메뉴 건너뛰기




Volumn 156, Issue 4, 2011, Pages 1934-1954

Light history influences the response of the marine cyanobacterium Synechococcus sp. WH7803 to oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

SYNECHOCOCCUS; SYNECHOCOCCUS ELONGATUS PCC 6301; SYNECHOCOCCUS SP.;

EID: 79961186172     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.111.174714     Document Type: Article
Times cited : (44)

References (150)
  • 1
    • 0041851885 scopus 로고    scopus 로고
    • Photoinhibition: A historical perspective
    • Adir N, Zer H, Shochat S, Ohad I (2003) Photoinhibition: a historical perspective. Photosynth Res 76: 343-370
    • (2003) Photosynth Res , vol.76 , pp. 343-370
    • Adir, N.1    Zer, H.2    Shochat, S.3    Ohad, I.4
  • 2
    • 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 SI, Murata N (2004) 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: 23-32
    • (2004) Biochim Biophys Acta , vol.1657 , pp. 23-32
    • Allakhverdiev, S.I.1    Murata, N.2
  • 4
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II: Inactivation, protein damage and turnover
    • Aro E-M, Virgin I, Andersson B (1993) Photoinhibition of photosystem II: inactivation, protein damage and turnover. Biochim Biophys Acta 1143: 113-134
    • (1993) Biochim Biophys Acta , vol.1143 , pp. 113-134
    • Aro, E.-M.1    Virgin, I.2    Andersson, B.3
  • 5
    • 0002844238 scopus 로고
    • Production and action of active oxygen species in photosynthetic tissues
    • In CH Foyer, PM Mullineaux, CRC Press, Boca Raton, FL
    • Asada K (1994) Production and action of active oxygen species in photosynthetic tissues. In CH Foyer, PM Mullineaux, eds, Causes of Photo-Oxidative Stress and Amelioration of Defense Systems in Plants. CRC Press, Boca Raton, FL, pp 77-104
    • (1994) Causes of Photo-Oxidative Stress and Amelioration of Defense Systems In Plants , pp. 77-104
    • Asada, K.1
  • 6
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons
    • Asada K (1999) The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons. Annu Rev Plant Physiol Plant Mol Biol 50: 601-639
    • (1999) Annu Rev Plant Physiol Plant Mol Biol , vol.50 , pp. 601-639
    • Asada, K.1
  • 7
    • 33750071088 scopus 로고    scopus 로고
    • The deg proteases protect Synechocystis sp. PCC 6803 during heat and light stresses but are not essential for removal of damaged D1 protein during the photosystem two repair cycle
    • Barker M, de Vries R, Nield J, Komenda J, Nixon PJ (2006) The deg proteases protect Synechocystis sp. PCC 6803 during heat and light stresses but are not essential for removal of damaged D1 protein during the photosystem two repair cycle. J Biol Chem 281: 30347-30355
    • (2006) J Biol Chem , vol.281 , pp. 30347-30355
    • Barker, M.1    de Vries, R.2    Nield, J.3    Komenda, J.4    Nixon, P.J.5
  • 8
    • 78149364258 scopus 로고    scopus 로고
    • Dynamic changes in the proteome of Synechocystis 6803 in response to CO(2) limitation revealed by quantitative proteomics
    • Battchikova N, Vainonen JP, Vorontsova N, Keranen M, Carmel D, Aro EM (2010) Dynamic changes in the proteome of Synechocystis 6803 in response to CO(2) limitation revealed by quantitative proteomics. J Proteome Res 9: 5896-5912
    • (2010) J Proteome Res , vol.9 , pp. 5896-5912
    • Battchikova, N.1    Vainonen, J.P.2    Vorontsova, N.3    Keranen, M.4    Carmel, D.5    Aro, E.M.6
  • 9
    • 0028944579 scopus 로고
    • Cyclic photophosphorylation and electron-transport
    • Bendall DS, Manasse RS (1995) Cyclic photophosphorylation and electron-transport. Biochim Biophys Acta 1229: 23-38
    • (1995) Biochim Biophys Acta , vol.1229 , pp. 23-38
    • Bendall, D.S.1    Manasse, R.S.2
  • 11
    • 17744364362 scopus 로고    scopus 로고
    • Effects of UV-B radiation on the D1 protein repair cycle of natural phytoplankton communities from three latitudes (Canada, Brazil, and Argentina)
    • Bouchard JN, Campbell DA, Roy S (2005) Effects of UV-B radiation on the D1 protein repair cycle of natural phytoplankton communities from three latitudes (Canada, Brazil, and Argentina). J Phycol 41: 273-286
    • (2005) J Phycol , vol.41 , pp. 273-286
    • Bouchard, J.N.1    Campbell, D.A.2    Roy, S.3
  • 12
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan BB, Balmer Y (2005) Redox regulation: a broadening horizon. Annu Rev Plant Biol 56: 187-220
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 13
    • 0021288059 scopus 로고
    • Paraquat: Model for oxidant-initiated toxicity
    • Bus JS, Gibson JE (1984) Paraquat: model for oxidant-initiated toxicity. Environ Health Perspect 55: 37-46
    • (1984) Environ Health Perspect , vol.55 , pp. 37-46
    • Bus, J.S.1    Gibson, J.E.2
  • 15
    • 0031940159 scopus 로고    scopus 로고
    • The cyanobacterium Synechococcus resists UV-B by exchanging photosystem II reaction-center D1 proteins
    • Campbell D, Eriksson MJ, Oquist G, Gustafsson P, Clarke AK (1998) The cyanobacterium Synechococcus resists UV-B by exchanging photosystem II reaction-center D1 proteins. Proc Natl Acad Sci USA 95: 364-369
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 364-369
    • Campbell, D.1    Eriksson, M.J.2    Oquist, G.3    Gustafsson, P.4    Clarke, A.K.5
  • 16
    • 0028822239 scopus 로고
    • Electron transport regulates exchange of two forms of photosystem II D1 protein in the cyanobacterium Synechococcus
    • Campbell D, Zhou GQ, Gustafsson P, Oquist G, Clarke AK (1995) Electron transport regulates exchange of two forms of photosystem II D1 protein in the cyanobacterium Synechococcus. EMBO J 14: 5457-5466
    • (1995) EMBO J , vol.14 , pp. 5457-5466
    • Campbell, D.1    Zhou, G.Q.2    Gustafsson, P.3    Oquist, G.4    Clarke, A.K.5
  • 17
    • 0026496536 scopus 로고
    • Photoinhibition of hydroxylamineextracted photosystem II membranes: Studies of the mechanism
    • Chen GX, Kazimir J, Cheniae GM (1992) Photoinhibition of hydroxylamineextracted photosystem II membranes: studies of the mechanism. Biochemistry 31: 11072-11083
    • (1992) Biochemistry , vol.31 , pp. 11072-11083
    • Chen, G.X.1    Kazimir, J.2    Cheniae, G.M.3
  • 18
    • 77953809155 scopus 로고    scopus 로고
    • The multifaceted capacity of Dps proteins to combat bacterial stress conditions: Detoxification of iron and hydrogen peroxide and DNA binding
    • Chiancone E, Ceci P (2010) The multifaceted capacity of Dps proteins to combat bacterial stress conditions: detoxification of iron and hydrogen peroxide and DNA binding. Biochim Biophys Acta 1800: 798-805
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 798-805
    • Chiancone, E.1    Ceci, P.2
  • 19
