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Volumn 75, Issue 5, 2013, Pages 858-866

Identification of a cyanobacterial CRR6 protein, Slr1097, required for efficient assembly of NDH-1 complexes in Synechocystis sp. PCC 6803

Author keywords

assembly; cyclic electron transport; maturation; NDH 1 complexes; Synechocystis 6803

Indexed keywords

CYCLIC ELECTRON TRANSPORT; MATURATION; NDH-1 COMPLEX; STRONG INTERACTION; SYNECHOCYSTIS 6803; SYNECHOCYSTIS SP. PCC 6803; THYLAKOID MEMBRANES; YEAST TWO-HYBRID SYSTEM;

EID: 84883243697     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12251     Document Type: Article
Times cited : (32)

References (53)
  • 1
    • 84984087585 scopus 로고
    • Simple conditions for growth of unicellular blue-green algae on plates
    • Allen, M.M., (1968) Simple conditions for growth of unicellular blue-green algae on plates. J. Phycol. 4, 1-4.
    • (1968) J. Phycol. , vol.4 , pp. 1-4
    • Allen, M.M.1
  • 2
    • 33750514379 scopus 로고    scopus 로고
    • Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy
    • Arteni, A.A., Zhang, P., Battchikova, N., Ogawa, T., Aro, E.M., and, Boekema, E.J., (2006) Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy. Biochim. Biophys. Acta, 1757, 1469-1475.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1469-1475
    • Arteni, A.A.1    Zhang, P.2    Battchikova, N.3    Ogawa, T.4    Aro, E.M.5    Boekema, E.J.6
  • 3
    • 84874352529 scopus 로고    scopus 로고
    • Crystal structure of the entire respiratory complex i
    • Baradaran, R., Berrisford, J.M., Minhas, G.S., and, Sazanov, L.A., (2013) Crystal structure of the entire respiratory complex I. Nature, 494, 443-448.
    • (2013) Nature , vol.494 , pp. 443-448
    • Baradaran, R.1    Berrisford, J.M.2    Minhas, G.S.3    Sazanov, L.A.4
  • 4
    • 34547747897 scopus 로고    scopus 로고
    • Cyanobacterial NDH-1 complexes: Multiplicity in function and subunit composition
    • Battchikova, N., and, Aro, E.M., (2007) Cyanobacterial NDH-1 complexes: multiplicity in function and subunit composition. Physiol. Plant. 131, 22-32.
    • (2007) Physiol. Plant. , vol.131 , pp. 22-32
    • Battchikova, N.1    Aro, E.M.2
  • 5
    • 80054716347 scopus 로고    scopus 로고
    • Identification of a novel Ssl0352 Protein (NdhS), essential for efficient operation of cyclic electron transport around photosystem I, in NADPH:Plastoquinone oxidoreductase (NDH-1) complexes of Synechocystis sp. PCC 6803
    • Battchikova, N., Wei, L., Du, L., Bersanini, L., Aro, E.M., and, Ma, W., (2011a) Identification of a novel Ssl0352 Protein (NdhS), essential for efficient operation of cyclic electron transport around photosystem I, in NADPH:plastoquinone oxidoreductase (NDH-1) complexes of Synechocystis sp. PCC 6803. J. Biol. Chem. 286, 36992-37001.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36992-37001
    • Battchikova, N.1    Wei, L.2    Du, L.3    Bersanini, L.4    Aro, E.M.5    Ma, W.6
  • 6
    • 79958120495 scopus 로고    scopus 로고
    • Cyanobacterial NDH-1 complexes: Novel insights and remaining puzzles
    • Battchikova, N., Eisenhut, M., and, Aro, E.M., (2011b) Cyanobacterial NDH-1 complexes: novel insights and remaining puzzles. Biochim. Biophys. Acta, 1807, 935-944.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 935-944
    • Battchikova, N.1    Eisenhut, M.2    Aro, E.M.3
  • 7
    • 78650144629 scopus 로고    scopus 로고
    • + reduction in various ndh-deficient mutants of Synechocystis sp. Strain PCC6803
    • + reduction in various ndh-deficient mutants of Synechocystis sp. strain PCC6803. J. Bacteriol. 193, 292-295.
