메뉴 건너뛰기




Volumn 168, Issue 2, 2015, Pages 443-451

Subunit Q is required to stabilize the large complex of NADPH dehydrogenase in synechocystis sp. Strain PCC 68031

Author keywords

[No Author keywords available]

Indexed keywords

CYANOBACTERIA; SYNECHOCYSTIS SP.; THERMOSYNECHOCOCCUS ELONGATUS;

EID: 84933052291     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.15.00503     Document Type: Article
Times cited : (29)

References (62)
  • 1
    • 84984087585 scopus 로고
    • Simple conditions for growth of unicellular blue-greenalgae on plates
    • Allen MM (1968) Simple conditions for growth of unicellular blue-greenalgae on plates. J Phycol 4: 1–4
    • (1968) J Phycol , vol.4 , pp. 1-4
    • Allen, M.M.1
  • 2
    • 84888419425 scopus 로고    scopus 로고
    • The PHOTOSYNTHESIS AFFECTEDMUTANT68-LIKE protein evolved from a PSII assembly factor to mediateassembly of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis
    • Armbruster U, Rühle T, Kreller R, Strotbek C, Zühlke J, Tadini L, Blunder T, Hertle AP, Qi Y, Rengstl B, et al (2013) The PHOTOSYNTHESIS AFFECTEDMUTANT68-LIKE protein evolved from a PSII assembly factor to mediateassembly of the chloroplast NAD(P)H dehydrogenase complex in Arabidopsis. Plant Cell 25: 3926–3943
    • (2013) Plant Cell , vol.25 , pp. 3926-3943
    • Armbruster, U.1    Rühle, T.2    Kreller, R.3    Strotbek, C.4    Zühlke, J.5    Tadini, L.6    Blunder, T.7    Hertle, A.P.8    Qi, Y.9    Rengstl, B.10
  • 3
    • 33750514379 scopus 로고    scopus 로고
    • Structural characterization of NDH-1 complexes of Thermosynechococcuselongatus by single particle electron microscopy
    • Arteni AA, Zhang P, Battchikova N, Ogawa T, Aro EM, Boekema EJ (2006) Structural characterization of NDH-1 complexes of Thermosynechococcuselongatus by single particle electron microscopy. BiochimBiophys Acta 1757: 1469–1475
    • (2006) Biochimbiophys 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
  • 4
    • 34547747897 scopus 로고    scopus 로고
    • Cyanobacterial NDH-1 complexes: Multiplicityin function and subunit composition
    • Battchikova N, Aro EM (2007) Cyanobacterial NDH-1 complexes: multiplicityin 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
    • 79958120495 scopus 로고    scopus 로고
    • Cyanobacterial NDH-1 complexes:Novel insights and remaining puzzles
    • Battchikova N, Eisenhut M, Aro EM (2011b) Cyanobacterial NDH-1 complexes:novel insights and remaining puzzles. Biochim Biophys Acta 1807: 935–944
    • (2011) Biochim Biophys Acta , pp. 935-944
    • Battchikova, N.1    Eisenhut, M.2    Aro, E.M.3
  • 6
    • 80054716347 scopus 로고    scopus 로고
    • Identificationof novel Ssl0352 protein (NdhS), essential for efficient operationof cyclic electron transport around photosystem I
    • NADPH:plastoquinoneoxidoreductase (NDH-1) complexes of Synechocystis sp. PCC6803
    • Battchikova N, Wei L, Du L, Bersanini L, Aro EM, Ma W (2011a) Identificationof novel Ssl0352 protein (NdhS), essential for efficient operationof cyclic electron transport around photosystem I, in NADPH:plastoquinoneoxidoreductase (NDH-1) complexes of Synechocystis sp. PCC6803. 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
  • 7
    • 13244281728 scopus 로고    scopus 로고
    • Identificationof NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes ofSynechocystis sp. PCC 6803
    • Battchikova N, Zhang P, Rudd S, Ogawa T, Aro EM (2005) Identificationof NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes ofSynechocystis sp. PCC 6803. J Biol Chem 280: 2587–2595
    • (2005) J Biol Chem , vol.280 , pp. 2587-2595
    • Battchikova, N.1    Zhang, P.2    Rudd, S.3    Ogawa, T.4    Aro, E.M.5
  • 8
    • 78650144629 scopus 로고    scopus 로고
