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Volumn 4, Issue NOV, 2013, Pages

A phosphorylation map of the photosystem II supercomplex C2S2M2

Author keywords

LHC II phosphorylation; Photoinhibition; PS II core phosphorylation; PS II repair cycle; PS II supercomplex; State transitions; Stn7; Stn8

Indexed keywords


EID: 84900866801     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2013.00459     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 0026556851 scopus 로고
    • Protein phosphorylation in regulation of photosynthesis
    • doi: 10.1016/S0005-2728(09)91014-3
    • Allen, J. F. (1992). Protein phosphorylation in regulation of photosynthesis. Biochim. Biophys. Acta 1098, 275-335. doi: 10.1016/S0005-2728(09)91014-3
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 2
    • 0037423884 scopus 로고    scopus 로고
    • State transitions-a question of balance
    • doi: 10.1126/science.1082833
    • Allen, J. F. (2003). State transitions-a question of balance. Science 299, 1530-1532. doi: 10.1126/science.1082833
    • (2003) Science , vol.299 , pp. 1530-1532
    • Allen, J.F.1
  • 3
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation-energy between photosystems
    • doi: 10.1038/291025a0
    • Allen, J. F., Bennett, J., Steinback, K. E., and Arntzen, C. J. (1981). Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation-energy between photosystems. Nature 291, 25-29. doi: 10.1038/291025a0
    • (1981) Nature , vol.291 , pp. 25-29
    • Allen, J.F.1    Bennett, J.2    Steinback, K.E.3    Arntzen, C.J.4
  • 4
    • 0035651544 scopus 로고    scopus 로고
    • Molecular recognition in thylakoid structure and function
    • doi: 10.1016/S1360-1385(01)02010-6
    • Allen, J. F., and Forsberg, J. (2001). Molecular recognition in thylakoid structure and function. Trends Plant Sci. 6, 317-326. doi: 10.1016/S1360-1385(01)02010-6
    • (2001) Trends Plant Sci. , vol.6 , pp. 317-326
    • Allen, J.F.1    Forsberg, J.2
  • 5
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II. Inactivation, protein damage and turnover
    • doi: 10.1016/0005-2728(93)90134-2
    • Aro, E. M., Virgin, I., and Andersson, B. (1993). Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochim. Biophys. Acta 1143, 113-134. doi: 10.1016/0005-2728(93)90134-2
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.M.1    Virgin, I.2    Andersson, B.3
  • 6
    • 14544282417 scopus 로고    scopus 로고
    • State transitions and light adaptation require chloroplast thylakoid protein kinase STN7
    • doi: 10.1038/nature03286
    • Bellafiore, S., Barneche, F., Peltier, G., and Rochaix, J. D. (2005). State transitions and light adaptation require chloroplast thylakoid protein kinase STN7. Nature 433, 892-895. doi: 10.1038/nature03286
    • (2005) Nature , vol.433 , pp. 892-895
    • Bellafiore, S.1    Barneche, F.2    Peltier, G.3    Rochaix, J.D.4
  • 7
    • 0017411320 scopus 로고
    • Phosphorylation of chloroplast membrane polypeptides
    • doi: 10.1038/269344a0
    • Bennett, J. (1977). Phosphorylation of chloroplast membrane polypeptides. Nature 269, 344-346. doi: 10.1038/269344a0
    • (1977) Nature , vol.269 , pp. 344-346
    • Bennett, J.1
  • 8
    • 0001138725 scopus 로고
    • Protein-phosphorylation in green plant chloroplasts
    • doi: 10.1146/annurev.pp.42.060191.001433
    • Bennett, J. (1991). Protein-phosphorylation in green plant chloroplasts. Annu. Rev. Plant Physiol. Plant Mol. Biol. 42, 281-311. doi: 10.1146/annurev.pp.42.060191.001433
    • (1991) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.42 , pp. 281-311