    • 0027144078 scopus 로고
    • Two functionally distinct forms of the photosystem II reaction-center protein D1 in the cyanobacterium Synechococcus sp. PCC 7942
    • Clarke AK, Hurry VM, Gustafsson P, Oquist G (1993a) Two functionally distinct forms of the photosystem II reaction-center protein D1 in the cyanobacterium Synechococcus sp. PCC 7942. Proc Natl Acad Sci USA 90: 11985-11989
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11985-11989
    • Clarke, A.K.1    Hurry, V.M.2    Gustafsson, P.3    Oquist, G.4
  • 20
    • 0027425573 scopus 로고
    • Rapid interchange between two distinct forms of cyanobacterial photosystem II reactioncenter protein D1 in response to photoinhibition
    • Clarke AK, Soitamo A, Gustafsson P, Oquist G (1993b) Rapid interchange between two distinct forms of cyanobacterial photosystem II reactioncenter protein D1 in response to photoinhibition. Proc Natl Acad Sci USA 90: 9973-9977
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9973-9977
    • Clarke, A.K.1    Soitamo, A.2    Gustafsson, P.3    Oquist, G.4
  • 21
    • 0034977905 scopus 로고    scopus 로고
    • Succinate dehydrogenase and other respiratory pathways in thylakoid membranes of Synechocystis sp. Strain PCC 6803: Capacity comparisons and physiological function
    • Cooley JW, Vermaas WFJ (2001) Succinate dehydrogenase and other respiratory pathways in thylakoid membranes of Synechocystis sp. Strain PCC 6803: capacity comparisons and physiological function. J Bacteriol 183: 4251-4258
    • (2001) J Bacteriol , vol.183 , pp. 4251-4258
    • Cooley, J.W.1    Vermaas, W.F.J.2
  • 22
    • 0035023305 scopus 로고    scopus 로고
    • Comparative gene expression profiles following UV exposure in wildtype and SOS-deficient Escherichia coli
    • Courcelle J, Khodursky A, Peter B, Brown PO, Hanawalt PC (2001) Comparative gene expression profiles following UV exposure in wildtype and SOS-deficient Escherichia coli. Genetics 158: 41-64
    • (2001) Genetics , vol.158 , pp. 41-64
    • Courcelle, J.1    Khodursky, A.2    Peter, B.3    Brown, P.O.4    Hanawalt, P.C.5
  • 24
    • 33746932518 scopus 로고    scopus 로고
    • Activation of superoxide dismutases: Putting the metal to the pedal
    • Culotta VC, Yang M, O'Halloran TV (2006) Activation of superoxide dismutases: putting the metal to the pedal. Biochim Biophys Acta 1763: 747-758
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 747-758
    • Culotta, V.C.1    Yang, M.2    O'Halloran, T.V.3
  • 25
    • 45949115903 scopus 로고
    • Light-induced oxidation of the acceptorside Fe(II) of photosystem-II by exogenous quinines acting through the QB binding-site. 2. Blockage by inhibitors and their effects on the Fe(III) electron-paramagnetic-res spectra
    • Diner BA, Petrouleas V (1987) Light-induced oxidation of the acceptorside Fe(II) of photosystem-II by exogenous quinines acting through the QB binding-site. 2. Blockage by inhibitors and their effects on the Fe(III) electron-paramagnetic-res spectra. Biochim Biophys Acta 893: 138-148
    • (1987) Biochim Biophys Acta , vol.893 , pp. 138-148
    • Diner, B.A.1    Petrouleas, V.2
  • 26
    • 3142559798 scopus 로고    scopus 로고
    • Function and regulation of the cyanobacterial genes lexA, recA and ruvB: LexA is critical to the survival of cells facing inorganic carbon starvation
    • Domain F, Houot L, Chauvat F, Cassier-Chauvat C (2004) Function and regulation of the cyanobacterial genes lexA, recA and ruvB: lexA is critical to the survival of cells facing inorganic carbon starvation. Mol Microbiol 53: 65-80
    • (2004) Mol Microbiol , vol.53 , pp. 65-80
    • Domain, F.1    Houot, L.2    Chauvat, F.3    Cassier-Chauvat, C.4
  • 29
    • 0036910689 scopus 로고    scopus 로고
    • Immunocytochemical localization of the stress-induced DpsA protein in the cyanobacterium Synechococcus sp. strain PCC 7942
    • Durham KA, Bullerjahn GS (2002) Immunocytochemical localization of the stress-induced DpsA protein in the cyanobacterium Synechococcus sp. strain PCC 7942. J Basic Microbiol 42: 367-372
    • (2002) J Basic Microbiol , vol.42 , pp. 367-372
    • Durham, K.A.1    Bullerjahn, G.S.2
  • 30
    • 57849101491 scopus 로고    scopus 로고
    • D1-protein dynamics in photosystem II: The lingering enigma
    • Edelman M, Mattoo AK (2008) D1-protein dynamics in photosystem II: the lingering enigma. Photosynth Res 98: 609-620
    • (2008) Photosynth Res , vol.98 , pp. 609-620
    • Edelman, M.1    Mattoo, A.K.2
  • 32
    • 70450235338 scopus 로고    scopus 로고
    • Novel effects of methyl viologen on photosystem II function in spinach leaves
    • Fan DY, Jia HS, Barber J, Chow WS (2009) Novel effects of methyl viologen on photosystem II function in spinach leaves. Eur Biophys J 39: 191-199
    • (2009) Eur Biophys J , vol.39 , pp. 191-199
    • Fan, D.Y.1    Jia, H.S.2    Barber, J.3    Chow, W.S.4
  • 33
    • 0025164943 scopus 로고
    • The sites of electron donation of photosystem-I to methyl viologen
    • Fujii T, Yokoyama E, Inoue K, Sakurai H (1990) The sites of electron donation of photosystem-I to methyl viologen. Biochim Biophys Acta 1015: 41-48
    • (1990) Biochim Biophys Acta , vol.1015 , pp. 41-48
    • Fujii, T.1    Yokoyama, E.2    Inoue, K.3    Sakurai, H.4
  • 34
    • 0033587579 scopus 로고    scopus 로고
    • A cyanobacterial gene family coding for singlehelix proteins resembling part of the light-harvesting proteins from higher plants
    • Funk C, Vermaas W (1999) A cyanobacterial gene family coding for singlehelix proteins resembling part of the light-harvesting proteins from higher plants. Biochemistry 38: 9397-9404
    • (1999) Biochemistry , vol.38 , pp. 9397-9404
    • Funk, C.1    Vermaas, W.2
  • 35
    • 51449089207 scopus 로고    scopus 로고
    • Function and evolution of the psbA gene family in marine Synechococcus: Synechococcus sp. WH7803 as a case study
    • Garczarek L, Dufresne A, Blot N, Cockshutt AM, Peyrat A, Campbell DA, Joubin L, Six C (2008) Function and evolution of the psbA gene family in marine Synechococcus: Synechococcus sp. WH7803 as a case study. ISME J 2: 937-953
    • (2008) ISME J , vol.2 , pp. 937-953
    • Garczarek, L.1    Dufresne, A.2    Blot, N.3    Cockshutt, A.M.4    Peyrat, A.5    Campbell, D.A.6    Joubin, L.7    Six, C.8
  • 37
    • 0036098201 scopus 로고    scopus 로고
    • Kinetics of paraquat and copper reactions with nitroxides: The effects of nitroxides on the aerobic and anoxic toxicity of paraquat
    • Goldstein S, Samuni A, Aronovitch Y, Godinger D, Russo A, Mitchell JB (2002) Kinetics of paraquat and copper reactions with nitroxides: the effects of nitroxides on the aerobic and anoxic toxicity of paraquat. Chem Res Toxicol 15: 686-691
    • (2002) Chem Res Toxicol , vol.15 , pp. 686-691
    • Goldstein, S.1    Samuni, A.2    Aronovitch, Y.3    Godinger, D.4    Russo, A.5    Mitchell, J.B.6
  • 38
    • 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, Tyystjärvi E (2005) Evidence for the role of the oxygen-evolving manganese complex in photoinhibition of photosystem II. Biochim Biophys Acta 1706: 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
  • 39
    • 0037422403 scopus 로고    scopus 로고
    • Elimination of highlight- inducible polypeptides related to eukaryotic chlorophyll a/bbinding proteins results in aberrant photoacclimation in Synechocystis PCC6803
    • Havaux M, Guedeney G, He Q, Grossman AR (2003) Elimination of highlight- inducible polypeptides related to eukaryotic chlorophyll a/bbinding proteins results in aberrant photoacclimation in Synechocystis PCC6803. Biochim Biophys Acta 1557: 21-33
    • (2003) Biochim Biophys Acta , vol.1557 , pp. 21-33
    • Havaux, M.1    Guedeney, G.2    He, Q.3    Grossman, A.R.4
  • 40
    • 0035808493 scopus 로고    scopus 로고
    • The high lightinducible polypeptides in Synechocystis PCC6803: Expression and function in high light
    • He QF, Dolganov N, Bjorkman O, Grossman AR (2001) The high lightinducible polypeptides in Synechocystis PCC6803: expression and function in high light. J Biol Chem 276: 306-314
    • (2001) J Biol Chem , vol.276 , pp. 306-314
    • He, Q.F.1    Dolganov, N.2    Bjorkman, O.3    Grossman, A.R.4
  • 41
    • 0001677706 scopus 로고
    • Light adaptation of cyclic electron transport through photosystem I in the cyanobacterium Synechococcus sp. PCC 7942
    • Herbert SK, Martin RE, Fork DC (1995) Light adaptation of cyclic electron transport through photosystem I in the cyanobacterium Synechococcus sp. PCC 7942. Photosynth Res 46: 277-285
    • (1995) Photosynth Res , vol.46 , pp. 277-285
    • Herbert, S.K.1    Martin, R.E.2    Fork, D.C.3
  • 42
    • 34547751888 scopus 로고    scopus 로고
    • Photosystem II damage induced by chemically generated singlet oxygen in tobacco leaves
    • Hideg E, Kós PB, Vass I (2007) Photosystem II damage induced by chemically generated singlet oxygen in tobacco leaves. Physiol Plant 131: 33-40
    • (2007) Physiol Plant , vol.131 , pp. 33-40
    • Hideg, E.1    Kós, P.B.2    Vass, I.3
  • 43
    • 0016701378 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes
    • Hildebraunt AG, Roots I (1975) Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes. Arch Biochem Biophys 171: 385-397
    • (1975) Arch Biochem Biophys , vol.171 , pp. 385-397
    • Hildebraunt, A.G.1    Roots, I.2
  • 44
    • 0029327403 scopus 로고
    • Effect of hydroxyl radical on intact microalgal photosynthesis
    • Hirayama S, Ueda R, Sugata K (1995) Effect of hydroxyl radical on intact microalgal photosynthesis. Energy Convers Manage 36: 685-688
    • (1995) Energy Convers Manage , vol.36 , pp. 685-688
    • Hirayama, S.1    Ueda, R.2    Sugata, K.3
  • 45
    • 12844253100 scopus 로고    scopus 로고
    • Anti-oxidative stress system in cyanobacteria: Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803
    • Hosoya-Matsuda N, Motohashi K, Yoshimura H, Nozaki A, Inoue K, Ohmori M, Hisabori T (2005) Anti-oxidative stress system in cyanobacteria: significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. J Biol Chem 280: 840-846
    • (2005) J Biol Chem , vol.280 , pp. 840-846
    • Hosoya-Matsuda, N.1    Motohashi, K.2    Yoshimura, H.3    Nozaki, A.4    Inoue, K.5    Ohmori, M.6    Hisabori, T.7
  • 46
    • 0036549167 scopus 로고    scopus 로고
    • HtpG plays a role in cold acclimation in cyanobacteria
    • Hossain MM, Nakamoto H (2002) HtpG plays a role in cold acclimation in cyanobacteria. Curr Microbiol 44: 291-296
    • (2002) Curr Microbiol , vol.44 , pp. 291-296
    • Hossain, M.M.1    Nakamoto, H.2
  • 47
    • 0038489504 scopus 로고    scopus 로고
    • Role for the cyanobacterial HtpG in protection from oxidative stress
    • Hossain MM, Nakamoto H (2003) Role for the cyanobacterial HtpG in protection from oxidative stress. Curr Microbiol 46: 70-76
    • (2003) Curr Microbiol , vol.46 , pp. 70-76
    • Hossain, M.M.1    Nakamoto, H.2
  • 49
    • 46749110034 scopus 로고    scopus 로고
    • FactoMineR: An R package for multivariate analysis
    • Husson F, Josse J, Lé S (2008) FactoMineR: an R package for multivariate analysis. J Stat Softw 25: 1-18
    • (2008) J Stat Softw , vol.25 , pp. 1-18
    • Husson, F.1    Josse, J.2    Lé, S.3
  • 50
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay JA (2003) Pathways of oxidative damage. Annu Rev Microbiol 57: 395-418
    • (2003) Annu Rev Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 51
    • 27744476037 scopus 로고    scopus 로고
    • Oxidation of the non-heme iron complex in photosystem II
    • Ishikita H, Knapp EW (2005) Oxidation of the non-heme iron complex in photosystem II. Biochemistry 44: 14772-14783
    • (2005) Biochemistry , vol.44 , pp. 14772-14783
    • Ishikita, H.1    Knapp, E.W.2
  • 52
    • 51349156127 scopus 로고    scopus 로고
    • Differential effects of severe water stress on linear and cyclic electron fluxes through photosystem I in spinach leaf discs in CO2-enriched air
    • Jia H, Oguchi R, Hope AB, Barber J, Chow WS (2008) Differential effects of severe water stress on linear and cyclic electron fluxes through photosystem I in spinach leaf discs in CO2-enriched air. Planta 228: 803-812
    • (2008) Planta , vol.228 , pp. 803-812
    • Jia, H.1    Oguchi, R.2    Hope, A.B.3    Barber, J.4    Chow, W.S.5
  • 53
    • 77956020092 scopus 로고    scopus 로고
    • Light-dependent adsorption of photosynthetic cyanophages to Synechococcus sp. WH7803
    • Jia Y, Shan JY, Millard A, Clokie MRJ, Mann NH (2010) Light-dependent adsorption of photosynthetic cyanophages to Synechococcus sp. WH7803. FEMS Microbiol Lett 310: 120-126
    • (2010) FEMS Microbiol Lett , vol.310 , pp. 120-126
    • Jia, Y.1    Shan, J.Y.2    Millard, A.3    Clokie, M.R.J.4    Mann, N.H.5
  • 54
    • 0037162477 scopus 로고    scopus 로고
    • Cyclic electron transfer in plant leaf
    • Joliot P, Joliot A (2002) Cyclic electron transfer in plant leaf. Proc Natl Acad Sci USA 99: 10209-10214
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10209-10214
    • Joliot, P.1    Joliot, A.2
  • 55
    • 45949121831 scopus 로고
    • Effect of irradiances up to 2000 mEm22s21 on marine Synechococcus WH7803-I: Growth, pigmentation, and cell composition
    • Kana TM, Glibert PM (1987a) Effect of irradiances up to 2000 mEm22s21 on marine Synechococcus WH7803-I: growth, pigmentation, and cell composition. Deep Sea Research Part A Oceanographic Research Papers 34: 479-495