    • Distinct roles of multipleNDH-1 complexes in the cyanobacterial electron transport network asrevealed by kinetic analysis of P700+ reduction in various Ndh-deficientmutants of Synechocystis sp. Strain PCC6803
    • Bernát G, Appel J, Ogawa T, Rögner M (2011) Distinct roles of multipleNDH-1 complexes in the cyanobacterial electron transport network asrevealed by kinetic analysis of P700+ reduction in various Ndh-deficientmutants 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
  • 9
    • 77954761012 scopus 로고    scopus 로고
    • Possibilities of subunit localization with fluorescentprotein tags and electron microscopy examplified by a cyanobacterialNDH-1 study
    • Birungi M, Folea M, Battchikova N, Xu M, Mi H, Ogawa T, Aro EM, Boekema EJ (2010) Possibilities of subunit localization with fluorescentprotein tags and electron microscopy examplified by a cyanobacterialNDH-1 study. Biochim Biophys Acta 1797: 1681–1686
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1681-1686
    • Birungi, M.1    Folea, M.2    Battchikova, N.3    Xu, M.4    Mi, H.5    Ogawa, T.6    Aro, E.M.7    Boekema, E.J.8
  • 10
    • 0032481317 scopus 로고    scopus 로고
    • Identification of afunctional respiratory complex in chloroplasts through analysis of tobaccomutants containing disrupted plastid ndh genes
    • Burrows PA, Sazanov LA, Svab Z, Maliga P, Nixon PJ (1998) Identification of afunctional respiratory complex in chloroplasts through analysis of tobaccomutants 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
  • 11
    • 84883243697 scopus 로고    scopus 로고
    • Identification of acyanobacterial CRR6 protein, Slr1097, required for efficient assembly ofNDH-1 complexes in Synechocystis sp
    • Dai H, Zhang L, Zhang J, Mi H, Ogawa T, Ma W (2013) Identification of acyanobacterial CRR6 protein, Slr1097, required for efficient assembly ofNDH-1 complexes in Synechocystis sp. PCC 6803.Plant J 75: 858–866
    • (2013) PCC 6803.Plant J , vol.75 , pp. 858-866
    • Dai, H.1    Zhang, L.2    Zhang, J.3    Mi, H.4    Ogawa, T.5    Ma, W.6
  • 12
    • 0038347204 scopus 로고    scopus 로고
    • Effects of low CO2 on NAD(P)H dehydrogenase,a mediator of cyclic electron transport around photosystem I in the cyanobacteriumsynechocystis PCC6803
    • Deng Y, Ye J, Mi H (2003) Effects of low CO2 on NAD(P)H dehydrogenase,a mediator of cyclic electron transport around photosystem I in the cyanobacteriumsynechocystis PCC6803 Plant Cell Physiol 44: 534–540
    • (2003) Plant Cell Physiol , vol.44 , pp. 534-540
    • Deng, Y.1    Ye, J.2    Mi, H.3
  • 13
    • 45949114408 scopus 로고
    • The role of respiratory electron flow in thecontrol of excitation energy distribution in blue-green algae
    • Dominy PJ, Williams WP (1987) The role of respiratory electron flow in thecontrol of excitation energy distribution in blue-green algae. BiochimBiophys Acta 892: 264–274
    • (1987) Biochimbiophys Acta , vol.892 , pp. 264-274
    • Dominy, P.J.1    Williams, W.P.2
  • 14
    • 0032790755 scopus 로고    scopus 로고
    • The role of chloroplasticNAD(P)H dehydrogenase in photoprotection
    • Endo T, Shikanai T, Takabayashi A, Asada K, Sato F (1999) The role of chloroplasticNAD(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
  • 15
    • 84989675177 scopus 로고
    • State I–state II transitions in the thermophilicblue-green alga (Cyanobacterium) Synechococcus lividus
    • Fork DC, Satoh K (1983) State I–state II transitions in the thermophilicblue-green alga (cyanobacterium) Synechococcus lividus. PhotochemPhotobiol 37: 421–427
    • (1983) Photochemphotobiol , vol.37 , pp. 421-427
    • Fork, D.C.1    Satoh, K.2
  • 16
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaeaand eukarya and its module common with membrane-boundmultisubunit hydrogenases