    • Bennett, J.1
  • 9
    • 67649304885 scopus 로고    scopus 로고
    • Light-induced dissociation of an antenna hetero-oligomer is needed for non-photochemical quenching induction
    • doi: 10.1074/jbc.M808625200
    • Betterle, N., Ballottari, M., Zorzan, S., De Bianchi, S., Cazzaniga, S., Dall'osto, L., et al. (2009). Light-induced dissociation of an antenna hetero-oligomer is needed for non-photochemical quenching induction. J. Biol. Chem. 284, 15255-15266. doi: 10.1074/jbc.M808625200
    • (2009) J. Biol. Chem. , vol.284 , pp. 15255-15266
    • Betterle, N.1    Ballottari, M.2    Zorzan, S.3    De Bianchi, S.4    Cazzaniga, S.5    Dall'osto, L.6
  • 10
    • 27144491327 scopus 로고    scopus 로고
    • Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases
    • doi: 10.1038/nature04016
    • Bonardi, V., Pesaresi, P., Becker, T., Schleiff, E., Wagner, R., Pfannschmidt, T., et al. (2005). Photosystem II core phosphorylation and photosynthetic acclimation require two different protein kinases. Nature 437, 1179-1182. doi: 10.1038/nature04016
    • (2005) Nature , vol.437 , pp. 1179-1182
    • Bonardi, V.1    Pesaresi, P.2    Becker, T.3    Schleiff, E.4    Wagner, R.5    Pfannschmidt, T.6
  • 11
    • 0014646190 scopus 로고
    • Fluorescence and oxygen evolution from Chlorella pyrenoidosa
    • doi: 10.1016/0005-2728(69)90168-6
    • Bonaventura, C., and Myers, J. (1969). Fluorescence and oxygen evolution from Chlorella pyrenoidosa. Biochim. Biophys. Acta 189, 366-383. doi: 10.1016/0005-2728(69)90168-6
    • (1969) Biochim. Biophys. Acta , vol.189 , pp. 366-383
    • Bonaventura, C.1    Myers, J.2
  • 12
    • 70350565366 scopus 로고    scopus 로고
    • Functional architecture of higher plant photosystem II supercomplexes
    • doi: 10.1038/emboj.2009.232
    • Caffarri, S., Kouril, R., Kereiche, S., Boekema, E. J., and Croce, R. (2009). Functional architecture of higher plant photosystem II supercomplexes. EMBO J. 28, 3052-3063. doi: 10.1038/emboj.2009.232
    • (2009) EMBO J. , vol.28 , pp. 3052-3063
    • Caffarri, S.1    Kouril, R.2    Kereiche, S.3    Boekema, E.J.4    Croce, R.5
  • 13
    • 0037423885 scopus 로고    scopus 로고
    • Rote of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas
    • doi: 10.1126/science.1081397
    • Depege, N., Bellafiore, S., and Rochaix, J. D. (2003). Rote of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas. Science 299, 1572-1575. doi: 10.1126/science.1081397
    • (2003) Science , vol.299 , pp. 1572-1575
    • Depege, N.1    Bellafiore, S.2    Rochaix, J.D.3
  • 14
    • 0026733569 scopus 로고
    • Identification, characterization, and resolution of the in vivo phosphorylated form of the D1 photosystem II reaction center protein
    • Elich, T. D., Edelman, M., and Mattoo, A. K. (1992). Identification, characterization, and resolution of the in vivo phosphorylated form of the D1 photosystem II reaction center protein. J. Biol. Chem. 267, 3523-3529.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3523-3529
    • Elich, T.D.1    Edelman, M.2    Mattoo, A.K.3
  • 15
    • 80052534971 scopus 로고    scopus 로고
    • High light induced disassembly of photosystem II supercomplexes in Arabidopsis requires STN7-dependent phosphorylation of CP29
    • doi: 10.1371/journal.pone.0024565
    • Fristedt, R., and Vener, A. V. (2011). High light induced disassembly of photosystem II supercomplexes in Arabidopsis requires STN7-dependent phosphorylation of CP29. PLoS ONE 6:e24565. doi: 10.1371/journal.pone.0024565
    • (2011) PLoS ONE , vol.6
