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Volumn 367, Issue 1608, 2012, Pages 3430-3443

Modulation of the light-harvesting chlorophyll antenna size in Chlamydomonas reinhardtii by TLA1 gene over-expression and RNA interference

Author keywords

Chl antenna size; Chlamydomonas reinhardtii; RNAi; Thylakoid membrane development; TLA1 gene; VIPP1 protein

Indexed keywords

CHLOROPHYLL; CHLOROPLAST; GENE EXPRESSION; GENETIC ANALYSIS; GREEN ALGA; PHOTOSYNTHESIS; PROTEIN; RNA; ULTRASTRUCTURE;

EID: 84869238309     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2012.0229     Document Type: Article
Times cited : (42)

References (70)
  • 1
    • 0000666754 scopus 로고
    • Two photochemical systems in photosynthesis
    • (doi:10.1038/190510a0)
    • Duysens, L. N. M., Amsez, J. & Kamp, B. M. 1961 Two photochemical systems in photosynthesis. Nature 190, 510-511. (doi:10.1038/190510a0)
    • (1961) Nature , vol.190 , pp. 510-511
    • Duysens, L.N.M.1    Amsez, J.2    Kamp, B.M.3
  • 2
    • 0000658235 scopus 로고    scopus 로고
    • Light-harvesting complexes of plants and algae: Introduction, survey and nomenclature
    • eds D. R. Ort & C. F. Yocum, Dordrecht, The Netherlands: Kluwer Academic Publishers
    • Simpson, D. J. & Knoetzel, J. 1996 Light-harvesting complexes of plants and algae: introduction, survey and nomenclature. In Oxygenic photosynthesis: the light reactions (eds D. R. Ort & C. F. Yocum), pp. 493-506. Dordrecht, The Netherlands: Kluwer Academic Publishers.
    • (1996) Oxygenic photosynthesis: The light reactions , pp. 493-506
    • Simpson, D.J.1    Knoetzel, J.2
  • 3
    • 0000784913 scopus 로고    scopus 로고
    • The light-harvesting chlorophyll a/b-binding polypeptides and their genes in angiosperm and gymnosperm species
    • eds D. R. Ort & C. F. Yocum, Dordrecht, The Netherlands: Kluwer Academic Publishers
    • Pichersky, E. & Jansson, S. 1996 The light-harvesting chlorophyll a/b-binding polypeptides and their genes in angiosperm and gymnosperm species. In Oxygenic photosynthesis: the light reactions (eds D. R. Ort & C. F. Yocum), pp. 507-521. Dordrecht, The Netherlands: Kluwer Academic Publishers.
    • (1996) Oxygenic photosynthesis: The light reactions , pp. 507-521
    • Pichersky, E.1    Jansson, S.2
  • 4
    • 0025797479 scopus 로고
    • Dynamics of photosynthetic membrane composition and function
    • (doi:10.1016/S0005-2728(05)80225-7)
    • Melis, A. 1991 Dynamics of photosynthetic membrane composition and function. Biochim. Biophys. Acta 1058, 87-106. (doi:10.1016/S0005-2728(05)80225-7)
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 87-106
    • Melis, A.1
  • 5
    • 0001696041 scopus 로고    scopus 로고
    • Excitation energy transfer: Functional and dynamic aspects of LHC (cab) proteins
    • eds D. R. Ort & C. F. Yocum, Dordrecht, The Netherlands: Kluwer Academic Publishersl
    • Melis, A. 1996 Excitation energy transfer: functional and dynamic aspects of LHC (cab) proteins. In Oxygenic photosynthesis: the light reactions (eds D. R. Ort & C. F. Yocum), pp. 523-538. Dordrecht, The Netherlands: Kluwer Academic Publishers.