    • Friedrich T, Scheide D (2000) The respiratory complex I of bacteria, archaeaand eukarya and its module common with membrane-boundmultisubunit hydrogenases. FEBS Lett 479: 1–5
    • (2000) FEBS Lett , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 17
    • 0029059910 scopus 로고
    • The proton-pumping respiratorycomplex I of bacteria and mitochondria and its homologue inchloroplasts
    • Friedrich T, Steinmüller K, Weiss H (1995) The proton-pumping respiratorycomplex I of bacteria and mitochondria and its homologue inchloroplasts. FEBS Lett 367: 107–111
    • (1995) FEBS Lett , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmüller, K.2    Weiss, H.3
  • 18
    • 0028606359 scopus 로고
    • The recovery of photosynthesis fromlow-temperature photoinhibition is accelerated by the unsaturation ofmembrane lipids: A mechanism of chilling tolerance
    • Gombos Z, Wada H, Murata N (1994) The recovery of photosynthesis fromlow-temperature photoinhibition is accelerated by the unsaturation ofmembrane lipids: a mechanism of chilling tolerance. Proc Natl Acad SciUSA 91: 8787–8791
    • (1994) Proc Natl Acad Sciusa , vol.91 , pp. 8787-8791
    • Gombos, Z.1    Wada, H.2    Murata, N.3
  • 19
    • 0345393082 scopus 로고    scopus 로고
    • A nucleusencodedfactor, CRR2, is essential for the expression of chloroplast ndhBin Arabidopsis
    • Hashimoto M, Endo T, Peltier G, Tasaka M, Shikanai T (2003) A nucleusencodedfactor, CRR2, is essential for the expression of chloroplast ndhBin 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
  • 21
    • 0344628670 scopus 로고    scopus 로고
    • Kinetic analyses of state transitionsof the cyanobacterium Synechococcus sp. PCC 7002 and its mutant strainsimpaired in electron transport
    • Huang C, Yuan X, Zhao J, Bryant DA (2003) Kinetic analyses of state transitionsof the cyanobacterium Synechococcus sp. PCC 7002 and its mutant strainsimpaired in electron transport. Biochim Biophys Acta 1607: 121–130
    • (2003) Biochim Biophys Acta , vol.1607 , pp. 121-130
    • Huang, C.1    Yuan, X.2    Zhao, J.3    Bryant, D.A.4
  • 22
    • 80052879596 scopus 로고    scopus 로고
    • Structure of the chloroplastNADH dehydrogenase-like complex: Nomenclature for nuclear-encodedsubunits
    • Ifuku K, Endo T, Shikanai T, Aro EM (2011) Structure of the chloroplastNADH dehydrogenase-like complex: nomenclature for nuclear-encodedsubunits. 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
  • 23
    • 47249158473 scopus 로고    scopus 로고
    • NDF6: A thylakoid protein specific to terrestrial plants is essential foractivity of chloroplastic NAD(P)H dehydrogenase in Arabidopsis
    • Ishikawa N, Takabayashi A, Ishida S, Hano Y, Endo T, Sato F (2008) NDF6: a thylakoid protein specific to terrestrial plants is essential foractivity of chloroplastic NAD(P)H dehydrogenase in Arabidopsis. PlantCell Physiol 49: 1066–1073
    • (2008) Plantcell Physiol , vol.49 , pp. 1066-1073
    • Ishikawa, N.1    Takabayashi, A.2    Ishida, S.3    Hano, Y.4    Endo, T.5    Sato, F.6
  • 24
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis ofthe genome of the unicellular cyanobacterium Synechocystis sp. StrainPCC6803. II. Sequence determination of the entire genome and assignmentof potential protein-coding regions
    • Kaneko T, Sato S, Kotani H, Tanaka A, Asamizu E, Nakamura Y, Miyajima N, Hirosawa M, Sugiura M, Sasamoto S, et al (1996) Sequence analysis ofthe genome of the unicellular cyanobacterium Synechocystis sp. strainPCC6803. II. Sequence determination of the entire genome and assignmentof 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    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6    Miyajima, N.7    Hirosawa, M.8    Sugiura, M.9    Sasamoto, S.10
  • 25
    • 0030829823 scopus 로고    scopus 로고
    • Analysis of thechloroplast protein complexes by blue-native polyacrylamide gel electrophoresis(BN-PAGE)
    • Kügler M, Jänsch L, Kruft V, Schmitz UK, Braun HP (1997) Analysis of thechloroplast 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
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly ofthe head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly ofthe head of bacteriophage T4 . Nature 227: 680–685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 85036210047 scopus 로고    scopus 로고
    • Effects of differentlight treatments on the natural transformation of Synechocystis sp. StrainPCC 6803
    • Long Z, Zhao J, Zhang J, Wei L, Wang Q, Ma W (2011) Effects of differentlight treatments on the natural transformation of Synechocystis sp. strainPCC 6803. Afr J Microbiol Res 5: 3603–3610
    • (2011) Afr J Microbiol Res , vol.5 , pp. 3603-3610
    • Long, Z.1    Zhao, J.2    Zhang, J.3    Wei, L.4    Wang, Q.5    Ma, W.6
  • 28
    • 63349097295 scopus 로고    scopus 로고
    • Identification, regulation and physiological functions of multipleNADPH dehydrogenase complexes in cyanobacteria
    • Ma W (2009) Identification, regulation and physiological functions of multipleNADPH dehydrogenase complexes in cyanobacteria. Front Biol China 4: 137–142
    • (2009) Front Biol China , vol.4 , pp. 137-142
    • Ma, W.1
  • 29
    • 24644456357 scopus 로고    scopus 로고
    • Expression and activity of type 1 NAD(P)H dehydrogenaseat different growth phases of the cyanobacterium, SynechocystisPCC 6803
    • Ma W, Mi H (2005) Expression and activity of type 1 NAD(P)H dehydrogenaseat different growth phases of the cyanobacterium, SynechocystisPCC 6803. Physiol Plant 125: 135–140
    • (2005) Physiol Plant , vol.125 , pp. 135-140
    • Ma, W.1    Mi, H.2
  • 30
    • 84925582509 scopus 로고    scopus 로고
    • Oxygenic photosynthesis-specific subunits of cyanobacterialNADPH dehydrogenases
    • Ma W, Ogawa T (2015) Oxygenic photosynthesis-specific subunits of cyanobacterialNADPH dehydrogenases. IUBMB Life 67: 3–8
    • (2015) . IUBMB Life , vol.67 , pp. 3-8
    • Ma, W.1    Ogawa, T.2
  • 31
    • 0038324426 scopus 로고    scopus 로고
    • Inorganic carbonlimitation and light control the expression of transcripts related to theCO2-concentrating mechanism in the cyanobacterium Synechocystis sp.Strain PCC6803
    • McGinn PJ, Price GD, Maleszka R, Badger MR (2003) Inorganic carbonlimitation and light control the expression of transcripts related to theCO2-concentrating mechanism in the cyanobacterium Synechocystis sp.strain PCC6803. Plant Physiol 132: 218–229
    • (2003) Plant Physiol , vol.132 , pp. 218-229
    • McGinn, P.J.1    Price, G.D.2    Maleszka, R.3    Badger, M.R.4
  • 32
    • 0028814979 scopus 로고
    • Thylakoid membrane-bound,NADPH-specific pyridine nucleotide dehydrogenase complex mediatescyclic electron transport in the cyanobacterium Synechocystis sp.PCC 6803
    • Mi H, Endo T, Ogawa T, Asada K (1995) Thylakoid membrane-bound,NADPH-specific pyridine nucleotide dehydrogenase complex mediatescyclic electron transport in the cyanobacterium Synechocystis sp.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
  • 33
    • 77957187653 scopus 로고
    • Electron donationfrom cyclic and respiratory flows to the photosynthetic intersystemchain is mediated by pyridine nucleotide dehydrogenase in the cyanobacteriumSynechocystis PCC 6803
    • Mi H, Endo T, Schreiber U, Ogawa T, Asada K (1992) Electron donationfrom cyclic and respiratory flows to the photosynthetic intersystemchain is mediated by pyridine nucleotide dehydrogenase in the cyanobacteriumSynechocystis 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
  • 34
    • 0000179113 scopus 로고
    • The state 2 transition in the cyanobacteriumSynechococcus 6301 can be driven by respiratory electron flow intothe plastoquinone pool
    • Mullineaux CW, Allen JF (1986) The state 2 transition in the cyanobacteriumSynechococcus 6301 can be driven by respiratory electron flow intothe plastoquinone pool. FEBS Lett 205: 155–160
    • (1986) FEBS Lett , vol.205 , pp. 155-160
    • Mullineaux, C.W.1    Allen, J.F.2
  • 35
    • 0000192749 scopus 로고
    • State 1-State 2 transitions in the cyanobacteriumSynechococcus 6301 are controlled by the redox state of electroncarriers between Photosystems I and II
    • Mullineaux CW, Allen JF (1990) State 1-State 2 transitions in the cyanobacteriumSynechococcus 6301 are controlled by the redox state of electroncarriers between Photosystems I and II. Photosynth Res 23: 297–311
    • (1990) Photosynth Res , vol.23 , pp. 297-311
    • Mullineaux, C.W.1    Allen, J.F.2
  • 37
    • 0025845648 scopus 로고
    • ) A gene homologous to the subunit-2 gene of NADH dehydrogenaseis essential to inorganic carbon transport of SynechocystisPCC6803
    • Ogawa T (1991) A gene homologous to the subunit-2 gene of NADH dehydrogenaseis essential to inorganic carbon transport of SynechocystisPCC6803. Proc Natl Acad Sci USA 88: 4275–4279
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4275-4279
    • Ogawa, T.1
  • 38
    • 84880242351 scopus 로고    scopus 로고
    • Disruption of the ndhF1gene affects Chl fluorescence through state transition in the CyanobacteriumSynechocystis sp. PCC 6803, resulting in apparent high efficiencyof photosynthesis
    • Ogawa T, Harada T, Ozaki H, Sonoike K (2013) Disruption of the ndhF1gene affects Chl fluorescence through state transition in the CyanobacteriumSynechocystis sp. PCC 6803, resulting in apparent high efficiencyof photosynthesis. Plant Cell Physiol 54: 1164–1171
    • (2013) Plant Cell Physiol , vol.54 , pp. 1164-1171
    • Ogawa, T.1    Harada, T.2    Ozaki, H.3    Sonoike, K.4
  • 39
    • 34547805062 scopus 로고    scopus 로고
    • Cyanobacterial NADPH dehydrogenase complexes
    • Ogawa T, Mi H (2007) Cyanobacterial NADPH dehydrogenase complexes. Photosynth Res 93: 69–77
    • (2007) Photosynth Res , vol.93 , pp. 69-77
    • Ogawa, T.1    Mi, H.2
  • 40
    • 0034644777 scopus 로고    scopus 로고
    • Two types of functionally distinctNAD(P)H dehydrogenases in Synechocystis sp. Strain PCC6803
    • Ohkawa H, Pakrasi HB, Ogawa T (2000) Two types of functionally distinctNAD(P)H dehydrogenases in Synechocystis sp. strain PCC6803. J BiolChem 275: 31630–31634
    • (2000) J Biolchem , vol.275 , pp. 31630-31634
    • Ohkawa, H.1    Pakrasi, H.B.2    Ogawa, T.3
  • 41
    • 0036326617 scopus 로고    scopus 로고
    • Functionally distinct NAD(P)H dehydrogenases and their membranelocalization in Synechocystis sp. PCC6803
    • Ohkawa H, Sonoda M, Hagino N, Shibata M, Pakrasi HB, Ogawa T (2002)Functionally distinct NAD(P)H dehydrogenases and their membranelocalization 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
  • 42
    • 0034900957 scopus 로고    scopus 로고
    • Localization of NAD(P)H dehydrogenase in the cyanobacterium Synechocystis sp. Strain PCC6803
    • Ohkawa H, Sonoda M, Shibata M, Ogawa T (2001) Localization of NAD(P)H dehydrogenase in the cyanobacterium Synechocystis sp. strain PCC6803. 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
  • 43
    • 84857730895 scopus 로고    scopus 로고
    • FujiwaraM, Shikanai T (2012)Multistep assembly of chloroplastNADH dehydrogenase-like subcomplex A requires several nucleus-encodedproteins, including CRR41 and CRR42, in Arabidopsis
    • Peng L, Fukao Y, FujiwaraM, Shikanai T (2012)Multistep assembly of chloroplastNADH dehydrogenase-like subcomplex A requires several nucleus-encodedproteins, including CRR41 and CRR42, in Arabidopsis. Plant Cell 24: 202–214
    • Plant Cell , vol.24 , pp. 202-214
    • Peng, L.1    Fukao, Y.2
  • 44