    • Fristedt, R.1    Vener, A.V.2
  • 16
    • 84865333904 scopus 로고    scopus 로고
    • Functional analyses of the plant photosystem I-light-harvesting complex II supercomplex reveal that light-harvesting complex II loosely bound to photosystem II is a very efficient antenna for photosystem I in state II
    • doi: 10.1105/tpc.112.100339
    • Galka, P., Santabarbara, S., Khuong, T. T., Degand, H., Morsomme, P., Jennings, R. C., et al. (2012). Functional analyses of the plant photosystem I-light-harvesting complex II supercomplex reveal that light-harvesting complex II loosely bound to photosystem II is a very efficient antenna for photosystem I in state II. Plant Cell 24, 2963-2978. doi: 10.1105/tpc.112.100339
    • (2012) Plant Cell , vol.24 , pp. 2963-2978
    • Galka, P.1    Santabarbara, S.2    Khuong, T.T.3    Degand, H.4    Morsomme, P.5    Jennings, R.C.6
  • 17
    • 77953523697 scopus 로고    scopus 로고
    • Visualizing the mobility and distribution of chlorophyll proteins in higher plant thylakoid membranes: Effects of photoinhibition and protein phosphorylation
    • doi: 10.1111/j.1365-313X.2010.04207.x
    • Goral, T. K., Johnson, M. P., Brain, A. P., Kirchhoff, H., Ruban, A. V., and Mullineaux, C. W. (2010). Visualizing the mobility and distribution of chlorophyll proteins in higher plant thylakoid membranes: effects of photoinhibition and protein phosphorylation. Plant J. Cell Mol. Biol. 62, 948-959. doi: 10.1111/j.1365-313X.2010.04207.x
    • (2010) Plant J. Cell Mol. Biol. , vol.62 , pp. 948-959
    • Goral, T.K.1    Johnson, M.P.2    Brain, A.P.3    Kirchhoff, H.4    Ruban, A.V.5    Mullineaux, C.W.6
  • 18
    • 0025908437 scopus 로고
    • Light-dependent phosphorylation of photosystem-ii polypeptides maintains electron-transport at high light-intensity-separation from effects of phosphorylation of LHC-Ii
    • doi: 10.1016/S0005-2728(05)80249-X
    • Harrison, M. A., and Allen, J. F. (1991). Light-dependent phosphorylation of photosystem-ii polypeptides maintains electron-transport at high light-intensity-separation from effects of phosphorylation of LHC-Ii. Biochim. Biophys. Acta 1058, 289-296. doi: 10.1016/S0005-2728(05)80249-X
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 289-296
    • Harrison, M.A.1    Allen, J.F.2
  • 19
    • 84870627370 scopus 로고    scopus 로고
    • Architectural switch in plant photosynthetic membranes induced by light stress
    • doi: 10.1073/pnas.1214265109
    • Herbstova, M., Tietz, S., Kinzel, C., Turkina, M. V., and Kirchhoff, H. (2012). Architectural switch in plant photosynthetic membranes induced by light stress. Proc. Natl. Acad. Sci. U.S.A. 109, 20130-20135. doi: 10.1073/pnas.1214265109
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 20130-20135
    • Herbstova, M.1    Tietz, S.2    Kinzel, C.3    Turkina, M.V.4    Kirchhoff, H.5
  • 20
    • 25444471029 scopus 로고    scopus 로고
    • Light-harvesting complex II protein CP29 binds to photosystem I of Chlamydomonas reinhardtii under State 2 conditions
    • doi: 10.1111/j.1742-4658.2005.04894.x
    • Kargul, J., Turkina, M. V., Nield, J., Benson, S., Vener, A. V., and Barber, J. (2005). Light-harvesting complex II protein CP29 binds to photosystem I of Chlamydomonas reinhardtii under State 2 conditions. FEBS J. 272, 4797-4806. doi: 10.1111/j.1742-4658.2005.04894.x
    • (2005) FEBS J. , vol.272 , pp. 4797-4806
    • Kargul, J.1    Turkina, M.V.2    Nield, J.3    Benson, S.4    Vener, A.V.5    Barber, J.6
  • 21
    • 84887436029 scopus 로고    scopus 로고
    • Architectural switches in plant thylakoid membranes