    • (1996) Oxygenic photosynthesis: The light reactions , pp. 523-538
    • Melis, A.1
  • 6
    • 0031875917 scopus 로고    scopus 로고
    • Photosystem-II repair and chloroplast recovery from irradiance stress: Relationship between chronic photoinhibition, light-harvesting chlorophyll antenna size and photosynthetic productivity in Dunaliella salina (green algae)
    • (doi:10. 1023/A:1006024827225)
    • Neidhardt, J., Benemann, J. R., Zhang, L. & Melis, A. 1998 Photosystem-II repair and chloroplast recovery from irradiance stress: relationship between chronic photoinhibition, light-harvesting chlorophyll antenna size and photosynthetic productivity in Dunaliella salina (green algae). Photosynth. Res. 56, 175-184. (doi:10. 1023/A:1006024827225)
    • (1998) Photosynth. Res. , vol.56 , pp. 175-184
    • Neidhardt, J.1    Benemann, J.R.2    Zhang, L.3    Melis, A.4
  • 7
    • 51249165015 scopus 로고
    • A nomenclature for the genes encoding the chlorophyll a/b-binding proteins of higher plants
    • (doi:10. 1007/BF02668357)
    • Jansson, S. et al. 1992 A nomenclature for the genes encoding the chlorophyll a/b-binding proteins of higher plants. Plant Mol. Biol. Rep. 10, 242-253. (doi:10. 1007/BF02668357)
    • (1992) Plant Mol. Biol. Rep. , vol.10 , pp. 242-253
    • Jansson, S.1
  • 8
    • 1442301640 scopus 로고    scopus 로고
    • A genome's-eye view of the light-harvesting polypeptides of Chlamydomonas reinhardtii
    • (doi:10.1007/ s00294-003-0460-x)
    • Elrad, D. & Grossman, A. R. 2004 A genome's-eye view of the light-harvesting polypeptides of Chlamydomonas reinhardtii. Curr. Genet. 45, 61-75. (doi:10.1007/ s00294-003-0460-x)
    • (2004) Curr. Genet. , vol.45 , pp. 61-75
    • Elrad, D.1    Grossman, A.R.2
  • 9
    • 0002276039 scopus 로고
    • Photoregulation of the composition, function and structure of thylakoid membranes
    • (doi:10.1146/ annurev.pp.37.060186.000521)
    • Anderson, J. M. 1986 Photoregulation of the composition, function and structure of thylakoid membranes. Annu. Rev. Plant Physiol. 37, 93-136. (doi:10.1146/ annurev.pp.37.060186.000521)
    • (1986) Annu. Rev. Plant Physiol. , vol.37 , pp. 93-136
    • Anderson, J.M.1
  • 10
    • 0028865421 scopus 로고
    • Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool
    • (doi:10.1073/pnas.92.22.10237)
    • Escoubas, J. M., Lomas, M., LaRoche, J. & Falkowski, P. G. 1995 Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool. Proc. Natl Acad. Sci. USA 92, 10 237-10 241. (doi:10.1073/pnas.92.22.10237)
    • (1995) Proc. Natl Acad. Sci. USA , vol.92
    • Escoubas, J.M.1    Lomas, M.2    LaRoche, J.3    Falkowski, P.G.4
  • 11
    • 0032103356 scopus 로고    scopus 로고
    • Energy balance and acclimation to light and cold
    • (doi:10.1016/S1360-1385(98)01248-5)
    • Huner, N. P. A., Oquist, G. & Sarhan, F. 1998 Energy balance and acclimation to light and cold. Trends Plant Sci. 3, 224-230. (doi:10.1016/S1360-1385(98)01248-5)
    • (1998) Trends Plant Sci. , vol.3 , pp. 224-230
    • Huner, N.P.A.1    Oquist, G.2    Sarhan, F.3
  • 12
    • 0037353408 scopus 로고    scopus 로고
    • Chlorophyll antenna size adjustments by irradiance in Dunaliella salina involve coordinate regulation of chlorophyll a oxygenase (CAO) and LHCb gene expression
    • (doi:10.1023/A:1022545118212)
    • Masuda, T., Tanaka, A. & Melis, A. 2003 Chlorophyll antenna size adjustments by irradiance in Dunaliella salina involve coordinate regulation of chlorophyll a oxygenase (CAO) and LHCb gene expression. Plant Mol. Biol. 51, 757-771. (doi:10.1023/A:1022545118212)
    • (2003) Plant Mol. Biol. , vol.51 , pp. 757-771
    • Masuda, T.1    Tanaka, A.2    Melis, A.3
  • 16
    • 0031002318 scopus 로고    scopus 로고
    • Irradiance-dependent changes in the size and composition of the chlorophyll a-b light-harvesting complex in the green alga Dunaliella salina
    • (doi:10.1093/ oxfordjournals.pcp.a029080)
    • Tanaka, A. & Melis, A. 1997 Irradiance-dependent changes in the size and composition of the chlorophyll a-b light-harvesting complex in the green alga Dunaliella salina. Plant Cell Physiol. 38, 17-24. (doi:10.1093/ oxfordjournals.pcp.a029080)
    • (1997) Plant Cell Physiol. , vol.38 , pp. 17-24
    • Tanaka, A.1    Melis, A.2
  • 17
    • 0029157207 scopus 로고
    • Light penetration into cell suspensions of photosynthetic bacteria and relation to hydrogen production
    • (doi:10.1016/0922-338X(95)98176-L)
    • Nakada, E., Asada, Y., Arai, T. & Miyake, J. 1995 Light penetration into cell suspensions of photosynthetic bacteria and relation to hydrogen production. J. Ferment. Bioeng. 80, 53-57. (doi:10.1016/0922-338X(95)98176-L)
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 53-57
    • Nakada, E.1    Asada, Y.2    Arai, T.3    Miyake, J.4
  • 18
    • 0037070179 scopus 로고    scopus 로고
    • Light control over the size of an antenna unit building block as an efficient strategy for light harvesting in photosynthesis
    • (doi:10.1016/ S0014-5793(02)02238-X)
    • Yakovlev, A. G., Taisova, A. S. & Fetisova, Z. G. 2002 Light control over the size of an antenna unit building block as an efficient strategy for light harvesting in photosynthesis. FEBS Lett. 512, 129-132. (doi:10.1016/ S0014-5793(02)02238-X)
    • (2002) FEBS Lett. , vol.512 , pp. 129-132
    • Yakovlev, A.G.1    Taisova, A.S.2    Fetisova, Z.G.3
  • 19
    • 58149139946 scopus 로고    scopus 로고
    • Optical properties of microalgae for enhanced biofuels production
    • (doi:10.1364/OE.16.021807)
    • Mitra, M. & Melis, A. 2008 Optical properties of microalgae for enhanced biofuels production. Opt. Express 16, 21 807-21 820. (doi:10.1364/OE.16.021807)
    • (2008) Opt. Express , vol.16
    • Mitra, M.1    Melis, A.2
  • 20
    • 84856569052 scopus 로고    scopus 로고
    • Assembly of the light-harvesting chlorophyll antenna in the green alga Chlamydomonas reinhardtii requires expression of the TLA2-CpFTSY gene
    • (doi:10.1104/pp. 111.189910)
    • Kirst, H., Garcia-Cerdan, J. G., Zurbriggen, A. & Melis, A. 2012 Assembly of the light-harvesting chlorophyll antenna in the green alga Chlamydomonas reinhardtii requires expression of the TLA2-CpFTSY gene. Plant Physiol. 158, 930-945. (doi:10.1104/pp. 111.189910)
    • (2012) Plant Physiol. , vol.158 , pp. 930-945
    • Kirst, H.1    Garcia-Cerdan, J.G.2    Zurbriggen, A.3    Melis, A.4
  • 21
    • 0031040835 scopus 로고    scopus 로고
    • Conversion of chlorophyll b to chlorophyll a and the assembly of chlorophyll with apoproteins by isolated chloroplasts
    • Ohtsuka, T., Ito, H. & Tanaka, A. 1997 Conversion of chlorophyll b to chlorophyll a and the assembly of chlorophyll with apoproteins by isolated chloroplasts. Plant Physiol. 113, 137-147.
    • (1997) Plant Physiol. , vol.113 , pp. 137-147
    • Ohtsuka, T.1    Ito, H.2    Tanaka, A.3
  • 22
    • 0034483041 scopus 로고    scopus 로고
    • The role of growth rates, redox-state of the plastoquinone pool and the trans-thylakoid pH in photoacclimation of Chlorella vulgaris to growth irradiance and temperature
    • (doi:10.1007/s004250000368)
    • Wilson, K. E. & Huner, N. P. A. 2000 The role of growth rates, redox-state of the plastoquinone pool and the trans-thylakoid pH in photoacclimation of Chlorella vulgaris to growth irradiance and temperature. Planta 212, 93-102. (doi:10.1007/s004250000368)
    • (2000) Planta , vol.212 , pp. 93-102
    • Wilson, K.E.1    Huner, N.P.A.2
  • 23
    • 0032423858 scopus 로고    scopus 로고
    • Dunaliella salina (Chlorophyta) with small chlorophyll antenna sizes exhibit higher photosynthetic productivities and photon use efficiencies than normally pigmented cells
    • (doi:10.1023/A:1008076231267)
    • Melis, A., Neidhardt, J. & Benemann, J. R. 1999 Dunaliella salina (Chlorophyta) with small chlorophyll antenna sizes exhibit higher photosynthetic productivities and photon use efficiencies than normally pigmented cells. J. Appl. Phycol. 10, 515-52. (doi:10.1023/A:1008076231267)
    • (1999) J. Appl. Phycol. , vol.10 , pp. 515-552
    • Melis, A.1    Neidhardt, J.2    Benemann, J.R.3
  • 24
    • 67651115666 scopus 로고    scopus 로고
    • Solar energy conversion efficiencies in photosynthesis: Minimizing the chlorophyll antennae to maximize efficiency
    • (doi:10. 1016/j.plantsci.2009.06.005)
    • Melis, A. 2009 Solar energy conversion efficiencies in photosynthesis: minimizing the chlorophyll antennae to maximize efficiency. Plant Sci. 177, 272-280. (doi:10. 1016/j.plantsci.2009.06.005)
    • (2009) Plant Sci. , vol.177 , pp. 272-280
    • Melis, A.1
  • 25
    • 0037596752 scopus 로고    scopus 로고
    • tla1, a DNA insertional transformant of the green alga Chlamydomonas reinhardtii with a truncated light-harvesting chlorophyll antenna size
    • Polle, J. E. W., Kanakagiri, S. & Melis, A. 2003 tla1, a DNA insertional transformant of the green alga Chlamydomonas reinhardtii with a truncated light-harvesting chlorophyll antenna size. Planta 217, 49-59.
    • (2003) Planta , vol.217 , pp. 49-59
    • Polle, J.E.W.1    Kanakagiri, S.2    Melis, A.3
  • 26
    • 33847289819 scopus 로고    scopus 로고
    • Development of the light-harvesting chlorophyll antenna in the green alga Chlamydomonas reinhardtii is regulated by the novel TLA1 gene
    • (doi:10.1007/ s00425-006-0392-z)
    • Tetali, S., Mitra, M. & Melis, A. 2007 Development of the light-harvesting chlorophyll antenna in the green alga Chlamydomonas reinhardtii is regulated by the novel TLA1 gene. Planta 225, 813-829. (doi:10.1007/ s00425-006-0392-z)
    • (2007) Planta , vol.225 , pp. 813-829
    • Tetali, S.1    Mitra, M.2    Melis, A.3
  • 27
    • 76049111244 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the TLA1 gene in Chlamydomonas reinhardtii
    • (doi:10.1007/s00425-009-1083-3)
    • Mitra, M. & Melis, A. 2010 Genetic and biochemical analysis of the TLA1 gene in Chlamydomonas reinhardtii. Planta 231, 729-740. (doi:10.1007/s00425-009-1083-3)
    • (2010) Planta , vol.231 , pp. 729-740
    • Mitra, M.1    Melis, A.2
  • 28
    • 84855496428 scopus 로고    scopus 로고
    • The TLA1 protein family members contain a variant of the plain MOV34/ MPN domain
    • (doi:10.3923/ajbmb.2012.1.18)
    • Mitra, M., Ng, S. & Melis, A. 2012 The TLA1 protein family members contain a variant of the plain MOV34/ MPN domain. Am. J. Biochem. Mol. Biol. 2, 1-18. (doi:10.3923/ajbmb.2012.1.18)
    • (2012) Am. J. Biochem. Mol. Biol. , vol.2 , pp. 1-18
    • Mitra, M.1    Ng, S.2    Melis, A.3
  • 29
    • 0002257867 scopus 로고
    • Mitotic replication of deoxyribonucleic acids in Chlamydomonas reinhardtii
    • (doi:10.1073/pnas.46.1.83)
    • Sueoka, N. 1960 Mitotic replication of deoxyribonucleic acids in Chlamydomonas reinhardtii. Proc. Natl Acad. Sci. USA 46, 83-91. (doi:10.1073/pnas.46.1.83)
    • (1960) Proc. Natl Acad. Sci. USA , vol.46 , pp. 83-91
    • Sueoka, N.1
  • 31
    • 0033849640 scopus 로고    scopus 로고
    • Photosynthetic apparatus organization and function in wild type and a Chl b-less mutant of Chlamydomonas reinhardtii
    • (doi:10.1007/s004250000279)
    • Polle, J. E. W., Benemann, J. R., Tanaka, A. & Melis, A. 2000 Photosynthetic apparatus organization and function in wild type and a Chl b-less mutant of Chlamydomonas reinhardtii. Dependence on carbon source. Planta 211, 335-344. (doi:10.1007/s004250000279)
    • (2000) Dependence on carbon source. Planta , vol.211 , pp. 335-344
    • Polle, J.E.W.1    Benemann, J.R.2    Tanaka, A.3    Melis, A.4
  • 32
  • 33
    • 84989675168 scopus 로고
    • Lightabsorption and electron-transport balance between PSII and PSI in spinach chloroplasts
    • (doi:10.1111/j.1751-1097.1987. tb08413.x)
    • Melis, A., Spangfort, M. & Andersson, B. 1987 Lightabsorption and electron-transport balance between PSII and PSI in spinach chloroplasts. Photochem. Photobiol. 45, 129-136. (doi:10.1111/j.1751-1097.1987. tb08413.x)
    • (1987) Photochem. Photobiol. , vol.45 , pp. 129-136
    • Melis, A.1    Spangfort, M.2    Andersson, B.3
  • 34
    • 0034888190 scopus 로고    scopus 로고
    • The flanking regions of PsaD drive efficient gene expression in the nucleus of the green alga Chlamydomonas reinhardtii
    • (doi:10.1007/ s004380100485)
    • Fischer, N. & Rochaix, J. D. 2001 The flanking regions of PsaD drive efficient gene expression in the nucleus of the green alga Chlamydomonas reinhardtii. Mol. Genet. Genomics 265, 888-894. (doi:10.1007/ s004380100485)
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 888-894
    • Fischer, N.1    Rochaix, J.D.2
  • 36
    • 0035904396 scopus 로고    scopus 로고
    • A Streptomyces rimosus aphVIII gene coding for a new type phosphotransferase provides stable antibiotic resistance to Chlamydomonas reinhardtii
    • (doi:10.1016/S0378-1119(01)00616-3)
    • Sizova, I., Fuhrmann, M. & Hegemann, P. 2001 A Streptomyces rimosus aphVIII gene coding for a new type phosphotransferase provides stable antibiotic resistance to Chlamydomonas reinhardtii. Gene 277, 221-229. (doi:10.1016/S0378-1119(01)00616-3)
    • (2001) Gene , vol.277 , pp. 221-229
    • Sizova, I.1    Fuhrmann, M.2    Hegemann, P.3
  • 37
    • 0024743663 scopus 로고
    • The arginosuccinate lyase gene of Chlamydomonas reinhardtii: An important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus
    • Debuchy, R., Purton, S. & Rochaix, J. D. 1989 The arginosuccinate lyase gene of Chlamydomonas reinhardtii: an important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus. EMBO J. 8, 2803-2809.
    • (1989) EMBO J. , vol.8 , pp. 2803-2809
    • Debuchy, R.1    Purton, S.2    Rochaix, J.D.3
  • 38
    • 0025117612 scopus 로고
    • High-frequency nuclear transformation of Chlamydomonas reinhardtii
    • (doi:10.1073/pnas.87.3.1228)
    • Kindle, K. L. 1990 High-frequency nuclear transformation of Chlamydomonas reinhardtii. Proc. Natl Acad. Sci. USA 87, 1228-1232. (doi:10.1073/pnas.87.3.1228)
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1228-1232
    • Kindle, K.L.1
  • 39
    • 0026695501 scopus 로고
    • Expression of the arylsulfatase gene from the 2-tubulin promoter in Chlamydomonas reinhardtii
    • (doi:10.1093/nar/20.12.2959)
    • Davies, J., Weeks, D. P. & Grossman, A. R. 1992 Expression of the arylsulfatase gene from the 2-tubulin promoter in Chlamydomonas reinhardtii. Nucleic Acids Res. 20, 2959-2965. (doi:10.1093/nar/20.12.2959)
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2959-2965
    • Davies, J.1    Weeks, D.P.2    Grossman, A.R.3
  • 40
    • 0026603642 scopus 로고
    • Purification of Chlamydomonas 28-kDa ubiquitinated protein and its identification as ubiquitinated histone H2B
    • (doi:10.1016/0003-9861(92)90157-R)
    • Shimogawara, K. & Muto, S. 1992 Purification of Chlamydomonas 28-kDa ubiquitinated protein and its identification as ubiquitinated histone H2B. Arch. Biochem. Biophys. 294, 193-199. (doi:10.1016/0003-9861(92)90157-R)
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 193-199
    • Shimogawara, K.1    Muto, S.2
  • 41
    • 34548853382 scopus 로고    scopus 로고
    • A rapid method for chloroplast isolation from the green alga Chlamydomonas reinhardtii
    • (doi:10.1038/nprot.2006.348)
    • Mason, C. B., Bricker, T. M. & Moroney, J. V. 2006 A rapid method for chloroplast isolation from the green alga Chlamydomonas reinhardtii. Nat. Protocols 1, 2227-2230. (doi:10.1038/nprot.2006.348)
    • (2006) Nat. Protocols , vol.1 , pp. 2227-2230
    • Mason, C.B.1    Bricker, T.M.2    Moroney, J.V.3
  • 42
    • 0011193963 scopus 로고
    • Chloroplast envelope proteins from Chlamydomonas: Separation into outer and inner envelopes and analysis by twodimensional gel electrophoresis
    • (doi:10.1016/0005-2736(88)90570-6)
    • Clemetson, J. M. & Boschetti, A. 1988 Chloroplast envelope proteins from Chlamydomonas: separation into outer and inner envelopes and analysis by twodimensional gel electrophoresis. Biochim. Biophys. Acta 943, 371-374. (doi:10.1016/0005-2736(88)90570-6)
    • (1988) Biochim. Biophys. Acta , vol.943 , pp. 371-374
    • Clemetson, J.M.1    Boschetti, A.2
  • 43
    • 0001436139 scopus 로고
    • The low CO,-inducible 36-kilodalton protein is localized to the chloroplast envelope of Chlamydomonas reinhardtii
    • Ramazanov, Z., Mason, C. B., Geraghty, A. M., Spalding, M. H. & Moroney, J. V. 1993 The low CO,-inducible 36-kilodalton protein is localized to the chloroplast envelope of Chlamydomonas reinhardtii. Plant Physiol. 101, 1195-1199.
    • (1993) Plant Physiol. , vol.101 , pp. 1195-1199
    • Ramazanov, Z.1    Mason, C.B.2    Geraghty, A.M.3    Spalding, M.H.4    Moroney, J.V.5
  • 44
    • 0028082719 scopus 로고
    • Polypeptide composition, assembly and phosphorylation patterns of the photosystem II antenna system of Chlamydomonas reinhardtii
    • (doi:10.1007/BF00201033)
    • Allen, K. D. & Staehelin, L. A. 1994 Polypeptide composition, assembly and phosphorylation patterns of the photosystem II antenna system of Chlamydomonas reinhardtii. Planta 194, 42-54. (doi:10.1007/BF00201033)
    • (1994) Planta , vol.194 , pp. 42-54
    • Allen, K.D.1    Staehelin, L.A.2
  • 45
    • 0001231299 scopus 로고
    • Stoichiometry of system I and system II reaction centers and of plastoquinone in different photosynthetic membranes
    • (doi:10.1073/pnas.77.8.4712)
    • Melis, A. & Brown, J. S. 1980 Stoichiometry of system I and system II reaction centers and of plastoquinone in different photosynthetic membranes. Proc. Natl Acad. Sci. USA 77, 4712-4716. (doi:10.1073/pnas.77.8.4712)
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 4712-4716
    • Melis, A.1    Brown, J.S.2
  • 46
    • 0000332775 scopus 로고
    • Response of the photosynthetic apparatus in Dunaliella salina (green algae) to irradiance stress
    • (doi:10.1104/pp.93.4.1433)
    • Smith, B. M., Morrissey, P. J., Guenther, J. E., Nemson, J. A., Harrison, M. A., Allen, J. F. & Melis, A. 1990 Response of the photosynthetic apparatus in Dunaliella salina (green algae) to irradiance stress. Plant Physiol. 93, 1433-1440. (doi:10.1104/pp.93.4.1433)
    • (1990) Plant Physiol. , vol.93 , pp. 1433-1440
    • Smith, B.M.1    Morrissey, P.J.2    Guenther, J.E.3    Nemson, J.A.4    Harrison, M.A.5    Allen, J.F.6    Melis, A.7
  • 47
    • 0002517303 scopus 로고
    • Spectroscopic methods in photosynthesis: Photosystem stoichiometry and chlorophyll antenna size
    • (doi:10.1098/rstb.1989.0019)
    • Melis, A. 1989 Spectroscopic methods in photosynthesis: photosystem stoichiometry and chlorophyll antenna size. Phil. Trans. R. Soc. Lond. B 323, 397-409. (doi:10.1098/rstb.1989.0019)
    • (1989) Phil. Trans. R. Soc. Lond. B , vol.323 , pp. 397-409
    • Melis, A.1
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • (doi:10.1038/227680a0)
    • Laemmli, U. K. 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. (doi:10.1038/227680a0)
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 0000116657 scopus 로고
    • Structural and functional organization of the photosystems in spinach chloroplasts: Antenna size, relative electron transport capacity and chlorophyll composition
    • Melis, A. & Anderson, J.M. 1983 Structural and functional organization of the photosystems in spinach chloroplasts: antenna size, relative electron transport capacity and chlorophyll composition. Biochim. Biophys. Acta 724, 473-484.
    • (1983) Biochim. Biophys. Acta , vol.724 , pp. 473-484
    • Melis, A.1    Anderson, J.M.2
  • 50
    • 0025393626 scopus 로고
    • Analysis of Chlamydomonas reinhardtii histones and chromatin
    • Morris, R. L., Keller, L. R., Zweidler, A. & Rizzo, P. J. 1990 Analysis of Chlamydomonas reinhardtii histones and chromatin. J. Protozool. 37, 117-123.
    • (1990) J. Protozool. , vol.37 , pp. 117-123
    • Morris, R.L.1    Keller, L.R.2    Zweidler, A.3    Rizzo, P.J.4
  • 52
    • 0035651544 scopus 로고    scopus 로고
    • Molecular recognition in thylakoid structure and function
    • (doi:10.1016/S1360-1385(01)02010-6)
    • Allen, J. F. & 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
  • 53
    • 0034799118 scopus 로고    scopus 로고
    • The redox state of the plastoquinone pool controls the level of the light-harvesting chlorophyll a/b binding protein complex II (LHC II) during photoacclimation: Cytochrome b(6)f deficient Lemna perpusilla plants are locked in a state of high-light acclimation
    • (doi:10.1023/A:1011849919438)
    • Yang, D. H., Andersson, B., Aro, E. M. & Ohad, I. 2001 The redox state of the plastoquinone pool controls the level of the light-harvesting chlorophyll a/b binding protein complex II (LHC II) during photoacclimation: cytochrome b(6)f deficient Lemna perpusilla plants are locked in a state of high-light acclimation. Photosynth. Res. 68, 163-174. (doi:10.1023/A:1011849919438)
    • (2001) Photosynth. Res. , vol.68 , pp. 163-174
    • Yang, D.H.1    Andersson, B.2    Aro, E.M.3    Ohad, I.4
  • 54
    • 33644828133 scopus 로고    scopus 로고
    • NAB1 is an RNA binding protein involved in the light-regulated differential expression of the light-harvesting antenna of Chlamydomonas reinhardtii
    • (doi:10.1105/tpc.105.035774)
    • Mussgnug, J. H. et al. 2005 NAB1 is an RNA binding protein involved in the light-regulated differential expression of the light-harvesting antenna of Chlamydomonas reinhardtii. Plant Cell 17, 3409-3421. (doi:10.1105/tpc.105.035774)
    • (2005) Plant Cell , vol.17 , pp. 3409-3421
    • Mussgnug, J.H.1
  • 55
    • 0033784328 scopus 로고    scopus 로고
    • Acclimation of Chlamydomonas reinhardtii to its nutrient environment
    • (doi:10.1078/1434-4610-00020)
    • Grossman, A. 2000 Acclimation of Chlamydomonas reinhardtii to its nutrient environment. Protist 151, 201-224. (doi:10.1078/1434-4610-00020)
    • (2000) Protist , vol.151 , pp. 201-224
    • Grossman, A.1
  • 56
    • 0000621957 scopus 로고
    • Effect of light intensity during growth of Atriplex patula on the capacity of photosynthetic reactions, chloroplast components and structure
    • Bjorkman et al. 1972 Effect of light intensity during growth of Atriplex patula on the capacity of photosynthetic reactions, chloroplast components and structure. Camegie Inst. Yearbook 71, 115-135.
    • (1972) Camegie Inst. Yearbook , vol.71 , pp. 115-135
    • Bjorkman1
  • 57
    • 0028467779 scopus 로고
    • Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes
    • (doi:10.1007/BF00029601)
    • Li, H. M., Kaneko, Y. & Keegstra, K. 1994 Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes. Plant Mol. Biol. 25, 619-632. (doi:10.1007/BF00029601)
    • (1994) Plant Mol. Biol. , vol.25 , pp. 619-632
    • Li, H.M.1    Kaneko, Y.2    Keegstra, K.3
  • 59
    • 14844293494 scopus 로고    scopus 로고
    • J-Domain protein CDJ2 andHSP70Bare a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1
    • (doi:10.1091/mbc.E04-08-0736)
    • Liu, C., Willmund, F., Whitelegge, J. P., Hawat, S., Knapp, B., Lodha, M. & Schroda, M. 2005 J-Domain protein CDJ2 andHSP70Bare a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1. Mol. Biol. Cell 16, 1165-1177. (doi:10.1091/mbc.E04-08-0736)
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1165-1177
    • Liu, C.1    Willmund, F.2    Whitelegge, J.P.3    Hawat, S.4    Knapp, B.5    Lodha, M.6    Schroda, M.7
  • 60
    • 59349113257 scopus 로고    scopus 로고
    • Depletion ofVIPP1in Synechocystis sp PCC6803 affects photosynthetic activity before the loss of thylakoid membranes
    • (doi:10.1111/j.1574-6968.2008.01470.x)
    • Gao, H. &Xu, X. 2009Depletion ofVIPP1in Synechocystis sp. PCC6803 affects photosynthetic activity before the loss of thylakoid membranes. FEMS Microbiol. Lett. 292, 63-70. (doi:10.1111/j.1574-6968.2008.01470.x)
    • (2009) FEMS Microbiol. Lett. , vol.292 , pp. 63-70
    • Gao, H.1    Xu, X.2
  • 61
    • 33646236590 scopus 로고    scopus 로고
    • Mapping the Arabidopsis organelle proteome
    • (doi:10.1073/pnas.0506958103)
    • Dunkley, T. P. J. et al. 2006 Mapping the Arabidopsis organelle proteome. Proc. Natl Acad. Sci. USA 103, 6518-6523. (doi:10.1073/pnas.0506958103)
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6518-6523
    • Dunkley, T.P.J.1
  • 62
    • 1842432608 scopus 로고    scopus 로고
    • The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions
    • (doi:10.1016/j.cub.2004.02.039)
    • Kleffmann, T., Russenberger, D., von Zychlinski, A., Christopher, W., Sjolander, K., Gruissem, W. & Baginsky, S. 2004 The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. Curr. Biol. 14, 354-362. (doi:10.1016/j.cub.2004.02.039)
    • (2004) Curr. Biol. , vol.14 , pp. 354-362
    • Kleffmann, T.1    Russenberger, D.2    von Zychlinski, A.3    Christopher, W.4    Sjolander, K.5    Gruissem, W.6    Baginsky, S.7
  • 63
    • 71249157340 scopus 로고    scopus 로고
    • Chloroplast proteins without cleavable transit peptides: Rare exceptions or a major constituent of the chloroplast proteome?
    • (doi:10.1093/mp/ssp082)
    • Armbruster, U. et al. 2009 Chloroplast proteins without cleavable transit peptides: rare exceptions or a major constituent of the chloroplast proteome? Mol. Plant 2, 1325-1335. (doi:10.1093/mp/ssp082)
    • (2009) Mol. Plant , vol.2 , pp. 1325-1335
    • Armbruster, U.1
  • 64
    • 0037033102 scopus 로고    scopus 로고
    • Non-canonical transit peptide for import into the chloroplast
    • (doi:10.1074/jbc.M207477200)
    • Miras, S., Salvi, D., Ferro, M., Grunwald, D., Garin, J., Joyard, J. & Rolland, N. 2002 Non-canonical transit peptide for import into the chloroplast. J. Biol. Chem. 277, 47 770-47 778. (doi:10.1074/jbc.M207477200)
    • (2002) J. Biol. Chem. , vol.277
    • Miras, S.1    Salvi, D.2    Ferro, M.3    Grunwald, D.4    Garin, J.5    Joyard, J.6    Rolland, N.7
  • 65
    • 35748972640 scopus 로고    scopus 로고
    • Toc159-and Toc75-independent import of a transit sequence-less precursor into the inner envelope of chloroplasts
    • (doi:10.1074/jbc.M611112200)
    • Miras, S., Salvi, D., Piette, L., Seigneurin-Berny, D., Grunwald, D., Reinbothe, C., Joyard, J., Reinbothe, S. & Rolland, N. 2007 Toc159-and Toc75-independent import of a transit sequence-less precursor into the inner envelope of chloroplasts. J. Biol. Chem. 282, 29 482-29 492. (doi:10.1074/jbc.M611112200)
    • (2007) J. Biol. Chem. , vol.282
    • Miras, S.1    Salvi, D.2    Piette, L.3    Seigneurin-Berny, D.4    Grunwald, D.5    Reinbothe, C.6    Joyard, J.7    Reinbothe, S.8    Rolland, N.9
  • 67
    • 4444230596 scopus 로고    scopus 로고
    • Inner envelope protein 32 is imported into chloroplasts by a novel pathway
    • (doi:10.1242/jcs.01265)
    • Nada, A. & Soll, J. 2004 Inner envelope protein 32 is imported into chloroplasts by a novel pathway. J. Cell Sci. 117, 3975-3982. (doi:10.1242/jcs.01265)
    • (2004) J. Cell Sci. , vol.117 , pp. 3975-3982
    • Nada, A.1    Soll, J.2
  • 68
    • 47249152709 scopus 로고    scopus 로고
    • Targeting of nucleus-encoded proteins to chloroplasts in plants
    • (doi:10.1111/j.1469-8137.2008.02452.x)
    • Jarvis, P. 2008 Targeting of nucleus-encoded proteins to chloroplasts in plants. New Phytol. 179, 257-285. (doi:10.1111/j.1469-8137.2008.02452.x)
    • (2008) New Phytol. , vol.179 , pp. 257-285
    • Jarvis, P.1
  • 69
    • 28544447361 scopus 로고    scopus 로고
    • Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast
    • (doi:10.1038/ncb1330)
    • Villarejo, A. et al. 2005 Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast. Nat. Cell Biol. 7, 1124-1140. (doi:10.1038/ncb1330)
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1124-1140
    • Villarejo, A.1
  • 70
    • 33746368041 scopus 로고    scopus 로고
    • Evidence for an ER to Golgi to chloroplast protein transport pathway
    • (doi:10.1016/j.tcb.2006.06.003)
    • Radhamony, R.N. & Theg, S.M. 2006 Evidence for an ER to Golgi to chloroplast protein transport pathway. Trends Cell Biol. 16, 385-387. (doi:10.1016/j.tcb.2006.06.003)
    • (2006) Trends Cell Biol. , vol.16 , pp. 385-387
    • Radhamony, R.N.1    Theg, S.M.2


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