    • (1987) Deep Sea Research Part a Oceanographic Research Papers , vol.34 , pp. 479-495
    • Kana, T.M.1    Glibert, P.M.2
  • 56
    • 45949126649 scopus 로고
    • Effect of irradiances up to 2000 mEm22s21 on marine Synechococcus WH7803-II: Photosynthetic responses and mechanisms
    • Kana TM, Glibert PM (1987b) Effect of irradiances up to 2000 mEm22s21 on marine Synechococcus WH7803-II: photosynthetic responses and mechanisms. Deep Sea Research Part A Oceanographic Research Papers 34: 497-516
    • (1987) Deep Sea Research Part a Oceanographic Research Papers , vol.34 , pp. 497-516
    • Kana, T.M.1    Glibert, P.M.2
  • 57
    • 84986782795 scopus 로고
    • Zeaxanthin and beta-carotene in Synechococcus WH7803 respond differently to irradiance
    • Kana TM, Glibert PM, Goericke R, Welschmeyer NA (1988) Zeaxanthin and beta-carotene in Synechococcus WH7803 respond differently to irradiance. Limnol Oceanogr 33: 1623-1627
    • (1988) Limnol Oceanogr , vol.33 , pp. 1623-1627
    • Kana, T.M.1    Glibert, P.M.2    Goericke, R.3    Welschmeyer, N.A.4
  • 58
    • 33846068839 scopus 로고    scopus 로고
    • Histidine kinases play important roles in the perception and signal transduction of hydrogen peroxide in the cyanobacterium, Synechocystis sp. PCC 6803
    • Kanesaki Y, Yamamoto H, Paithoonrangsarid K, Shoumskaya M, Suzuki I, Hayashi H, Murata N (2007) Histidine kinases play important roles in the perception and signal transduction of hydrogen peroxide in the cyanobacterium, Synechocystis sp. PCC 6803. Plant J 49: 313-324
    • (2007) Plant J , vol.49 , pp. 313-324
    • Kanesaki, Y.1    Yamamoto, H.2    Paithoonrangsarid, K.3    Shoumskaya, M.4    Suzuki, I.5    Hayashi, H.6    Murata, N.7
  • 59
    • 0031026304 scopus 로고    scopus 로고
    • Mechanism of photosystem II photoinactivation and D1 protein degradation at low light: The role of back electron flow
    • Keren N, Berg A, van Kan PJM, Levanon H, Ohad I (1997) Mechanism of photosystem II photoinactivation and D1 protein degradation at low light: the role of back electron flow. Proc Natl Acad Sci USA 94: 1579-1584
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1579-1584
    • Keren, N.1    Berg, A.2    van Kan, P.J.M.3    Levanon, H.4    Ohad, I.5
  • 61
    • 34548153334 scopus 로고    scopus 로고
    • Photoprotection in cyanobacteria: The orange carotenoid protein (OCP)-related non-photochemical-quenching mechanism
    • Kirilovsky D (2007) Photoprotection in cyanobacteria: the orange carotenoid protein (OCP)-related non-photochemical-quenching mechanism. Photosynth Res 93: 7-16
    • (2007) Photosynth Res , vol.93 , pp. 7-16
    • Kirilovsky, D.1
  • 62
    • 77956206479 scopus 로고    scopus 로고
    • Phylogenetic and evolutionary patterns in microbial carotenoid biosynthesis are revealed by comparative genomics
    • Klassen JL (2010) Phylogenetic and evolutionary patterns in microbial carotenoid biosynthesis are revealed by comparative genomics. PLoS ONE 5: e11257
    • (2010) PLoS ONE , vol.5
    • Klassen, J.L.1
  • 63
    • 46549102099 scopus 로고
    • Singlet oxygen and plants
    • Knox JP, Dodge AD (1985) Singlet oxygen and plants. Phytochemistry 24: 889-896
    • (1985) Phytochemistry , vol.24 , pp. 889-896
    • Knox, J.P.1    Dodge, A.D.2
  • 65
  • 67
    • 33644867870 scopus 로고    scopus 로고
    • The FtsH protease slr0228 is important for quality control of photosystem II in the thylakoid membrane of Synechocystis sp. PCC 6803
    • Komenda J, Barker M, Kuviková S, de Vries R, Mullineaux CW, Tichý M, Nixon PJ (2006) The FtsH protease slr0228 is important for quality control of photosystem II in the thylakoid membrane of Synechocystis sp. PCC 6803. J Biol Chem 281: 1145-1151
    • (2006) J Biol Chem , vol.281 , pp. 1145-1151
    • Komenda, J.1    Barker, M.2    Kuviková, S.3    de Vries, R.4    Mullineaux, C.W.5    Tichý, M.6    Nixon, P.J.7
  • 68
    • 77950370531 scopus 로고    scopus 로고
    • Role of FtsH2 in the repair of photosystem II in mutants of the cyanobacterium Synechocystis PCC 6803 with impaired assembly or stability of the CaMn4 cluster
    • Komenda J, Knoppova J, Krynicka V, Nixon PJ, Tichý M (2010) Role of FtsH2 in the repair of photosystem II in mutants of the cyanobacterium Synechocystis PCC 6803 with impaired assembly or stability of the CaMn4 cluster. Biochim Biophys Acta 1797: 566-575
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 566-575
    • Komenda, J.1    Knoppova, J.2    Krynicka, V.3    Nixon, P.J.4    Tichý, M.5
  • 69
    • 84989714150 scopus 로고
    • Photoinhibition of photosynthesis and growth-responses at different light levels in psbA gene mutants of the cyanobacterium Synechococcus
    • Krupa Z, Oquist G, Gustafsson P (1991) Photoinhibition of photosynthesis and growth-responses at different light levels in psbA gene mutants of the cyanobacterium Synechococcus. Physiol Plant 82: 1-8
    • (1991) Physiol Plant , vol.82 , pp. 1-8
    • Krupa, Z.1    Oquist, G.2    Gustafsson, P.3
  • 71
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda
    • Kuzminov A (1999) Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda. Microbiol Mol Biol Rev 63: 751-813
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 73
    • 24944541498 scopus 로고    scopus 로고
    • Iron starvation leads to oxidative stress in Anabaena sp. strain PCC 7120
    • Latifi A, Jeanjean R, Lemeille S, Havaux M, Zhang CC (2005) Iron starvation leads to oxidative stress in Anabaena sp. strain PCC 7120. J Bacteriol 187: 6596-6598
    • (2005) J Bacteriol , vol.187 , pp. 6596-6598
    • Latifi, A.1    Jeanjean, R.2    Lemeille, S.3    Havaux, M.4    Zhang, C.C.5
  • 75
    • 27644554315 scopus 로고    scopus 로고
    • Singlet oxygen and photo-oxidative stress management in plants and algae
    • Ledford HK, Niyogi KK (2005) Singlet oxygen and photo-oxidative stress management in plants and algae. Plant Cell Environ 28: 1037-1045
    • (2005) Plant Cell Environ , vol.28 , pp. 1037-1045
    • Ledford, H.K.1    Niyogi, K.K.2
  • 76
    • 33645220455 scopus 로고    scopus 로고
    • Oxidative stress in marine environments: Biochemistry and physiological ecology
    • Lesser MP (2006) Oxidative stress in marine environments: biochemistry and physiological ecology. Annu Rev Physiol 68: 253-278
    • (2006) Annu Rev Physiol , vol.68 , pp. 253-278
    • Lesser, M.P.1
  • 77
    • 2442682940 scopus 로고    scopus 로고
    • Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. strain PCC 6803