    • (2011) J. Bacteriol. , vol.193 , pp. 292-295
    • Bernát, G.1    Appel, J.2    Ogawa, T.3    Rögner, M.4
  • 8
    • 0032481317 scopus 로고    scopus 로고
    • Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes
    • Burrows, P.A., Sazanov, L.A., Svab, Z., Maliga, P., and, Nixon, P.J., (1998) Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes. EMBO J. 17, 868-876.
    • (1998) EMBO J. , vol.17 , pp. 868-876
    • Burrows, P.A.1    Sazanov, L.A.2    Svab, Z.3    Maliga, P.4    Nixon, P.J.5
  • 9
    • 0038347204 scopus 로고    scopus 로고
    • 2 on NAD(P)H dehydrogenase, a mediator of cyclic electron transport around photosystem i in the cyanobacterium Synechocystis PCC 6803
    • 2 on NAD(P)H dehydrogenase, a mediator of cyclic electron transport around photosystem I in the cyanobacterium Synechocystis PCC 6803. Plant Cell Physiol. 44, 534-540.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 534-540
    • Deng, Y.1    Ye, J.2    Mi, H.3
  • 10
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex i
    • Efremov, R.G., Baradaran, R., and, Sazanov, L.A., (2010) The architecture of respiratory complex I. Nature, 465, 441-445.
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 11
    • 0032790755 scopus 로고    scopus 로고
    • The role of chloroplastic NAD(P)H dehydrogenase in photoprotection
    • Endo, T., Shikanai, T., Takabayashi, A., Asada, K., and, Sato, F., (1999) The role of chloroplastic NAD(P)H dehydrogenase in photoprotection. FEBS Lett. 457, 5-8.
    • (1999) FEBS Lett. , vol.457 , pp. 5-8
    • Endo, T.1    Shikanai, T.2    Takabayashi, A.3    Asada, K.4    Sato, F.5
  • 12
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex i of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • Friedrich, T., and, Scheide, D., (2000) The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479, 1-5.
    • (2000) FEBS Lett. , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 13
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex i of bacteria and mitochondria and its homolog in chloroplasts
    • Friedrich, T., Steinmüller, K., and, Weiss, H., (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homolog in chloroplasts. FEBS Lett. 367, 107-111.
    • (1995) FEBS Lett. , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmüller, K.2    Weiss, H.3
  • 14
    • 0028606359 scopus 로고
    • The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane lipids: A mechanism of chilling tolerance
    • Gombos, Z., Wada, H., and, Murata, N., (1994) The recovery of photosynthesis from low-temperature photoinhibition is accelerated by the unsaturation of membrane lipids: a mechanism of chilling tolerance. Proc. Natl Acad. Sci. USA, 91, 8787-8791.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 8787-8791
    • Gombos, Z.1    Wada, H.2    Murata, N.3
  • 15
    • 0345393082 scopus 로고    scopus 로고
    • A nucleus-encoded factor, CRR2, is essential for the expression of chloroplast ndhB in Arabidopsis
    • Hashimoto, M., Endo, T., Peltier, G., Tasaka, M., and, Shikanai, T., (2003) A nucleus-encoded factor, CRR2, is essential for the expression of chloroplast ndhB in Arabidopsis. Plant J. 36, 541-549.
    • (2003) Plant J. , vol.36 , pp. 541-549
    • Hashimoto, M.1    Endo, T.2    Peltier, G.3    Tasaka, M.4    Shikanai, T.5
  • 16
    • 80052879596 scopus 로고    scopus 로고
    • Structure of the chloroplast NADH dehydrogenase-like complex: Nomenclature for nuclear-encoded subunits
    • Ifuku, K., Endo, T., Shikanai, T., and, Aro, E.M., (2011) Structure of the chloroplast NADH dehydrogenase-like complex: nomenclature for nuclear-encoded subunits. Plant Cell Physiol. 52, 1560-1568.
    • (2011) Plant Cell Physiol. , vol.52 , pp. 1560-1568
    • Ifuku, K.1    Endo, T.2    Shikanai, T.3    Aro, E.M.4
  • 17
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. Strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko, T., Sato, S., Kotani, H., et al,. (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3, 109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3
  • 18
    • 0030829823 scopus 로고    scopus 로고
    • Analysis of the chloroplast protein complexes by blue-native polyacrylamide gel electrophoresis (BN-PAGE)
    • Kügler, M., Jänsch, L., Kruft, V., Schmitz, U.K., and, Braun, H.P., (1997) Analysis of the chloroplast protein complexes by blue-native polyacrylamide gel electrophoresis (BN-PAGE). Photosynth. Res. 53, 35-44.
    • (1997) Photosynth. Res. , vol.53 , pp. 35-44
    • Kügler, M.1    Jänsch, L.2    Kruft, V.3    Schmitz, U.K.4    Braun, H.P.5
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K., (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 1642441937 scopus 로고    scopus 로고
    • The universally conserved HCF101 protein is involved in assembly of [4Fe-4S]-cluster-containing complexes in Arabidopsis thaliana chloroplasts
    • Lezhneva, L., Amann, K., and, Meurer, J., (2004) The universally conserved HCF101 protein is involved in assembly of [4Fe-4S]-cluster-containing complexes in Arabidopsis thaliana chloroplasts. Plant J. 37, 174-185.
    • (2004) Plant J. , vol.37 , pp. 174-185
    • Lezhneva, L.1    Amann, K.2    Meurer, J.3
  • 21
    • 63349097295 scopus 로고    scopus 로고
    • Identification, regulation and physiological functions of multiple NADPH dehydrogenase complexes in cyanobacteria
    • Ma, W., (2009) Identification, regulation and physiological functions of multiple NADPH dehydrogenase complexes in cyanobacteria. Front. Biol. China, 4, 137-142.
    • (2009) Front. Biol. China , vol.4 , pp. 137-142
    • Ma, W.1
  • 22
    • 24644456357 scopus 로고    scopus 로고
    • Expression and activity of type 1 NAD(P)H dehydrogenase at different growth phases of cyanobacterium, Synechocystis PCC6803
    • Ma, W., and, Mi, H., (2005) Expression and activity of type 1 NAD(P)H dehydrogenase at different growth phases of cyanobacterium, Synechocystis PCC6803. Physiol. Plant. 125, 135-140.
    • (2005) Physiol. Plant. , vol.125 , pp. 135-140
    • Ma, W.1    Mi, H.2
  • 23
    • 0036845754 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii plastid chromosome: Islands of genes in a sea of repeats
    • Maul, J.E., Lilly, J.W., Cui, L., dePamphilis, C.W., Miller, W., Harris, E.H., and, Stern, D.B., (2002) The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats. Plant Cell, 14, 2659-2679.
    • (2002) Plant Cell , vol.14 , pp. 2659-2679
    • Maul, J.E.1    Lilly, J.W.2    Cui, L.3    Depamphilis, C.W.4    Miller, W.5    Harris, E.H.6    Stern, D.B.7
  • 24
    • 77957187653 scopus 로고
    • Electron donation from cyclic and respiratory flows to the photosynthetic intersystem chain is mediated by pyridine nucleotide dehydrogenase in the cyanobacterium Synechocystis PCC 6803
    • Mi, H., Endo, T., Schreiber, U., Ogawa, T., and, Asada, K., (1992) Electron donation from cyclic and respiratory flows to the photosynthetic intersystem chain is mediated by pyridine nucleotide dehydrogenase in the cyanobacterium Synechocystis PCC 6803. Plant Cell Physiol. 33, 1233-1237.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 1233-1237
    • Mi, H.1    Endo, T.2    Schreiber, U.3    Ogawa, T.4    Asada, K.5
  • 25
    • 0028814979 scopus 로고
    • Thylakoid membrane-bound pyridine nucleotide dehydrogenase complex mediates cyclic electron transport in the cyanobacteria Synechocystis PCC 6803
    • Mi, H., Endo, T., Ogawa, T., and, Asada, K., (1995) Thylakoid membrane-bound pyridine nucleotide dehydrogenase complex mediates cyclic electron transport in the cyanobacteria Synechocystis PCC 6803. Plant Cell Physiol. 36, 661-668.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 661-668
    • Mi, H.1    Endo, T.2    Ogawa, T.3    Asada, K.4
  • 26
    • 33644878578 scopus 로고    scopus 로고
    • Identification of a novel protein, CRR7, required for the stabilization of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis
    • Munshi, M.K., Kobayashi, Y., and, Shikanai, T., (2005) Identification of a novel protein, CRR7, required for the stabilization of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis. Plant J. 44, 1036-1044.
    • (2005) Plant J. , vol.44 , pp. 1036-1044
    • Munshi, M.K.1    Kobayashi, Y.2    Shikanai, T.3
  • 27
    • 33745678982 scopus 로고    scopus 로고
    • Chlororespiratory reduction 6 is a novel factor required for accumulation of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis
    • Munshi, M.K., Kobayashi, Y., and, Shikanai, T., (2006) Chlororespiratory reduction 6 is a novel factor required for accumulation of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis. Plant Physiol. 141, 737-744.
    • (2006) Plant Physiol. , vol.141 , pp. 737-744
    • Munshi, M.K.1    Kobayashi, Y.2    Shikanai, T.3
  • 28
    • 0025845648 scopus 로고
    • A gene homologous to the subunit-2 gene of NADH dehydrogenase is essential to inorganic carbon transport of Synechocystis PCC 6803
    • Ogawa, T., (1991) A gene homologous to the subunit-2 gene of NADH dehydrogenase is essential to inorganic carbon transport of Synechocystis PCC 6803. Proc. Natl Acad. Sci. USA, 88, 4275-4279.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4275-4279
    • Ogawa, T.1
  • 29
    • 34547805062 scopus 로고    scopus 로고
    • Cyanobacterial NADPH dehydrogenase complexes
    • Ogawa, T., and, 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
  • 30
    • 0034644777 scopus 로고    scopus 로고
    • Two types of functionally distinct NAD(P)H dehydrogenases in Synechocystis sp. Strain PCC6803
    • Ohkawa, H., Pakrasi, H.B., and, Ogawa, T., (2000) Two types of functionally distinct NAD(P)H dehydrogenases in Synechocystis sp. strain PCC6803. J. Biol. Chem. 275, 31630-31634.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31630-31634
    • Ohkawa, H.1    Pakrasi, H.B.2    Ogawa, T.3
  • 31
    • 0034900957 scopus 로고    scopus 로고
    • Localization of NAD(P)H dehydrogenase in the cyanobacterium Synechocystis sp. Strain PCC 6803
    • Ohkawa, H., Sonoda, M., Shibata, M., and, Ogawa, T., (2001) Localization of NAD(P)H dehydrogenase in the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 183, 4938-4939.
    • (2001) J. Bacteriol. , vol.183 , pp. 4938-4939
    • Ohkawa, H.1    Sonoda, M.2    Shibata, M.3    Ogawa, T.4
  • 32
    • 0036326617 scopus 로고    scopus 로고
    • Functionally distinct NAD(P)H dehydrogenases and their membrane localization in Synechocystis sp. PCC6803
    • Ohkawa, H., Sonoda, M., Hagino, N., Shibata, M., Pakrasi, H.B., and, Ogawa, T., (2002) Functionally distinct NAD(P)H dehydrogenases and their membrane localization in Synechocystis sp. PCC6803. Funct. Plant Biol. 29, 195-200.
    • (2002) Funct. Plant Biol. , vol.29 , pp. 195-200
    • Ohkawa, H.1    Sonoda, M.2    Hagino, N.3    Shibata, M.4    Pakrasi, H.B.5    Ogawa, T.6
  • 33
    • 34249692500 scopus 로고    scopus 로고
    • Large-scale analysis of chlorophyll fluorescence kinetics in Synechocystis sp. PCC 6803: Identification of the factors involved in the modulation of photosystem stoichiometry
    • Ozaki, H., Ikeuchi, M., Ogawa, T., Fukuzawa, H., and, Sonoike, K., (2007) Large-scale analysis of chlorophyll fluorescence kinetics in Synechocystis sp. PCC 6803: identification of the factors involved in the modulation of photosystem stoichiometry. Plant Cell Physiol. 48, 451-458.
    • (2007) Plant Cell Physiol. , vol.48 , pp. 451-458
    • Ozaki, H.1    Ikeuchi, M.2    Ogawa, T.3    Fukuzawa, H.4    Sonoike, K.5
  • 34
    • 73249123281 scopus 로고    scopus 로고
    • Efficient operation of NAD(P)H dehydrogenase requires the supercomplex formation with photosystem i via minor LHCI in Arabidopsis
    • Peng, L., Fukao, Y., Fujiwara, M., Takami, T., and, Shikanai, T., (2009) Efficient operation of NAD(P)H dehydrogenase requires the supercomplex formation with photosystem I via minor LHCI in Arabidopsis. Plant Cell, 21, 3623-3640.
    • (2009) Plant Cell , vol.21 , pp. 3623-3640
    • Peng, L.1    Fukao, Y.2    Fujiwara, M.3    Takami, T.4    Shikanai, T.5
  • 35
    • 77954436604 scopus 로고    scopus 로고
    • Chloroplast stromal proteins, CRR6 and CRR7, are required for assembly of the NAD(P)H dehydrogenase subcomplex A in Arabidopsis
    • Peng, L., Cai, W., and, Shikanai, T., (2010) Chloroplast stromal proteins, CRR6 and CRR7, are required for assembly of the NAD(P)H dehydrogenase subcomplex A in Arabidopsis. Plant J. 63, 203-211.
    • (2010) Plant J. , vol.63 , pp. 203-211
    • Peng, L.1    Cai, W.2    Shikanai, T.3
  • 36
    • 79958082745 scopus 로고    scopus 로고
    • Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase complex
    • Peng, L., Yamamoto, H., and, Shikanai, T., (2011a) Structure and biogenesis of the chloroplast NAD(P)H dehydrogenase complex. Biochim. Biophys. Acta, 1807, 945-953.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 945-953
    • Peng, L.1    Yamamoto, H.2    Shikanai, T.3
  • 37
    • 79955492385 scopus 로고    scopus 로고
    • A chaperonin subunit with unique structures is essential for folding of a specific substrate
    • Peng, L., Fukao, Y., Myouga, F., Motohashi, R., Shinozaki, K., and, Shikanai, T., (2011b) A chaperonin subunit with unique structures is essential for folding of a specific substrate. PLoS Biol. 9, e1001040.
    • (2011) PLoS Biol. , vol.9
    • Peng, L.1    Fukao, Y.2    Myouga, F.3    Motohashi, R.4    Shinozaki, K.5    Shikanai, T.6
  • 38
    • 84857730895 scopus 로고    scopus 로고
    • Multistep assembly of chloroplast NADH dehydrogenase-like subcomplex A requires several nucleus-encoded proteins, including CRR41 and CRR42, in Arabidopsis
    • Peng, L., Fukao, Y., Fujiwara, M., and, Shikanai, T., (2012) Multistep assembly of chloroplast NADH dehydrogenase-like subcomplex A requires several nucleus-encoded proteins, including CRR41 and CRR42, in Arabidopsis. Plant Cell, 24, 202-214.
    • (2012) Plant Cell , vol.24 , pp. 202-214
    • Peng, L.1    Fukao, Y.2    Fujiwara, M.3    Shikanai, T.4
  • 39
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex i from Thermus thermophilus
    • Sazanov, L.A., and, Hinchliffe, P., (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science, 311, 1430-1436.
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 41
    • 0032483030 scopus 로고    scopus 로고
    • Directed disruption of the tobacco ndhB gene impairs cyclic electron flow around photosystem i
    • Shikanai, T., Endo, T., Hashimoto, T., Yamada, Y., Asada, K., and, Yokota, A., (1998) Directed disruption of the tobacco ndhB gene impairs cyclic electron flow around photosystem I. Proc. Natl Acad. Sci. USA, 95, 9705-9709.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9705-9709
    • Shikanai, T.1    Endo, T.2    Hashimoto, T.3    Yamada, Y.4    Asada, K.5    Yokota, A.6
  • 44
    • 71249105141 scopus 로고    scopus 로고
    • Towards characterization of the chloroplast NAD(P)H dehydrogenase complex
    • Suorsa, M., Sirpiö, S., and, Aro, E.M., (2009) Towards characterization of the chloroplast NAD(P)H dehydrogenase complex. Mol. Plant, 2, 1127-1140.
    • (2009) Mol. Plant , vol.2 , pp. 1127-1140
    • Suorsa, M.1    Sirpiö, S.2    Aro, E.M.3
  • 45
    • 58349120608 scopus 로고    scopus 로고
    • Three novel subunits of Arabidopsis chloroplastic NAD(P)H dehydrogenase identified by bioinformatic and reverse genetic approaches
    • Takabayashi, A., Ishikawa, N., Obayashi, T., Ishida, S., Obokata, J., Endo, T., and, Sato, F., (2009) Three novel subunits of Arabidopsis chloroplastic NAD(P)H dehydrogenase identified by bioinformatic and reverse genetic approaches. Plant J. 57, 207-219.
    • (2009) Plant J. , vol.57 , pp. 207-219
    • Takabayashi, A.1    Ishikawa, N.2    Obayashi, T.3    Ishida, S.4    Obokata, J.5    Endo, T.6    Sato, F.7
  • 46
    • 33745668217 scopus 로고    scopus 로고
    • Chloroplastic NAD(P)H dehydrogenase in tobacco leave functions in alleviation of oxidative damage caused by temperature stress
    • Wang, P., Duan, W., Takabayashi, A., Endo, T., Shikanai, T., Ye, J.Y., and, Mi, H., (2006) Chloroplastic NAD(P)H dehydrogenase in tobacco leave 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.7
  • 47
    • 0020595035 scopus 로고
    • Stable integration of foreign DNA into the chromosome of the cyanobacterium Synechococcus R2
    • Williams, J.G.K., and, Szalay, A.A., (1983) Stable integration of foreign DNA into the chromosome of the cyanobacterium Synechococcus R2. Gene, 24, 37-51.
    • (1983) Gene , vol.24 , pp. 37-51
    • Williams, J.G.K.1    Szalay, A.A.2
  • 48
  • 49
    • 79957773110 scopus 로고    scopus 로고
    • An Src homology 3 domain-like fold protein forms a ferredoxin-binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis
    • Yamamoto, H., Peng, L., Fukao, Y., and, Shikanai, T., (2011) An Src homology 3 domain-like fold protein forms a ferredoxin-binding site for the chloroplast NADH dehydrogenase-like complex in Arabidopsis. Plant Cell, 23, 1480-1493.
    • (2011) Plant Cell , vol.23 , pp. 1480-1493
    • Yamamoto, H.1    Peng, L.2    Fukao, Y.3    Shikanai, T.4
  • 50
    • 0035543363 scopus 로고    scopus 로고
    • The signaling mechanism of Arabidopsis CRY1 involves direct interaction with COP1
    • Yang, H.Q., Tang, R.H., and, Cashmore, A.R., (2001) The signaling mechanism of Arabidopsis CRY1 involves direct interaction with COP1. Plant Cell, 13, 2573-2587.
    • (2001) Plant Cell , vol.13 , pp. 2573-2587
    • Yang, H.Q.1    Tang, R.H.2    Cashmore, A.R.3
  • 51
    • 18844436373 scopus 로고    scopus 로고
    • Expression and functional roles of the two distinct NDH-1 complexes and the carbon acquisition complex NdhD3/NdhF3/CupA/Sll1735 in Synechocystis sp. PCC 6803
    • Zhang, P., Battchikova, N., Jansen, T., Appel, J., Ogawa, T., and, Aro, E.M., (2004) Expression and functional roles of the two distinct NDH-1 complexes and the carbon acquisition complex NdhD3/NdhF3/CupA/Sll1735 in Synechocystis sp. PCC 6803. Plant Cell, 16, 3326-3340.
    • (2004) Plant Cell , vol.16 , pp. 3326-3340
    • Zhang, P.1    Battchikova, N.2    Jansen, T.3    Appel, J.4    Ogawa, T.5    Aro, E.M.6
  • 52
    • 65449190158 scopus 로고    scopus 로고
    • Flavodiiron proteins in oxygenic photosynthetic organisms: Photoprotection of photosystem II by Flv2 and Flv4 in Synechocystis sp. PCC 6803
    • Zhang, P., Allahverdiyeva, Y., Eisenhut, M., and, Aro, E.M., (2009) Flavodiiron proteins in oxygenic photosynthetic organisms: photoprotection of photosystem II by Flv2 and Flv4 in Synechocystis sp. PCC 6803. PLoS One, 4, e5331.
    • (2009) PLoS One , vol.4
    • Zhang, P.1    Allahverdiyeva, Y.2    Eisenhut, M.3    Aro, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.