    • 73249123281 scopus 로고    scopus 로고
    • Efficient operationof NAD(P)H dehydrogenase requires supercomplex formation with photosystemI via minor LHCI in Arabidopsis
    • Peng L, Fukao Y, Fujiwara M, Takami T, Shikanai T (2009) Efficient operationof NAD(P)H dehydrogenase requires supercomplex formation with photosystemI 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
  • 45
    • 79955492385 scopus 로고    scopus 로고
    • A chaperonin subunit with unique structures is essential forfolding of a specific substrate
    • Peng L, Fukao Y, Myouga F, Motohashi R, Shinozaki K, Shikanai T(2011b) A chaperonin subunit with unique structures is essential forfolding 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
  • 46
    • 79958082745 scopus 로고    scopus 로고
    • Structure and biogenesis of the chloroplastNAD(P)H dehydrogenase complex
    • Peng L, Yamamoto H, Shikanai T (2011a) Structure and biogenesis of the chloroplastNAD(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
  • 47
    • 3142653751 scopus 로고    scopus 로고
    • Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803:Identification of two new ndh gene products with nuclear-encoded homologuesin the chloroplast Ndh complex
    • Prommeenate P, Lennon AM, Markert C, Hippler M, Nixon PJ (2004)Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803:identification of two new ndh gene products with nuclear-encoded homologuesin the chloroplast Ndh complex. J Biol Chem 279: 28165–28173
    • (2004) J Biol Chem , vol.279 , pp. 28165-28173
    • Prommeenate, P.1    Lennon, A.M.2    Markert, C.3    Hippler, M.4    Nixon, P.J.5
  • 48
    • 0028830806 scopus 로고
    • Quenching analysis of chlorophyllfluorescence by the saturation pulse method: Particular aspects relating to thestudy of eukaryotic algae and cyanobacteria
    • Schreiber U, Endo T, Mi H, Asada K (1995) Quenching analysis of chlorophyllfluorescence by the saturation pulse method: particular aspects relating to thestudy of eukaryotic algae and cyanobacteria. Plant Cell Physiol 36: 873–882
    • (1995) Plant Cell Physiol , vol.36 , pp. 873-882
    • Schreiber, U.1    Endo, T.2    Mi, H.3    Asada, K.4
  • 49
    • 34250847628 scopus 로고    scopus 로고
    • Cyclic electron transport around photosystem I: Geneticapproaches
    • Shikanai T (2007) Cyclic electron transport around photosystem I: geneticapproaches. Annu Rev Plant Biol 58: 199–217
    • (2007) . Annurev Plant Biol , vol.58 , pp. 199-217
    • Shikanai, T.1
  • 50
    • 0032483030 scopus 로고    scopus 로고
    • Directed disruption of the tobacco ndhB gene impairs cyclic electronflow around photosystem I
    • Shikanai T, Endo T, Hashimoto T, Yamada Y, Asada K, Yokota A (1998) Directed disruption of the tobacco ndhB gene impairs cyclic electronflow 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
  • 52
    • 71249105141 scopus 로고    scopus 로고
    • Towards characterization of the chloroplastNAD(P)H dehydrogenase complex
    • Suorsa M, Sirpiö S, Aro EM (2009) Towards characterization of the chloroplastNAD(P)H dehydrogenase complex. Mol Plant 2: 1127–1140
    • (2009) Mol Plant , vol.2 , pp. 1127-1140
    • Suorsa, M.1    Sirpiö, S.2    Em, A.3
  • 53
    • 33745668217 scopus 로고    scopus 로고
    • Chloroplastic NAD(P)H dehydrogenase in tobacco leaves functions inalleviation of oxidative damage caused by temperature stress
    • Wang P, Duan W, Takabayashi A, Endo T, Shikanai T, Ye JY, Mi H (2006)Chloroplastic NAD(P)H dehydrogenase in tobacco leaves functions inalleviation of oxidative damage caused by temperature stress. PlantPhysiol 141: 465–474
    • (2006) Plantphysiol , 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
  • 54
    • 0020595035 scopus 로고
    • Stable integration of foreign DNA into thechromosome of the cyanobacterium Synechococcus
    • Williams JGK, Szalay AA (1983) Stable integration of foreign DNA into thechromosome of the cyanobacterium Synechococcus R2 Gene 24: 37–51
    • (1983) R2 Gene , vol.24 , pp. 37-51
    • Williams, J.1    Szalay, A.A.2
  • 55
    • 84905910215 scopus 로고    scopus 로고
    • The 5 kDa protein NdhP is essential for stable NDH-1L assemblyin Thermosynechococcus elongatus
    • Wulfhorst H, Franken LE, Wessinghage T, Boekema EJ, Nowaczyk MM(2014) The 5 kDa protein NdhP is essential for stable NDH-1L assemblyin Thermosynechococcus elongatus. PLoS ONE 9: e103584
    • (2014) Plos ONE , vol.9
    • Wulfhorst, H.1    Franken, L.E.2    Wessinghage, T.3    Boekema, E.J.4    Nowaczyk, M.M.5
  • 56
    • 48849109157 scopus 로고    scopus 로고
    • Identification and localization of theCupB protein involved in constitutive CO2 uptake in the cyanobacterium,Synechocystis sp. Strain PCC 6803
    • Xu M, Ogawa T, Pakrasi HB, Mi H (2008) Identification and localization of theCupB protein involved in constitutive CO2 uptake in the cyanobacterium,Synechocystis sp. strain PCC 6803. Plant Cell Physiol 49: 994–997
    • (2008) Plant Cell Physiol , vol.49 , pp. 994-997
    • Xu, M.1    Ogawa, T.2    Pakrasi, H.B.3    Mi, H.4
  • 57
    • 77953606649 scopus 로고    scopus 로고
    • Three PsbQ-like proteins are required for the function ofthe chloroplast NAD(P)H dehydrogenase complex in Arabidopsis
    • Yabuta S, Ifuku K, Takabayashi A, Ishihara S, Ido K, Ishikawa N, Endo T, Sato F (2010) Three PsbQ-like proteins are required for the function ofthe chloroplast NAD(P)H dehydrogenase complex in Arabidopsis. PlantCell Physiol 51: 866–876
    • (2010) Plantcell Physiol , vol.51 , pp. 866-876
    • Yabuta, S.1    Ifuku, K.2    Takabayashi, A.3    Ishihara, S.4    Ido, K.5    Ishikawa, N.6    Endo, T.7    Sato, F.8
  • 58
    • 79957773110 scopus 로고    scopus 로고
    • An Src Homology 3Domain-Like fold protein forms a ferredoxin binding site for the chloroplastNADH dehydrogenase-like complex in Arabidopsis
    • Yamamoto H, Peng L, Fukao Y, Shikanai T (2011) An Src Homology 3Domain-Like fold protein forms a ferredoxin binding site for the chloroplastNADH 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
  • 59
    • 84903825375 scopus 로고    scopus 로고
    • NdhP is an exclusivesubunit of large complex of NADPH dehydrogenase essential to stabilize thecomplex in Synechocystis sp. Strain PCC 6803
    • Zhang J, Gao F, Zhao J, Ogawa T, Wang Q, Ma W (2014) NdhP is an exclusivesubunit of large complex of NADPH dehydrogenase essential to stabilize thecomplex in Synechocystis sp. strain PCC 6803. J Biol Chem 289: 18770–18781
    • (2014) J Biol Chem , vol.289 , pp. 18770-18781
    • Zhang, J.1    Gao, F.2    Zhao, J.3    Ogawa, T.4    Wang, Q.5    Ma, W.6
  • 60
    • 18844436373 scopus 로고    scopus 로고
    • Expression and functional roles of the two distinct NDH-1 complexesand the carbon acquisition complex NdhD3/NdhF3/CupA/Sll1735 inSynechocystis sp PCC 6803
    • Zhang P, Battchikova N, Jansen T, Appel J, Ogawa T, Aro EM (2004) Expression and functional roles of the two distinct NDH-1 complexesand the carbon acquisition complex NdhD3/NdhF3/CupA/Sll1735 inSynechocystis 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
  • 62
    • 84907586739 scopus 로고    scopus 로고
    • NdhO, a subunit ofNADPH dehydrogenase, destabilizes medium size complex of the enzymein Synechocystis sp. Strain PCC 6803
    • Zhao J, Gao F, Zhang J, Ogawa T, Ma W (2014) NdhO, a subunit ofNADPH dehydrogenase, destabilizes medium size complex of the enzymein Synechocystis sp. strain PCC 6803. J Biol Chem 289: 26669–26676
    • (2014) J Biol Chem , vol.289 , pp. 26669-26676
    • Zhao, J.1    Gao, F.2    Zhang, J.3    Ogawa, T.4    Ma, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.