    • doi: 10.1007/s11120-013-9843-0
    • Kirchhoff, H. (2013a). Architectural switches in plant thylakoid membranes. Photosyn. Res. 116, 481-487. doi: 10.1007/s11120-013-9843-0
    • (2013) Photosyn. Res. , vol.116 , pp. 481-487
    • Kirchhoff, H.1
  • 22
    • 84875861876 scopus 로고    scopus 로고
    • Structural constraints for protein repair in plant photosynthetic membranes
    • doi: 10.4161/psb.23634
    • Kirchhoff, H. (2013b). Structural constraints for protein repair in plant photosynthetic membranes. Plant Signal. Behav. 18:e23634. doi: 10.4161/psb.23634
    • (2013) Plant Signal. Behav. , vol.18
    • Kirchhoff, H.1
  • 23
    • 43049166553 scopus 로고    scopus 로고
    • Protein diffusion and macromolecular crowding in thylakoid membranes
    • doi: 10.1104/pp.107.115170
    • Kirchhoff, H., Haferkamp, S., Allen, J. F., Epstein, D. B., and Mullineaux, C. W. (2008). Protein diffusion and macromolecular crowding in thylakoid membranes. Plant Physiol. 146, 1571-1578. doi: 10.1104/pp.107.115170
    • (2008) Plant Physiol. , vol.146 , pp. 1571-1578
    • Kirchhoff, H.1    Haferkamp, S.2    Allen, J.F.3    Epstein, D.B.4    Mullineaux, C.W.5
  • 24
    • 80655135259 scopus 로고    scopus 로고
    • Supramolecular organization of photosystem II in green plants
    • doi: 10.1016/j.bbabio.2011.05.024
    • Kouril, R., Dekker, J. P., and Boekema, E. J. (2012). Supramolecular organization of photosystem II in green plants. Biochim. Biophys. Acta 1817, 2-12. doi: 10.1016/j.bbabio.2011.05.024
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 2-12
    • Kouril, R.1    Dekker, J.P.2    Boekema, E.J.3
  • 25
    • 0001449340 scopus 로고
    • Membrane protein damage and repair: Selective loss of a quinone-protein function in chloroplast membranes
    • doi: 10.1073/pnas.81.13.4070
    • Kyle, D. J., Ohad, I., and Arntzen, C. J. (1984). Membrane protein damage and repair: selective loss of a quinone-protein function in chloroplast membranes. Proc. Natl. Acad. Sci. U.S.A. 81, 4070-4074. doi: 10.1073/pnas.81.13.4070
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 4070-4074
    • Kyle, D.J.1    Ohad, I.2    Arntzen, C.J.3
  • 26
    • 78650244316 scopus 로고    scopus 로고
    • State transitions at the crossroad of thylakoid signalling pathways
    • doi: 10.1007/s11120-010-9538-8
    • Lemeille, S., and Rochaix, J. D. (2010). State transitions at the crossroad of thylakoid signalling pathways. Photosyn. Res. 106, 33-46. doi: 10.1007/s11120-010-9538-8
    • (2010) Photosyn. Res. , vol.106 , pp. 33-46
    • Lemeille, S.1    Rochaix, J.D.2
  • 27
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
    • doi: 10.1038/nature02373
    • Liu, Z., Yan, H., Wang, K., Kuang, T., Zhang, J., Gui, L., et al. (2004). Crystal structure of spinach major light-harvesting complex at 2.72 A resolution. Nature 428, 287-292. doi: 10.1038/nature02373
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6
  • 28
    • 0027953119 scopus 로고
    • Photoinhibition of Photosynthesis in Nature
    • doi: 10.1146/annurev.pp.45.060194.003221
    • Long, S. P., Humphries, S., and Falkowski, P. G. (1994). Photoinhibition of Photosynthesis in Nature. Annu. Rev. Plant Physiol. Plant Mol. Biol. 45, 633-662. doi: 10.1146/annurev.pp.45.060194.003221
    • (1994) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.45 , pp. 633-662
    • Long, S.P.1    Humphries, S.2    Falkowski, P.G.3
  • 29
    • 0032948239 scopus 로고    scopus 로고
    • Photosystem-II damage and repair cycle in chloroplasts: What modulates the rate of photodamage?
    • doi: 10.1016/S1360-1385(99)01387-4
    • Melis, A. (1999). Photosystem-II damage and repair cycle in chloroplasts: what modulates the rate of photodamage? Trends Plant Sci. 4, 130-135. doi: 10.1016/S1360-1385(99)01387-4
    • (1999) Trends Plant Sci. , vol.4 , pp. 130-135
    • Melis, A.1
  • 30
    • 55649119566 scopus 로고    scopus 로고
    • Factors controlling the mobility of photosynthetic proteins
    • doi: 10.1111/j.1751-1097.2008.00420.x
    • Mullineaux, C. W. (2008). Factors controlling the mobility of photosynthetic proteins. Photochem. Photobiol. 84, 1310-1316. doi: 10.1111/j.1751-1097.2008.00420.x
    • (2008) Photochem. Photobiol. , vol.84 , pp. 1310-1316
    • Mullineaux, C.W.1
  • 31
    • 0014690121 scopus 로고
    • Control of excitation transfer in photosynthesis. I. Light-induced changes of chlorophyll a fluorescence in Porphyridium cruentum
    • doi: 10.1016/0005-2728(69)90067-X
    • Murata, N. (1969). Control of excitation transfer in photosynthesis. I. Light-induced changes of chlorophyll a fluorescence in Porphyridium cruentum. Biochim. Biophys. Acta 172, 242-251. doi: 10.1016/0005-2728(69)90067-X
    • (1969) Biochim. Biophys. Acta , vol.172 , pp. 242-251
    • Murata, N.1
  • 32
    • 84886259384 scopus 로고    scopus 로고
    • Loss-of-function of OsSTN8 suppresses the photosystem (PS) II core protein phosphorylation and interferes with PSII repair mechanism in rice (Oryza sativa)
    • doi: 10.1111/tpj.12331
    • Nath, K., Poudyal, R. S., Eom, J. S., Park, Y. S., Zulfugarov, I. S., Mishra, S. R., et al. (2013). Loss-of-function of OsSTN8 suppresses the photosystem (PS) II core protein phosphorylation and interferes with PSII repair mechanism in rice (Oryza sativa). Plant J. 76, 675-686. doi: 10.1111/tpj.12331
    • (2013) Plant J. , vol.76 , pp. 675-686
    • Nath, K.1    Poudyal, R.S.2    Eom, J.S.3    Park, Y.S.4    Zulfugarov, I.S.5    Mishra, S.R.6
  • 33
    • 77956375190 scopus 로고    scopus 로고
    • Recent advances in understanding the assembly and repair of photosystem II
    • doi: 10.1093/aob/mcq059
    • Nixon, P. J., Michoux, F., Yu, J., Boehm, M., and Komenda, J. (2010). Recent advances in understanding the assembly and repair of photosystem II. Ann. Bot. 106, 1-16. doi: 10.1093/aob/mcq059
    • (2010) Ann. Bot. , vol.106 , pp. 1-16
    • Nixon, P.J.1    Michoux, F.2    Yu, J.3    Boehm, M.4    Komenda, J.5
  • 34
    • 79952362580 scopus 로고    scopus 로고
    • Structural insights into energy regulation of light-harvesting complex CP29 from spinach
    • doi: 10.1038/nsmb.2008
    • Pan, X. W., Li, M., Wan, T., Wang, L. F., Jia, C. J., Hou, Z. Q., et al. (2011). Structural insights into energy regulation of light-harvesting complex CP29 from spinach. Nat. Struct. Mol. Biol. 18, 309-315. doi: 10.1038/nsmb.2008
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 309-315
    • Pan, X.W.1    Li, M.2    Wan, T.3    Wang, L.F.4    Jia, C.J.5    Hou, Z.Q.6
  • 35
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • doi: 10.1002/jcc.20084
    • Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., et al. (2004). UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612. doi: 10.1002/jcc.20084
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Huang, C.C.3    Couch, G.S.4    Greenblatt, D.M.5    Meng, E.C.6
  • 36
    • 75749085797 scopus 로고    scopus 로고
    • Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and thylakoid electron flow
    • doi: 10.1371/journal.pbio.1000288
    • Pribil, M., Pesaresi, P., Hertle, A., Barbato, R., and Leister, D. (2010). Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and thylakoid electron flow. PLoS Biol. 8:e1000288. doi: 10.1371/journal.pbio.1000288
    • (2010) PLoS Biol. , vol.8
    • Pribil, M.1    Pesaresi, P.2    Hertle, A.3    Barbato, R.4    Leister, D.5
  • 37
    • 0032548785 scopus 로고    scopus 로고
    • Thylakoid protein phosphorylation in evolutionally divergent species with oxygenic photosynthesis
    • doi: 10.1016/S0014-5793(98)00088-X
    • Pursiheimo, S., Rintamaki, E., Baena-Gonzalez, E., and Aro, E. M. (1998). Thylakoid protein phosphorylation in evolutionally divergent species with oxygenic photosynthesis. FEBS Lett. 423, 178-182. doi: 10.1016/S0014-5793(98)00088-X
    • (1998) FEBS Lett. , vol.423 , pp. 178-182
    • Pursiheimo, S.1    Rintamaki, E.2    Baena-Gonzalez, E.3    Aro, E.M.4
  • 38
    • 79958152724 scopus 로고    scopus 로고
    • A mechanism for regulation of chloroplast LHC II kinase by plastoquinol and thioredoxin
    • doi: 10.1016/j.febslet.2011.04.076
    • Puthiyaveetil, S. (2011). A mechanism for regulation of chloroplast LHC II kinase by plastoquinol and thioredoxin. FEBS Lett. 585, 1717-1721. doi: 10.1016/j.febslet.2011.04.076
    • (2011) FEBS Lett. , vol.585 , pp. 1717-1721
    • Puthiyaveetil, S.1
  • 39
    • 84855352370 scopus 로고    scopus 로고
    • Oxidation-reduction signalling components in regulatory pathways of state transitions and photosystem stoichiometry adjustment in chloroplasts
    • doi: 10.1111/j.1365-3040.2011.02349.x
    • Puthiyaveetil, S., Ibrahim, I. M., and Allen, J. F. (2012). Oxidation-reduction signalling components in regulatory pathways of state transitions and photosystem stoichiometry adjustment in chloroplasts. Plant Cell Environ. 35, 347-359. doi: 10.1111/j.1365-3040.2011.02349.x
    • (2012) Plant Cell Environ. , vol.35 , pp. 347-359
    • Puthiyaveetil, S.1    Ibrahim, I.M.2    Allen, J.F.3
  • 40
    • 79961220621 scopus 로고    scopus 로고
    • Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF)
    • doi: 10.1073/pnas.1104734108
    • Reiland, S., Finazzi, G., Endler, A., Willig, A., Baerenfaller, K., Grossmann, J., et al. (2011). Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF). Proc. Natl. Acad. Sci. U.S.A. 108, 12955-12960. doi: 10.1073/pnas.1104734108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 12955-12960
    • Reiland, S.1    Finazzi, G.2    Endler, A.3    Willig, A.4    Baerenfaller, K.5    Grossmann, J.6
  • 41
    • 0034633748 scopus 로고    scopus 로고
    • Cooperative regulation of light-harvesting complex II phosphorylation via the plastoquinol and ferredoxin-thioredoxin system in chloroplasts
    • doi: 10.1073/pnas.180054297
    • Rintamaki, E., Martinsuo, P., Pursiheimo, S., and Aro, E. M. (2000). Cooperative regulation of light-harvesting complex II phosphorylation via the plastoquinol and ferredoxin-thioredoxin system in chloroplasts. Proc. Natl. Acad. Sci. U.S.A. 97, 11644-11649. doi: 10.1073/pnas.180054297
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11644-11649
    • Rintamaki, E.1    Martinsuo, P.2    Pursiheimo, S.3    Aro, E.M.4
  • 42
    • 84864479585 scopus 로고    scopus 로고
    • Identification of a photosystem II phosphatase involved in light acclimation in Arabidopsis
    • doi: 10.1105/tpc.112.095703
    • Samol, I., Shapiguzov, A., Ingelsson, B., Fucile, G., Crevecoeur, M., Vener, A. V., et al. (2012). Identification of a photosystem II phosphatase involved in light acclimation in Arabidopsis. Plant Cell 24, 2596-2609. doi: 10.1105/tpc.112.095703
