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Volumn 9, Issue 8, 2014, Pages

The 5 kDa protein NdhP is essential for stable NDH-1L assembly in Thermosynechococcus elongatus

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; NAD(P)H PLASTOQUINONE OXIDOREDUCTASE; OXIDOREDUCTASE; PROTEIN SUBUNIT;

EID: 84905910215     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0103584     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • DOI 10.1016/S0014-5793(00)01867-6, PII S0014579300018676
    • Friedrich T, 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. (Pubitemid 30625247)
    • (2000) FEBS Letters , vol.479 , Issue.1-2 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 2
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:Quinone oxidoreductase (complex I)
    • Brandt U (2006) Energy converting NADH:quinone oxidoreductase (complex I). Annu Rev Biochem 75: 69-92.
    • (2006) Annu Rev Biochem , vol.75 , pp. 69-92
    • Brandt, U.1
  • 3
    • 73849114263 scopus 로고    scopus 로고
    • Towards the molecular mechanism of respiratory complex I
    • Hirst J (2010) Towards the molecular mechanism of respiratory complex I. Biochem J 425: 327-339.
    • (2010) Biochem J , vol.425 , pp. 327-339
    • Hirst, J.1
  • 5
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • DOI 10.1126/science.1123809
    • Sazanov LA, Hinchliffe P (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311: 1430-1436. (Pubitemid 43376691)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 7
    • 84883769323 scopus 로고    scopus 로고
    • Central role of cyclic electron transport around photosystem I in the regulation of photosynthesis
    • Shikanai T (2014) Central role of cyclic electron transport around photosystem I in the regulation of photosynthesis. Curr Opin Biotechnol 26C: 25-30.
    • (2014) Curr Opin Biotechnol , vol.26 C , pp. 25-30
    • Shikanai, T.1
  • 8
    • 84893874251 scopus 로고    scopus 로고
    • Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex
    • Kouril R, Strouhal O, Nosek L, Lenobel R, Chamrad I, et al. (2014) Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex. Plant J 77: 568-576.
    • (2014) Plant J , vol.77 , pp. 568-576
    • Kouril, R.1    Strouhal, O.2    Nosek, L.3    Lenobel, R.4    Chamrad, I.5
  • 9
    • 77954761012 scopus 로고    scopus 로고
    • Possibilities of subunit localization with fluorescent protein tags and electron microscopy examplified by a cyanobacterial NDH-1 study
    • Birungi M, Folea M, Battchikova N, Xu M, Mi H, et al. (2010) Possibilities of subunit localization with fluorescent protein tags and electron microscopy examplified by a cyanobacterial NDH-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
  • 10
    • 80052879596 scopus 로고    scopus 로고
    • Structure of the chloroplast NADH dehydrogenase-like complex: Nomenclature for nuclear-encoded subunits
    • Ifuku K, Endo T, Shikanai T, Aro EM (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
  • 11
    • 84880697838 scopus 로고    scopus 로고
    • Enzymatic characterization of an active NDH complex from Thermosynechococcus elongatus
    • Hu P, Lv J, Fu P, Hualing M (2013) Enzymatic characterization of an active NDH complex from Thermosynechococcus elongatus. FEBS Lett 587: 2340-2345.
    • (2013) FEBS Lett , vol.587 , pp. 2340-2345
    • Hu, P.1    Lv, J.2    Fu, P.3    Hualing, M.4
  • 12
    • 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, 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
  • 13
    • 34547805062 scopus 로고    scopus 로고
    • Cyanobacterial NADPH dehydrogenase complexes
    • DOI 10.1007/s11120-006-9128-y, Govindjee Special Issue: Part A, Celebrating Govindjee's 50 Years in Photosynthesis Research and his 75th Birthday
    • Ogawa T, Mi H (2007) Cyanobacterial NADPH dehydrogenase complexes. Photosynth Res 93: 69-77. (Pubitemid 47310278)
    • (2007) Photosynthesis Research , vol.93 , Issue.1-3 , pp. 69-77
    • Ogawa, T.1    Mi, H.2
  • 14
    • 79958120495 scopus 로고    scopus 로고
    • Cyanobacterial NDH-1 complexes: Novel insights and remaining puzzles
    • Battchikova N, Eisenhut M, Aro EM (2011) 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
  • 15
    • 78650144629 scopus 로고    scopus 로고
    • Distinct roles of multiple NDH-1 complexes in the cyanobacterial electron transport network as revealed by kinetic analysis of P700+ reduction in various Ndh-deficient mutants of Synechocystis sp. Strain PCC6803
    • Bernat G, Appel J, Ogawa T, Rogner M (2011) Distinct roles of multiple NDH-1 complexes in the cyanobacterial electron transport network as revealed by kinetic analysis of P700+ reduction in various Ndh-deficient mutants of Synechocystis sp. strain PCC6803. J Bacteriol 193: 292-295.
    • (2011) J Bacteriol , vol.193 , pp. 292-295
    • Bernat, G.1    Appel, J.2    Ogawa, T.3    Rogner, M.4
  • 16
    • 79951598800 scopus 로고    scopus 로고
    • NdhP and NdhQ: Two novel small subunits of the cyanobacterial NDH-1 complex
    • Nowaczyk MM, Wulfhorst H, Ryan CM, Souda P, Zhang H, et al. (2011) NdhP and NdhQ: two novel small subunits of the cyanobacterial NDH-1 complex. Biochemistry 50: 1121-1124.
    • (2011) Biochemistry , vol.50 , pp. 1121-1124
    • Nowaczyk, M.M.1    Wulfhorst, H.2    Ryan, C.M.3    Souda, P.4    Zhang, H.5
  • 17
    • 84886796320 scopus 로고    scopus 로고
    • The gene sml0013 of Synechocystis species strain PCC 6803 encodes for a novel subunit of the NAD(P)H oxidoreductase or complex I that is ubiquitously distributed among Cyanobacteria
    • Schwarz D, Schubert H, Georg J, Hess WR, Hagemann M (2013) The gene sml0013 of Synechocystis species strain PCC 6803 encodes for a novel subunit of the NAD(P)H oxidoreductase or complex I that is ubiquitously distributed among Cyanobacteria. Plant Physiol 163: 1191-1202.
    • (2013) Plant Physiol , vol.163 , pp. 1191-1202
    • Schwarz, D.1    Schubert, H.2    Georg, J.3    Hess, W.R.4    Hagemann, M.5
  • 18
    • 47249158473 scopus 로고    scopus 로고
    • NDF6: A thylakoid protein specific to terrestrial plants is essential for activity of chloroplastic NAD(P)H dehydrogenase in Arabidopsis
    • DOI 10.1093/pcp/pcn083
    • Ishikawa N, Takabayashi A, Ishida S, Hano Y, Endo T, et al. (2008) NDF6: a thylakoid protein specific to terrestrial plants is essential for activity of chloroplastic NAD(P)H dehydrogenase in Arabidopsis. Plant Cell Physiol 49: 1066-1073. (Pubitemid 351989694)
    • (2008) