메뉴 건너뛰기




Volumn 14, Issue 9, 2002, Pages 2303-2314

Loss of Albino3 leads to the specific depletion of the light-harvesting system

Author keywords

[No Author keywords available]

Indexed keywords

CHLOROPHYLL; ENZYMES; ESCHERICHIA COLI; GENES; HARVESTING; MUTAGENESIS;

EID: 0036737470     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.003442     Document Type: Article
Times cited : (89)

References (47)
  • 1
    • 0033198467 scopus 로고    scopus 로고
    • Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes
    • Amin, P., Sy, D.A., Pilgrim, M.L., Parry, D.H., Nussaume, L., and Hoffman, N.E. (1999). Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes. Plant Physiol. 121, 61-70.
    • (1999) Plant Physiol. , vol.121 , pp. 61-70
    • Amin, P.1    Sy, D.A.2    Pilgrim, M.L.3    Parry, D.H.4    Nussaume, L.5    Hoffman, N.E.6
  • 2
    • 0033860532 scopus 로고    scopus 로고
    • Participation of nuclear genes in chloroplast gene expression
    • Barkan, A., and Goldschmidt-Clermont, M. (2000). Participation of nuclear genes in chloroplast gene expression. Biochimie 82, 559-572.
    • (2000) Biochimie , vol.82 , pp. 559-572
    • Barkan, A.1    Goldschmidt-Clermont, M.2
  • 3
    • 0030889911 scopus 로고    scopus 로고
    • Molecular identification of a novel protein that regulates biogenesis of photosystem I, a membrane protein complex
    • Bartsevich, V.V., and Pakrasi, H.B. (1997). Molecular identification of a novel protein that regulates biogenesis of photosystem I, a membrane protein complex. J. Biol. Chem. 272, 6382-6387.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6382-6387
    • Bartsevich, V.V.1    Pakrasi, H.B.2
  • 4
    • 0028245283 scopus 로고
    • OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes, controls cytochrome oxidase biogenesis
    • Bonnefoy, N., Chalvet, F., Hamel, P., Slonimski, P.P., and Dujardin, G. (1994). OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes, controls cytochrome oxidase biogenesis. J. Mol. Biol. 239, 201-212.
    • (1994) J. Mol. Biol. , vol.239 , pp. 201-212
    • Bonnefoy, N.1    Chalvet, F.2    Hamel, P.3    Slonimski, P.P.4    Dujardin, G.5
  • 5
    • 0030664113 scopus 로고    scopus 로고
    • The chloroplast ycf3 and ycf4 open reading frames of Chlamydomonas reinhardtii are required for the accumulation of the photosystem I complex
    • Boudreau, E., Takahashi, Y., Lemieux, C., Turmel, M., and Rochaix, J.D. (1997). The chloroplast ycf3 and ycf4 open reading frames of Chlamydomonas reinhardtii are required for the accumulation of the photosystem I complex. EMBO J. 16, 6095-6104.
    • (1997) EMBO J. , vol.16 , pp. 6095-6104
    • Boudreau, E.1    Takahashi, Y.2    Lemieux, C.3    Turmel, M.4    Rochaix, J.D.5
  • 6
    • 0014219621 scopus 로고
    • Chlamydomonas reinhardtii: Heterozygous diploid strains
    • Ebersold, W.T. (1967). Chlamydomonas reinhardtii: Heterozygous diploid strains. Science 157, 447-449.
    • (1967) Science , vol.157 , pp. 447-449
    • Ebersold, W.T.1
  • 7
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson, O., Nielsen, H., and von Heijne, G. (1999). ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8, 978-984.
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 8
    • 0024679389 scopus 로고
    • Characterization of a Chlamydomonas transposon, Gulliver, resembling those in higher plants
    • Ferris, P.J. (1989). Characterization of a Chlamydomonas transposon, Gulliver, resembling those in higher plants. Genetics 122, 363-377.
    • (1989) Genetics , vol.122 , pp. 363-377
    • Ferris, P.J.1
  • 9
    • 0029083422 scopus 로고
    • Localization of the nic-7, ac-29 and thi-10 genes within the mating-type locus of Chlamydomonas reinhardtii
    • Ferris, P.J. (1995). Localization of the nic-7, ac-29 and thi-10 genes within the mating-type locus of Chlamydomonas reinhardtii. Genetics 141, 543-549.
    • (1995) Genetics , vol.141 , pp. 543-549
    • Ferris, P.J.1
  • 10
    • 0028297314 scopus 로고
    • The mating-type locus of Chlamydomonas reinhardtii contains highly rearranged DNA sequences
    • Ferris, P.J., and Goodenough, U.W. (1994). The mating-type locus of Chlamydomonas reinhardtii contains highly rearranged DNA sequences. Cell 76, 1135-1145.
    • (1994) Cell , vol.76 , pp. 1135-1145
    • Ferris, P.J.1    Goodenough, U.W.2
  • 11
    • 0034888190 scopus 로고    scopus 로고
    • The flanking regions of PsaD drive efficient gene expression in the nucleus of the green alga Chlamydomonas reinhardtii
    • Fischer, N., and 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.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 888-894
    • Fischer, N.1    Rochaix, J.D.2
  • 12
    • 0342618603 scopus 로고    scopus 로고
    • Targeted mutations in the psaC gene of Chlamydomonas reinhardtii: Preferential reduction of FB at low temperature is not accompanied by altered electron flow from photosystem I to ferredoxin
    • Fischer, N., Setif, P., and Rochaix, J.D. (1997). Targeted mutations in the psaC gene of Chlamydomonas reinhardtii: Preferential reduction of FB at low temperature is not accompanied by altered electron flow from photosystem I to ferredoxin. Biochemistry 36, 93-102.
    • (1997) Biochemistry , vol.36 , pp. 93-102
    • Fischer, N.1    Setif, P.2    Rochaix, J.D.3
  • 13
    • 0030464460 scopus 로고    scopus 로고
    • Seaview and Phylo_Win: Two graphic tools for sequence alignment and molecular phylogeny
    • Galtier, N., and Gouy, M. (1996). SEAVIEW and PHYLO_WIN: Two graphic tools for sequence alignment and molecular phylogeny. Comp. Appl Biosci. 12, 543-548.
    • (1996) Comp. Appl. Biosci. , vol.12 , pp. 543-548
    • Galtier, N.1    Gouy, M.2
  • 15
    • 0032478139 scopus 로고    scopus 로고
    • Oxa1p, an essential component of the N-tail protein export machinery in mitochondria
    • Hell, K., Herrmann, J.M., Pratje, E., Neupert, W., and Stuart, R.A. (1998). Oxa1p, an essential component of the N-tail protein export machinery in mitochondria. Proc. Natl. Acad. Sci. USA 95, 2250-2255.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2250-2255
    • Hell, K.1    Herrmann, J.M.2    Pratje, E.3    Neupert, W.4    Stuart, R.A.5
  • 16
    • 0035868763 scopus 로고    scopus 로고
    • Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA
    • Hell, K., Neupert, W., and Stuart, R.A. (2001). Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA. EMBO J. 20, 1281-1288.
    • (2001) EMBO J. , vol.20 , pp. 1281-1288
    • Hell, K.1    Neupert, W.2    Stuart, R.A.3
  • 17
    • 0034617438 scopus 로고    scopus 로고
    • Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA
    • Houben, E.N., Scotti, P.A., Valent, Q.A., Brunner, J., de Gier, J.L., Oudega, B., and Luirink, J. (2000). Nascent Lep inserts into the Escherichia coli inner membrane in the vicinity of YidC, SecY and SecA. FEBS Lett. 476, 229-233.
    • (2000) FEBS Lett. , vol.476 , pp. 229-233
    • Houben, E.N.1    Scotti, P.A.2    Valent, Q.A.3    Brunner, J.4    De Gier, J.L.5    Oudega, B.6    Luirink, J.7
  • 18
    • 0037205410 scopus 로고    scopus 로고
    • Chloroplast YidC homologue Albino3 can functionally complement the bacterial YidC depletion strain and promote membrane insertion of both bacterial and chloroplast thylakoid proteins
    • Jiang, F., Moore, M., Chen, M., Rohl, T., van Wijk, K., de Gier, J.-W., Henry, R., and Dalbey, R. (2002). Chloroplast YidC homologue Albino3 can functionally complement the bacterial YidC depletion strain and promote membrane insertion of both bacterial and chloroplast thylakoid proteins. J. Biol. Chem. 277, 19281-19288.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19281-19288
    • Jiang, F.1    Moore, M.2    Chen, M.3    Rohl, T.4    Van Wijk, K.5    De Gier, J.-W.6    Henry, R.7    Dalbey, R.8
  • 19
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • Keegstra, K., and Cline, K. (1999). Protein import and routing systems of chloroplasts. Plant Cell 11, 557-570.
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 20
    • 0025117612 scopus 로고
    • High-frequency nuclear transformation of Chlamydomonas reinhardtii
    • Kindle, K.L. (1990). High-frequency nuclear transformation of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 87, 1228-1232.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1228-1232
    • Kindle, K.L.1
  • 21
    • 6544282660 scopus 로고    scopus 로고
    • A chromodomain protein encoded by the Arabidopsis CAO gene is a plant-specific component of the chloroplast signal recognition particle pathway that is involved in LHCP targeting
    • Klimyuk, V.I., Persello-Cartieaux, F., Havaux, M., Contard-David, P., Schuenemann, D., Meiherhoff, K., Gouet, P., Jones, J.D., Hoffman, N.E., and Nussaume, L. (1999). A chromodomain protein encoded by the Arabidopsis CAO gene is a plant-specific component of the chloroplast signal recognition particle pathway that is involved in LHCP targeting. Plant Cell 11, 87-99.
    • (1999) Plant Cell , vol.11 , pp. 87-99
    • Klimyuk, V.I.1    Persello-Cartieaux, F.2    Havaux, M.3    Contard-David, P.4    Schuenemann, D.5    Meiherhoff, K.6    Gouet, P.7    Jones, J.D.8    Hoffman, N.E.9    Nussaume, L.10
  • 22
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E.L. (2001). Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305, 567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 23
    • 0014893430 scopus 로고
    • The genetics of photosynthesis and of the chloroplast in Chlamydomonas reinhardtii
    • Levine, R.P., and Goodenough, U.W. (1970). The genetics of photosynthesis and of the chloroplast in Chlamydomonas reinhardtii. Annu. Rev. Genet. 4, 397-408.
    • (1970) Annu. Rev. Genet. , vol.4 , pp. 397-408
    • Levine, R.P.1    Goodenough, U.W.2
  • 24
    • 0029041304 scopus 로고
    • A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes
    • Li, X., Henry, R., Yuan, J., Cline, K., and Hoffman, N.E. (1995). A chloroplast homologue of the signal recognition particle subunit SRP54 is involved in the posttranslational integration of a protein into thylakoid membranes. Proc. Natl. Acad. Sci. USA 92, 3789-3793.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3789-3793
    • Li, X.1    Henry, R.2    Yuan, J.3    Cline, K.4    Hoffman, N.E.5
  • 25
    • 0035854694 scopus 로고    scopus 로고
    • YidC/Oxa1p/Alb3: Evolutionarily conserved mediators of membrane protein assembly
    • Luirink, J., Samuelsson, T., and de Gier, J.W. (2001). YidC/Oxa1p/Alb3: Evolutionarily conserved mediators of membrane protein assembly. FEBS Lett. 501, 1-5.
    • (2001) FEBS Lett. , vol.501 , pp. 1-5
    • Luirink, J.1    Samuelsson, T.2    De Gier, J.W.3
  • 26
    • 0344404400 scopus 로고    scopus 로고
    • A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana
    • Meurer, J., Plucken, H., Kowallik, K.V., and Westhoff, P. (1998). A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana. EMBO J. 17, 5286-5297.
    • (1998) EMBO J. , vol.17 , pp. 5286-5297
    • Meurer, J.1    Plucken, H.2    Kowallik, K.V.3    Westhoff, P.4
  • 27
    • 0034695557 scopus 로고    scopus 로고
    • Chloroplast Oxa1p homolog Albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes
    • Moore, M., Harrison, M.S., Peterson, E.C., and Henry, R. (2000). Chloroplast Oxa1p homolog albino3 is required for post-translational integration of the light harvesting chlorophyll-binding protein into thylakoid membranes. J. Biol. Chem. 275, 1529-1532.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1529-1532
    • Moore, M.1    Harrison, M.S.2    Peterson, E.C.3    Henry, R.4
  • 28
    • 0037066703 scopus 로고    scopus 로고
    • The Oxa1 protein forms a homooligomeric complex and is an essential part of the mitochondrial export translocase in Neurospora crassa
    • Nargang, F.E., Preuss, M., Neupert, W., and Herrmann, J.M. (2002). The Oxa1 protein forms a homooligomeric complex and is an essential part of the mitochondrial export translocase in Neurospora crassa. J. Biol. Chem. 277, 12846-12853.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12846-12853
    • Nargang, F.E.1    Preuss, M.2    Neupert, W.3    Herrmann, J.M.4
  • 29
    • 0028279252 scopus 로고
    • The CRY1 gene in Chlamydomonas reinhardtii: Structure and use as a dominant selectable marker for nuclear transformation
    • Nelson, J.A., Savereide, P.B., and Lefebvre, P.A. (1994). The CRY1 gene in Chlamydomonas reinhardtii: Structure and use as a dominant selectable marker for nuclear transformation. Mol. Cell. Biol. 14, 4011-4019.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4011-4019
    • Nelson, J.A.1    Savereide, P.B.2    Lefebvre, P.A.3
  • 30
    • 0033081464 scopus 로고    scopus 로고
    • Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54
    • Nilsson, R., Brunner, J., Hoffman, N.E., and van Wijk, K.J. (1999). Interactions of ribosome nascent chain complexes of the chloroplast-encoded D1 thylakoid membrane protein with cpSRP54. EMBO J. 18, 733-742.
    • (1999) EMBO J. , vol.18 , pp. 733-742
    • Nilsson, R.1    Brunner, J.2    Hoffman, N.E.3    Van Wijk, K.J.4
  • 31
    • 0033571587 scopus 로고    scopus 로고
    • A factor related to pseudouridine synthases is required for chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii
    • Perron, K., Goldschmidt-Clermont, M., and Rochaix, J.D. (1999). A factor related to pseudouridine synthases is required for chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii. EMBO J. 18, 6481-6490.
    • (1999) EMBO J. , vol.18 , pp. 6481-6490
    • Perron, K.1    Goldschmidt-Clermont, M.2    Rochaix, J.D.3
  • 32
    • 0033849640 scopus 로고    scopus 로고
    • Photosynthetic apparatus organization and function in the wild type and a chlorophyll b-less mutant of Chlamydomonas reinhardtii: Dependence on carbon source
    • Polle, J.E., Benemann, J.R., Tanaka, A., and Melis, A. (2000). Photosynthetic apparatus organization and function in the wild type and a chlorophyll b-less mutant of Chlamydomonas reinhardtii: Dependence on carbon source. Planta 211, 335-344.
    • (2000) Planta , vol.211 , pp. 335-344
    • Polle, J.E.1    Benemann, J.R.2    Tanaka, A.3    Melis, A.4
  • 33
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra, R., Thompson, W., and Kriedemann, P. (1989). Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta 975, 384-394.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.1    Thompson, W.2    Kriedemann, P.3
  • 34
    • 0035350689 scopus 로고    scopus 로고
    • Protein targeting by the twin-arginine translocation pathway
    • Robinson, C., and Bolhuis, A. (2001). Protein targeting by the twin-arginine translocation pathway. Nat. Rev. Mol. Cell Biol. 2, 350-356.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 350-356
    • Robinson, C.1    Bolhuis, A.2
  • 35
    • 1842301050 scopus 로고    scopus 로고
    • Targeted inactivation of a tobacco intron-containing open reading frame reveals a novel chloroplast-encoded photosystem I-related gene
    • Ruf, S., Kossel, H., and Bock, R. (1997). Targeted inactivation of a tobacco intron-containing open reading frame reveals a novel chloroplast-encoded photosystem I-related gene. J. Cell Biol. 139, 95-102.
    • (1997) J. Cell Biol. , vol.139 , pp. 95-102
    • Ruf, S.1    Kossel, H.2    Bock, R.3
  • 36
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic tree
    • Saitou, N., and Nei, M. (1987). The neighbor-joining method: A new method for reconstructing phylogenetic tree. Mol. Biol. Evol. 4, 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 38
    • 0025374557 scopus 로고
    • A Chlamydomonas gene encodes a G protein β subunit-like polypeptide
    • Schloss, J.A. (1990). A Chlamydomonas gene encodes a G protein β subunit-like polypeptide. Mol. Gen. Genet. 221, 443-452.
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 443-452
    • Schloss, J.A.1
  • 40
    • 0031131609 scopus 로고    scopus 로고
    • Albino3, an Arabidopsis nuclear gene essential for chloroplast differentiation, encodes a chloroplast protein that shows homology to proteins present in bacterial membranes and yeast mitochondria
    • Sundberg, E., Slagter, J.G., Fridborg, I., Cleary, S.P., Robinson, C., and Coupland, G. (1997). ALBINO3, an Arabidopsis nuclear gene essential for chloroplast differentiation, encodes a chloroplast protein that shows homology to proteins present in bacterial membranes and yeast mitochondria. Plant Cell 9, 717-730.
    • (1997) Plant Cell , vol.9 , pp. 717-730
    • Sundberg, E.1    Slagter, J.G.2    Fridborg, I.3    Cleary, S.P.4    Robinson, C.5    Coupland, G.6
  • 41
    • 0027968068 scopus 로고
    • ClustalW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). ClustalW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 0033578755 scopus 로고    scopus 로고
    • Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes
    • Tu, C.J., Schuenemann, D., and Hoffman, N.E. (1999). Chloroplast FtsY, chloroplast signal recognition particle, and GTP are required to reconstitute the soluble phase of light-harvesting chlorophyll protein transport into thylakoid membranes. J. Biol. Chem. 274, 27219-27224.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27219-27224
    • Tu, C.J.1    Schuenemann, D.2    Hoffman, N.E.3
  • 44
    • 0029294130 scopus 로고
    • Inactivation of a Synechocystis sp strain PCC 6803 gene with homology to conserved chloroplast open reading frame 184 increases the photosystem II-to-photosystem I ratio
    • Wilde, A., Hartel, H., Hubschmann, T., Hoffmann, P., Shestakov, S.V., and Borner, T. (1995). Inactivation of a Synechocystis sp strain PCC 6803 gene with homology to conserved chloroplast open reading frame 184 increases the photosystem II-to-photosystem I ratio. Plant Cell 7, 649-658.
    • (1995) Plant Cell , vol.7 , pp. 649-658
    • Wilde, A.1    Hartel, H.2    Hubschmann, T.3    Hoffmann, P.4    Shestakov, S.V.5    Borner, T.6
  • 46
    • 0033119032 scopus 로고    scopus 로고
    • Subcellular localization of the BtpA protein in the cyanobacterium Synechocystis sp. PCC 6803
    • Zak, E., Norling, B., Andersson, B., and Pakrasi, H.B. (1999). Subcellular localization of the BtpA protein in the cyanobacterium Synechocystis sp. PCC 6803. Eur. J. Biochem. 261, 311-316.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 311-316
    • Zak, E.1    Norling, B.2    Andersson, B.3    Pakrasi, H.B.4
  • 47
    • 0034126922 scopus 로고    scopus 로고
    • The BtpA protein stabilizes the reaction center proteins of photosystem I in the cyanobacterium Synechocystis sp. PCC 6803 at low temperature
    • Zak, E., and Pakrasi, H.B. (2000). The BtpA protein stabilizes the reaction center proteins of photosystem I in the cyanobacterium Synechocystis sp. PCC 6803 at low temperature. Plant Physiol. 123, 215-222.
    • (2000) Plant Physiol. , vol.123 , pp. 215-222
    • Zak, E.1    Pakrasi, H.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.