    • Li H, Singh AK, McIntyre LM, Sherman LA (2004) Differential gene expression in response to hydrogen peroxide and the putative PerR regulon of Synechocystis sp. strain PCC 6803. J Bacteriol 186: 3331-3345
    • (2004) J Bacteriol , vol.186 , pp. 3331-3345
    • Li, H.1    Singh, A.K.2    McIntyre, L.M.3    Sherman, L.A.4
  • 78
    • 77958150922 scopus 로고    scopus 로고
    • Computational analysis of LexA regulons in cyanobacteria
    • Li S, Xu M, Su Z (2010) Computational analysis of LexA regulons in cyanobacteria. BMC Genomics 11: 527
    • (2010) BMC Genomics , vol.11 , pp. 527
    • Li, S.1    Xu, M.2    Su, Z.3
  • 79
    • 0035433101 scopus 로고    scopus 로고
    • Ecological aspects of ntcA gene expression and its use as an indicator of the nitrogen status of marine Synechococcus spp
    • Lindell D, Post AF (2001) Ecological aspects of ntcA gene expression and its use as an indicator of the nitrogen status of marine Synechococcus spp. Appl Environ Microbiol 67: 3340-3349
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3340-3349
    • Lindell, D.1    Post, A.F.2
  • 80
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-D D C(T)) method
    • Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-D D C(T)) method. Methods 25: 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 82
    • 10744226907 scopus 로고    scopus 로고
    • Oxidative modifications of the photosystem II D1 protein by reactive oxygen species: From isolated protein to cyanobacterial cells
    • Lupínková L, Komenda J (2004) Oxidative modifications of the photosystem II D1 protein by reactive oxygen species: from isolated protein to cyanobacterial cells. Photochem Photobiol 79: 152-162
    • (2004) Photochem Photobiol , vol.79 , pp. 152-162
    • Lupínková, L.1    Komenda, J.2
  • 83
    • 0038545398 scopus 로고    scopus 로고
    • Sensitivity of cyanobacterial antenna, reaction center and CO2 assimilation transcripts and proteins to moderate UVB: Light acclimation potentiates resistance to UVB
    • MacDonald TM, Dubois L, Smith LC, Campbell DA (2003) Sensitivity of cyanobacterial antenna, reaction center and CO2 assimilation transcripts and proteins to moderate UVB: light acclimation potentiates resistance to UVB. Photochem Photobiol 77: 405-412
    • (2003) Photochem Photobiol , vol.77 , pp. 405-412
    • Macdonald, T.M.1    Dubois, L.2    Smith, L.C.3    Campbell, D.A.4
  • 85
    • 0030620443 scopus 로고    scopus 로고
    • Enumeration and cell cycle analysis of natural populations of marine picoplankton by flow cytometry using the nucleic acid stain SYBR Green I
    • Marie D, Partensky F, Jacquet S, Vaulot D (1997) Enumeration and cell cycle analysis of natural populations of marine picoplankton by flow cytometry using the nucleic acid stain SYBR Green I. Appl Environ Microbiol 63: 186-193
    • (1997) Appl Environ Microbiol , vol.63 , pp. 186-193
    • Marie, D.1    Partensky, F.2    Jacquet, S.3    Vaulot, D.4
  • 86
    • 0642277748 scopus 로고    scopus 로고
    • Two-component systems in Prochlorococcus MED4: Genomic analysis and differential expression under stress
    • Mary I, Vaulot D (2003) Two-component systems in Prochlorococcus MED4: genomic analysis and differential expression under stress. FEMS Microbiol Lett 226: 135-144
    • (2003) FEMS Microbiol Lett , vol.226 , pp. 135-144
    • Mary, I.1    Vaulot, D.2
  • 87
    • 0031750450 scopus 로고    scopus 로고
    • Beta-carotene hydroxylase gene from the cyanobacterium Synechocystis sp. PCC6803
    • Masamoto K, Misawa N, Kaneko T, Kikuno R, Toh H (1998) Beta-carotene hydroxylase gene from the cyanobacterium Synechocystis sp. PCC6803. Plant Cell Physiol 39: 560-564
    • (1998) Plant Cell Physiol , vol.39 , pp. 560-564
    • Masamoto, K.1    Misawa, N.2    Kaneko, T.3    Kikuno, R.4    Toh, H.5
  • 90
    • 22744444676 scopus 로고    scopus 로고
    • After 30 years of study, the bacterial SOS response still surprises us
    • Michel B (2005) After 30 years of study, the bacterial SOS response still surprises us. PLoS Biol 3: e255
    • (2005) PLoS Biol , vol.3
    • Michel, B.1
  • 91
    • 0032241725 scopus 로고    scopus 로고
    • Extraction of cellular and tissue RNA
    • Millican DS, Bird IM (1998) Extraction of cellular and tissue RNA. Methods Mol Biol 105: 315-324
    • (1998) Methods Mol Biol , vol.105 , pp. 315-324
    • Millican, D.S.1    Bird, I.M.2
  • 92
    • 0036728244 scopus 로고    scopus 로고
    • Oxidative stress, antioxidants and stress tolerance
    • Mittler R (2002) Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci 7: 405-410
    • (2002) Trends Plant Sci , vol.7 , pp. 405-410
    • Mittler, R.1
  • 93
    • 0029127671 scopus 로고
    • Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: Implications for the mechanism of degradation of the D1 protein under illumination
    • Miyao M, Ikeuchi M, Yamamoto N, Ono T (1995) Specific degradation of the D1 protein of photosystem II by treatment with hydrogen peroxide in darkness: implications for the mechanism of degradation of the D1 protein under illumination. Biochemistry 34: 10019-10026
    • (1995) Biochemistry , vol.34 , pp. 10019-10026
    • Miyao, M.1    Ikeuchi, M.2    Yamamoto, N.3    Ono, T.4
  • 94
    • 0034722337 scopus 로고    scopus 로고
    • The family of light-harvesting-related proteins (LHCs, ELIPs, HLIPs): Was the harvesting of light their primary function?
    • Montané MH, Kloppstech K (2000) The family of light-harvesting-related proteins (LHCs, ELIPs, HLIPs): was the harvesting of light their primary function? Gene 258: 1-8
    • (2000) Gene , vol.258 , pp. 1-8
    • Montané, M.H.1    Kloppstech, K.2
  • 95
    • 0029109040 scopus 로고
    • Comparative physiology of Synechococcus and Prochlorococcus: Influence of light and temperature on growth, pigments, fluorescence and absorptive properties
    • Moore LR, Goericke R, Chisholm SW (1995) Comparative physiology of Synechococcus and Prochlorococcus: influence of light and temperature on growth, pigments, fluorescence and absorptive properties. Mar Ecol Prog Ser 116: 259-275
    • (1995) Mar Ecol Prog Ser , vol.116 , pp. 259-275
    • Moore, L.R.1    Goericke, R.2    Chisholm, S.W.3
  • 96
    • 0001567189 scopus 로고    scopus 로고
    • Marine photochemistry and its impact on carbon cycling
    • In S Demers, S de Mora, M Vernet, Cambridge University Press, Cambridge, UK
    • Mopper K, Kieber DJ (2000) Marine photochemistry and its impact on carbon cycling. In S Demers, S de Mora, M Vernet, eds, Effects of UV Radiation on Marine Ecosystems. Cambridge University Press, Cambridge, UK, pp 101-129
    • (2000) Effects of UV Radiation On Marine Ecosystems , pp. 101-129
    • Mopper, K.1    Kieber, D.J.2
  • 98
