopus 로고
    • Differential expression of the psbA genes in the cyanobacterium Synechocystis 6803
    • Mohamed A., Eriksson J., Osiewacz H.D., Jansson C. Differential expression of the psbA genes in the cyanobacterium Synechocystis 6803. Mol. Gen. Genet. 238:1993;161-168
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 161-168
    • Mohamed, A.1    Eriksson, J.2    Osiewacz, H.D.3    Jansson, C.4
  • 48
    • 0027354590 scopus 로고
    • Analysis of the function of the two homologous copies of the psbA gene in Synechocystis PCC 6714 and 6803
    • Bouyoub A., Vernotte C., Astier C. Analysis of the function of the two homologous copies of the psbA gene in Synechocystis PCC 6714 and 6803. Plant Mol. Biol. 21:1993;249-258
    • (1993) Plant Mol. Biol. , vol.21 , pp. 249-258
    • Bouyoub, A.1    Vernotte, C.2    Astier, C.3


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