    • (2012) Plant Cell , vol.24 , pp. 2596-2609
    • Samol, I.1    Shapiguzov, A.2    Ingelsson, B.3    Fucile, G.4    Crevecoeur, M.5    Vener, A.V.6
  • 43
    • 77949510295 scopus 로고    scopus 로고
    • The PPH1 phosphatase is specifically involved in LHCII dephosphorylation and state transitions in Arabidopsis
    • doi: 10.1073/pnas.0913810107
    • Shapiguzov, A., Ingelsson, B., Samol, I., Andres, C., Kessler, F., Rochaix, J. D., et al. (2010). The PPH1 phosphatase is specifically involved in LHCII dephosphorylation and state transitions in Arabidopsis. Proc. Natl. Acad. Sci. U.S.A. 107, 4782-4787. doi: 10.1073/pnas.0913810107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4782-4787
    • Shapiguzov, A.1    Ingelsson, B.2    Samol, I.3    Andres, C.4    Kessler, F.5    Rochaix, J.D.6
  • 44
    • 31044439022 scopus 로고    scopus 로고
    • Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii
    • doi: 10.1073/pnas.0509952103
    • Takahashi, H., Iwai, M., Takahashi, Y., and Minagawa, J. (2006). Identification of the mobile light-harvesting complex II polypeptides for state transitions in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. U.S.A. 103, 477-482. doi: 10.1073/pnas.0509952103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 477-482
    • Takahashi, H.1    Iwai, M.2    Takahashi, Y.3    Minagawa, J.4
  • 45
    • 82755187237 scopus 로고    scopus 로고
    • Thylakoid protein phosphorylation in dynamic regulation of photosystem II in higher plants
    • doi: 10.1016/j.bbabio.2011.05.005
    • Tikkanen, M., and Aro, E. M. (2012). Thylakoid protein phosphorylation in dynamic regulation of photosystem II in higher plants. Biochim. Biophys. Acta 1817, 232-238. doi: 10.1016/j.bbabio.2011.05.005
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 232-238
    • Tikkanen, M.1    Aro, E.M.2
  • 46
    • 54349098202 scopus 로고    scopus 로고
    • Core protein phosphorylation facilitates the repair of photodamaged photosystem II at high light
    • doi: 10.1016/j.bbabio.2008.08.004
    • Tikkanen, M., Nurmi, M., Kangasjarvi, S., and Aro, E. M. (2008). Core protein phosphorylation facilitates the repair of photodamaged photosystem II at high light. Biochim. Biophys. Acta 1777, 1432-1437. doi: 10.1016/j.bbabio.2008.08.004
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1432-1437
    • Tikkanen, M.1    Nurmi, M.2    Kangasjarvi, S.3    Aro, E.M.4
  • 47
    • 33748333438 scopus 로고    scopus 로고
    • Environmentally modulated phosphoproteome of photosynthetic membranes in the green alga Chlamydomonas reinhardtii
    • doi: 10.1074/mcp.M600066-MCP200
    • Turkina, M. V., Kargul, J., Blanco-Rivero, A., Villarejo, A., Barber, J., and Vener, A. V. (2006). Environmentally modulated phosphoproteome of photosynthetic membranes in the green alga Chlamydomonas reinhardtii. Mol. Cell. Proteomics 5, 1412-1425. doi: 10.1074/mcp.M600066-MCP200
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1412-1425
    • Turkina, M.V.1    Kargul, J.2    Blanco-Rivero, A.3    Villarejo, A.4    Barber, J.5    Vener, A.V.6
  • 48
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 angstrom
    • doi: 10.1038/nature09913
    • Umena, Y., Kawakami, K., Shen, J.-R., and Kamiya, N. (2011). Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 angstrom. Nature 473, 55-65. doi: 10.1038/nature09913
    • (2011) Nature , vol.473 , pp. 55-65
    • Umena, Y.1    Kawakami, K.2    Shen, J.-R.3    Kamiya, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.