    • 33746761616 scopus 로고    scopus 로고
    • A new paradigm for the action of reactive oxygen species in the photoinhibition of photosystem II
    • Nishiyama Y, Allakhverdiev SI, Murata N (2006) A new paradigm for the action of reactive oxygen species in the photoinhibition of photosystem II. Biochim Biophys Acta 1757: 742-749
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 742-749
    • Nishiyama, Y.1    Allakhverdiev, S.I.2    Murata, N.3
  • 99
    • 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 SI, Yamamoto H, Hayashi H, Murata N (2004) Singlet oxygen inhibits the repair of photosystem II by suppressing the translation elongation of the D1 protein in Synechocystis sp. PCC 6803. Biochemistry 43: 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
  • 100
    • 0035886704 scopus 로고    scopus 로고
    • Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery
    • Nishiyama Y, Yamamoto H, Allakhverdiev SI, Inaba M, Yokota A, Murata N (2001) Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery. EMBO J 20: 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
  • 101
    • 77956375190 scopus 로고    scopus 로고
    • Recent advances in understanding the assembly and repair of photosystem II
    • Nixon PJ, Michoux F, Yu JF, Boehm M, Komenda J (2010) Recent advances in understanding the assembly and repair of photosystem II. Ann Bot (Lond) 106: 1-16
    • (2010) Ann Bot (Lond) , vol.106 , pp. 1-16
    • Nixon, P.J.1    Michoux, F.2    Yu, J.F.3    Boehm, M.4    Komenda, J.5
  • 102
    • 33751280335 scopus 로고    scopus 로고
    • Protein constituents of photosystem II: The D1 and D2 core proteins
    • In T Wydrzynski, K Satoh, Kluwer Academic Publications, Dordrecht, The Netherlands
    • Nixon PJ, Sarcina M, Diner BA (2005) Protein constituents of photosystem II: the D1 and D2 core proteins. In T Wydrzynski, K Satoh, eds, Photosystem II: The Water/Plastoquinone Oxido-Reductase In Photosynthesis, Vol 22. Kluwer Academic Publications, Dordrecht, The Netherlands, pp 71-94
    • (2005) Photosystem II: The Water/Plastoquinone Oxido-Reductase In Photosynthesis , vol.22 , pp. 71-94
    • Nixon, P.J.1    Sarcina, M.2    Diner, B.A.3
  • 103
    • 0031735647 scopus 로고    scopus 로고
    • Ascorbate and glutathione: Keeping active oxygen under control
    • Noctor G, Foyer CH (1998) Ascorbate and glutathione: keeping active oxygen under control. Annu Rev Plant Physiol Plant Mol Biol 49: 249-279
    • (1998) Annu Rev Plant Physiol Plant Mol Biol , vol.49 , pp. 249-279
    • Noctor, G.1    Foyer, C.H.2
  • 104
    • 34547805062 scopus 로고    scopus 로고
    • Cyanobacterial NADPH dehydrogenase complexes
    • Ogawa T, Mi H (2007) Cyanobacterial NADPH dehydrogenase complexes. Photosynth Res 93: 69-77
    • (2007) Photosynth Res , vol.93 , pp. 69-77
    • Ogawa, T.1    Mi, H.2
  • 105
    • 20444405387 scopus 로고    scopus 로고
    • Two-step mechanism of photodamage to photosystem II: Step 1 occurs at the oxygen-evolving complex and step 2 occurs at the photochemical reaction center
    • Ohnishi N, Allakhverdiev SI, Takahashi S, Higashi S, Watanabe M, Nishiyama Y, Murata N (2005) Two-step mechanism of photodamage to photosystem II: step 1 occurs at the oxygen-evolving complex and step 2 occurs at the photochemical reaction center. Biochemistry 44: 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
  • 106
    • 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 TA, MiyaoM(1996) 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: 73-79
    • (1996) Biochim Biophys Acta , vol.1274 , pp. 73-79
    • Okada, K.1    Ikeuchi, M.2    Yamamoto, N.3    Ono, T.A.4    Miyao, M.5
  • 107
    • 0028795997 scopus 로고
    • Light inactivation of functional photosystem-II in leaves of peas grown in moderate light depends on photon exposure
    • Park YI, Chow WS, Anderson JM (1995) Light inactivation of functional photosystem-II in leaves of peas grown in moderate light depends on photon exposure. Planta 196: 401-411
    • (1995) Planta , vol.196 , pp. 401-411
    • Park, Y.I.1    Chow, W.S.2    Anderson, J.M.3
  • 108
    • 0002220172 scopus 로고
    • Photosynthetic production of hydrogen peroxide by Anacystis nidulans
    • Patterson CO, Myers J (1973) Photosynthetic production of hydrogen peroxide by Anacystis nidulans. Plant Physiol 51: 104-109
    • (1973) Plant Physiol , vol.51 , pp. 104-109
    • Patterson, C.O.1    Myers, J.2
  • 109
    • 33746234719 scopus 로고    scopus 로고
    • A LexA-related protein regulates redox-sensitive expression of the cyanobacterial RNA helicase, crhR
    • Patterson-Fortin LM, Colvin KR, Owttrim GW (2006) A LexA-related protein regulates redox-sensitive expression of the cyanobacterial RNA helicase, crhR. Nucleic Acids Res 34: 3446-3454
    • (2006) Nucleic Acids Res , vol.34 , pp. 3446-3454
    • Patterson-Fortin, L.M.1    Colvin, K.R.2    Owttrim, G.W.3
  • 110
    • 67649948825 scopus 로고    scopus 로고
    • Production of reactive oxygen species by photosystem II
    • Pospísil P (2009) Production of reactive oxygen species by photosystem II. Biochim Biophys Acta 1787: 1151-1160
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1151-1160
    • Pospísil, P.1
  • 112
    • 77954217839 scopus 로고    scopus 로고
    • Detection of reactive oxygen species (ROS) by the oxidant-sensing probe 2',7'-dichlorodihydrofluorescein diacetate in the cyanobacterium Anabaena variabilis PCC 7937
    • Rastogi RP, Singh SP, Häder DP, Sinha RP (2010) Detection of reactive oxygen species (ROS) by the oxidant-sensing probe 2',7'-dichlorodihydrofluorescein diacetate in the cyanobacterium Anabaena variabilis PCC 7937. Biochem Biophys Res Commun 397: 603-607
    • (2010) Biochem Biophys Res Commun , vol.397 , pp. 603-607
    • Rastogi, R.P.1    Singh, S.P.2    Häder, D.P.3    Sinha, R.P.4
  • 113
    • 0033657261 scopus 로고    scopus 로고
    • Principal components analysis to summarize microarray experiments: Application to sporulation time series
    • Raychaudhuri S, Stuart JM, Altman RB (2000) Principal components analysis to summarize microarray experiments: application to sporulation time series. Pac Symp Biocomput 5: 455-466
    • (2000) Pac Symp Biocomput , vol.5 , pp. 455-466
    • Raychaudhuri, S.1    Stuart, J.M.2    Altman, R.B.3
  • 115
  • 116
    • 33750494694 scopus 로고
    • Hydrogen-peroxide photoproduction sensitized with rose-bengal with semicarbazide as the electron source
    • Roncel M, Navarro JA, Delarosa MA (1988) Hydrogen-peroxide photoproduction sensitized with rose-bengal with semicarbazide as the electron source. J Photochem Photobiol Chem 45: 341-353
    • (1988) J Photochem Photobiol Chem , vol.45 , pp. 341-353
    • Roncel, M.1    Navarro, J.A.2    Delarosa, M.A.3
  • 117
    • 33646369630 scopus 로고    scopus 로고
    • Toxin release in response to oxidative stress and programmed cell death in the cyanobacterium Microcystis aeruginosa
    • Ross C, Santiago-Vázquez L, Paul V (2006) Toxin release in response to oxidative stress and programmed cell death in the cyanobacterium Microcystis aeruginosa. Aquat Toxicol 78: 66-73
    • (2006) Aquat Toxicol , vol.78 , pp. 66-73
    • Ross, C.1    Santiago-Vázquez, L.2    Paul, V.3
  • 118
    • 77951610740 scopus 로고    scopus 로고
    • HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942
    • Sato T, Minagawa S, Kojima E, Okamoto N, Nakamoto H (2010) HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942. MolMicrobiol 76: 576-589
    • (2010) MolMicrobiol , vol.76 , pp. 576-589
    • Sato, T.1    Minagawa, S.2    Kojima, E.3    Okamoto, N.4    Nakamoto, H.5
  • 120
    • 13544267729 scopus 로고    scopus 로고
    • Functional in situ evaluation of photosynthesis-protecting carotenoids in mutants of the cyanobacterium Synechocystis PCC6803
    • Schäfer L, Vioque A, Sandmann G (2005) Functional in situ evaluation of photosynthesis-protecting carotenoids in mutants of the cyanobacterium Synechocystis PCC6803. J Photochem Photobiol B 78: 195-201
    • (2005) J Photochem Photobiol B , vol.78 , pp. 195-201
    • Schäfer, L.1    Vioque, A.2    Sandmann, G.3
  • 121
    • 0036068418 scopus 로고    scopus 로고
    • The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus
    • Schelin J, Lindmark F, Clarke AK (2002) The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus. Microbiology 148: 2255-2265
    • (2002) Microbiology , vol.148 , pp. 2255-2265
    • Schelin, J.1    Lindmark, F.2    Clarke, A.K.3
  • 122
    • 42949151399 scopus 로고    scopus 로고
    • The ferredoxin/thioredoxin system of oxygenic photosynthesis
    • Schürmann P, Buchanan BB (2008) The ferredoxin/thioredoxin system of oxygenic photosynthesis. Antioxid Redox Signal 10: 1235-1274
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1235-1274
    • Schürmann, P.1    Buchanan, B.B.2
  • 123
    • 23844543308 scopus 로고    scopus 로고
    • Acclimation of unicellular cyanobacteria to macronutrient deficiency: Emergence of a complex network of cellular responses
    • Schwarz R, Forchhammer K (2005) Acclimation of unicellular cyanobacteria to macronutrient deficiency: emergence of a complex network of cellular responses. Microbiology 151: 2503-2514
    • (2005) Microbiology , vol.151 , pp. 2503-2514
    • Schwarz, R.1    Forchhammer, K.2
  • 124
    • 44349169371 scopus 로고    scopus 로고
    • Light variability illuminates niche-partitioning among marine picocyanobacteria
    • Six C, Finkel ZV, Irwin AJ, Campbell DA (2007a) Light variability illuminates niche-partitioning among marine picocyanobacteria. PLoS ONE 2: e1341
    • (2007) PLoS ONE , vol.2
    • Six, C.1    Finkel, Z.V.2    Irwin, A.J.3    Campbell, D.A.4
  • 125
    • 38749091643 scopus 로고    scopus 로고
    • Contrasting photoacclimation costs in ecotypes of the marine eukaryotic picoplankter Ostreococcus
    • Six C, Finkel ZV, Rodriguez F, Marie D, Partensky F, Campbell DA (2008) Contrasting photoacclimation costs in ecotypes of the marine eukaryotic picoplankter Ostreococcus. Limnol Oceanogr 53: 255-265
    • (2008) Limnol Oceanogr , vol.53 , pp. 255-265
    • Six, C.1    Finkel, Z.V.2    Rodriguez, F.3    Marie, D.4    Partensky, F.5    Campbell, D.A.6
  • 126
    • 34547127369 scopus 로고    scopus 로고
    • UVinduced phycobilisome dismantling in the marine picocyanobacterium Synechococcus sp. WH8102
    • Six C, Joubin L, Partensky F, Holtzendorff J, Garczarek L (2007b) UVinduced phycobilisome dismantling in the marine picocyanobacterium Synechococcus sp. WH8102. Photosynth Res 92: 75-86
    • (2007) Photosynth Res , vol.92 , pp. 75-86
    • Six, C.1    Joubin, L.2    Partensky, F.3    Holtzendorff, J.4    Garczarek, L.5
  • 127
    • 4243163130 scopus 로고    scopus 로고
    • Photophysiology of the marine cyanobacterium Synechococcus sp. WH8102, a new model organism
    • Six C, Thomas JC, Brahamsha B, Lemoine Y, Partensky F (2004) Photophysiology of the marine cyanobacterium Synechococcus sp. WH8102, a new model organism. Aquat Microb Ecol 35: 17-29
    • (2004) Aquat Microb Ecol , vol.35 , pp. 17-29
    • Six, C.1    Thomas, J.C.2    Brahamsha, B.3    Lemoine, Y.4    Partensky, F.5
  • 128
    • 14244253561 scopus 로고    scopus 로고
    • Two novel phycoerythrin-associated linker proteins in the marine cyanobacterium Synechococcus sp. strain WH8102
    • Six C, Thomas JC, Thion L, Lemoine Y, Zal F, Partensky F (2005) Two novel phycoerythrin-associated linker proteins in the marine cyanobacterium Synechococcus sp. strain WH8102. J Bacteriol 187: 1685-1694
    • (2005) J Bacteriol , vol.187 , pp. 1685-1694
    • Six, C.1    Thomas, J.C.2    Thion, L.3    Lemoine, Y.4    Zal, F.5    Partensky, F.6
  • 129
    • 4544341015 scopus 로고    scopus 로고
    • Linear models and empirical Bayes methods for assessing differential expression in microarray experiments
    • Smyth GK (2004) Linear models and empirical Bayes methods for assessing differential expression in microarray experiments. Stat Appl Genet Mol Biol 3: Article 3
    • (2004) Stat Appl Genet Mol Biol 3: Article , pp. 3
    • Smyth, G.K.1
  • 130
    • 0242333835 scopus 로고    scopus 로고
    • Normalization of cDNA microarray data
    • Smyth GK, Speed T (2003) Normalization of cDNA microarray data. Methods 31: 265-273
    • (2003) Methods , vol.31 , pp. 265-273
    • Smyth, G.K.1    Speed, T.2
  • 131
    • 33846305759 scopus 로고    scopus 로고
    • Damage to the oxygenevolving complex by superoxide anion, hydrogen peroxide, and hydroxyl radical in photoinhibition of photosystem II
    • Song YG, Liu B, Wang LF, Li MH, Liu Y (2006) Damage to the oxygenevolving complex by superoxide anion, hydrogen peroxide, and hydroxyl radical in photoinhibition of photosystem II. Photosynth Res 90: 67-78
    • (2006) Photosynth Res , vol.90 , pp. 67-78
    • Song, Y.G.1    Liu, B.2    Wang, L.F.3    Li, M.H.4    Liu, Y.5
  • 132
    • 34347232349 scopus 로고    scopus 로고
    • Distinctive types of ATP-dependent Clp proteases in cyanobacteria
    • Stanne TM, Pojidaeva E, Andersson FI, Clarke AK (2007) Distinctive types of ATP-dependent Clp proteases in cyanobacteria. J Biol Chem 282: 14394-14402
    • (2007) J Biol Chem , vol.282 , pp. 14394-14402
    • Stanne, T.M.1    Pojidaeva, E.2    Andersson, F.I.3    Clarke, A.K.4
  • 134
    • 41549083289 scopus 로고    scopus 로고
    • How do environmental stresses accelerate photoinhibition?
    • Takahashi S, Murata N (2008) How do environmental stresses accelerate photoinhibition? Trends Plant Sci 13: 178-182
    • (2008) Trends Plant Sci , vol.13 , pp. 178-182
    • Takahashi, S.1    Murata, N.2
  • 135
    • 0036024664 scopus 로고    scopus 로고
    • Quick and easy implementation of the Benjamini-Hochberg procedure for controlling the false positive rate in multiple comparisons
    • Thissen D, Steinberg L, Kuang D (2002) Quick and easy implementation of the Benjamini-Hochberg procedure for controlling the false positive rate in multiple comparisons. J Educ Behav Stat 27: 77-83
    • (2002) J Educ Behav Stat , vol.27 , pp. 77-83
    • Thissen, D.1    Steinberg, L.2    Kuang, D.3
  • 136
    • 0001045008 scopus 로고    scopus 로고
    • A cyanobacterium lacking iron superoxide dismutase is sensitized to oxidative stress induced with methyl viologen but is not sensitized to oxidative stress induced with norflurazon
    • Thomas DJ, Avenson TJ, Thomas JB, Herbert SK (1998) A cyanobacterium lacking iron superoxide dismutase is sensitized to oxidative stress induced with methyl viologen but is not sensitized to oxidative stress induced with norflurazon. Plant Physiol 116: 1593-1602
    • (1998) Plant Physiol , vol.116 , pp. 1593-1602
    • Thomas, D.J.1    Avenson, T.J.2    Thomas, J.B.3    Herbert, S.K.4
  • 137
    • 0042266279 scopus 로고    scopus 로고
    • Synechocystis 6803 mutants expressing distinct forms of the photosystem II D1 protein from Synechococcus 7942: Relationship between the psbA coding region and sensitivity to visible and UV-B radiation
    • Tichý M, Lupínková L, Sicora C, Vass I, Kuviková S, Prásil O, Komenda J (2003) Synechocystis 6803 mutants expressing distinct forms of the photosystem II D1 protein from Synechococcus 7942: relationship between the psbA coding region and sensitivity to visible and UV-B radiation. Biochim Biophys Acta 1605: 55-66
    • (2003) Biochim Biophys Acta , vol.1605 , pp. 55-66
    • Tichý, M.1    Lupínková, L.2    Sicora, C.3    Vass, I.4    Kuviková, S.5    Prásil, O.6    Komenda, J.7
  • 138
    • 0032987969 scopus 로고    scopus 로고
    • In vivo role of catalase-peroxidase in Synechocystis sp. strain PCC 6803
    • Tichý M, Vermaas W (1999) In vivo role of catalase-peroxidase in Synechocystis sp. strain PCC 6803. J Bacteriol 181: 1875-1882
    • (1999) J Bacteriol , vol.181 , pp. 1875-1882
    • Tichý, M.1    Vermaas, W.2
  • 139
    • 0032710402 scopus 로고    scopus 로고
    • Swimming marine Synechococcus strains with widely different photosynthetic pigment ratios form a monophyletic group
    • Toledo G, Palenik B, Brahamsha B (1999) Swimming marine Synechococcus strains with widely different photosynthetic pigment ratios form a monophyletic group. Appl Environ Microbiol 65: 5247-5251
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5247-5251
    • Toledo, G.1    Palenik, B.2    Brahamsha, B.3
  • 140
    • 0029921367 scopus 로고    scopus 로고
    • The rate constant of photoinhibition,measured in lincomycin-treated leaves, is directly proportional to light intensity
    • Tyystjärvi E, Aro EM (1996) The rate constant of photoinhibition,measured in lincomycin-treated leaves, is directly proportional to light intensity. Proc Natl Acad Sci USA 93: 2213-2218
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2213-2218
    • Tyystjärvi, E.1    Aro, E.M.2
  • 141
    • 63549106377 scopus 로고    scopus 로고
    • Janus-faced charge recombinations in photosystem II photoinhibition
    • Vass I, Cser K (2009) Janus-faced charge recombinations in photosystem II photoinhibition. Trends Plant Sci 14: 200-205
    • (2009) Trends Plant Sci , vol.14 , pp. 200-205
    • Vass, I.1    Cser, K.2
  • 142
    • 0026604580 scopus 로고
    • Reversible and irreversible intermediates during photoinhibition of photosystem II: Stable reduced QA species promote chlorophyll triplet formation
    • Vass I, Styring S, Hundal T, Koivuniemi A, Aro EM, Andersson B (1992) Reversible and irreversible intermediates during photoinhibition of photosystem II: stable reduced QA species promote chlorophyll triplet formation. Proc Natl Acad Sci USA 89: 1408-1412
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1408-1412
    • Vass, I.1    Styring, S.2    Hundal, T.3    Koivuniemi, A.4    Aro, E.M.5    Andersson, B.6
  • 143
    • 38049174822 scopus 로고    scopus 로고
    • Small Cab-like proteins retard degradation of photosystem II-associated chlorophyll in Synechocystis sp. PCC 6803: Kinetic analysis of pigment labeling with 15N and 13C
    • Vavilin D, Yao D, Vermaas W (2007) Small Cab-like proteins retard degradation of photosystem II-associated chlorophyll in Synechocystis sp. PCC 6803: kinetic analysis of pigment labeling with 15N and 13C. J Biol Chem 282: 37660-37668
    • (2007) J Biol Chem , vol.282 , pp. 37660-37668
    • Vavilin, D.1    Yao, D.2    Vermaas, W.3
  • 144
    • 33745668217 scopus 로고    scopus 로고
    • Chloroplastic NAD(P)H dehydrogenase in tobacco leaves functions in alleviation of oxidative damage caused by temperature stress
    • Wang P, Duan W, Takabayashi A, Endo T, Shikanai T, Ye JY, Mi HL (2006) Chloroplastic NAD(P)H dehydrogenase in tobacco leaves functions in alleviation of oxidative damage caused by temperature stress. Plant Physiol 141: 465-474
    • (2006) Plant Physiol , vol.141 , pp. 465-474
    • Wang, P.1    Duan, W.2    Takabayashi, A.3    Endo, T.4    Shikanai, T.5    Ye, J.Y.6    Mi, H.L.7
  • 145
    • 33745445226 scopus 로고    scopus 로고
    • A soluble carotenoid protein involved in phycobilisome-related energy dissipation in cyanobacteria
    • Wilson A, Ajlani G, Verbavatz JM, Vass I, Kerfeld CA, Kirilovsky D (2006) A soluble carotenoid protein involved in phycobilisome-related energy dissipation in cyanobacteria. Plant Cell 18: 992-1007
    • (2006) Plant Cell , vol.18 , pp. 992-1007
    • Wilson, A.1    Ajlani, G.2    Verbavatz, J.M.3    Vass, I.4    Kerfeld, C.A.5    Kirilovsky, D.6
  • 146
    • 4043137829 scopus 로고    scopus 로고
    • Normalization for two-color cDNA microarray data
    • Yang YH, Thorne NP (2003) Normalization for two-color cDNA microarray data. Lecture Notes Monogr Ser 40: 403-418
    • (2003) Lecture Notes Monogr Ser , vol.40 , pp. 403-418
    • Yang, Y.H.1    Thorne, N.P.2
  • 147
    • 0347625655 scopus 로고    scopus 로고
    • Comparative analysis of idiA and isiA transcription under iron starvation and oxidative stress in Synechococcus elongatus PCC 7942 wild-type and selected mutants
    • Yousef N, Pistorius EK, Michel KP (2003) Comparative analysis of idiA and isiA transcription under iron starvation and oxidative stress in Synechococcus elongatus PCC 7942 wild-type and selected mutants. Arch Microbiol 180: 471-483
    • (2003) Arch Microbiol , vol.180 , pp. 471-483
    • Yousef, N.1    Pistorius, E.K.2    Michel, K.P.3
  • 148
    • 0001944852 scopus 로고
    • psaE is required for in-vivo cyclic electron flow around photosystem I in the cyanobacterium Synechococcus sp PCC 7002
    • Yu L, Zhao JD, Muhlenhoff U, Bryant DA, Golbeck JH (1993) psaE is required for in-vivo cyclic electron flow around photosystem I in the cyanobacterium Synechococcus sp PCC 7002. Plant Physiol 103: 171-180
    • (1993) Plant Physiol , vol.103 , pp. 171-180
    • Yu, L.1    Zhao, J.D.2    Muhlenhoff, U.3    Bryant, D.A.4    Golbeck, J.H.5
  • 149
    • 77957914336 scopus 로고    scopus 로고
    • Roles of xanthophyll carotenoids in protection against photoinhibition and oxidative stress in the cyanobacterium Synechococcus sp. strain PCC 7002
    • Zhu YH, Graham JE, Ludwig M, Xiong W, Alvey RM, Shen GZ, Bryant DA (2010) Roles of xanthophyll carotenoids in protection against photoinhibition and oxidative stress in the cyanobacterium Synechococcus sp. strain PCC 7002. Arch Biochem Biophys 504: 86-99
    • (2010) Arch Biochem Biophys , vol.504 , pp. 86-99
    • Zhu, Y.H.1    Graham, J.E.2    Ludwig, M.3    Xiong, W.4    Alvey, R.M.5    Shen, G.Z.6    Bryant, D.A.7
  • 150
    • 0037015995 scopus 로고    scopus 로고
    • Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses
    • Zolla L, Rinalducci S (2002) Involvement of active oxygen species in degradation of light-harvesting proteins under light stresses. Biochemistry 41: 14391-14402
    • (2002) Biochemistry , vol.41 , pp. 14391-14402
    • Zolla, L.1    Rinalducci, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.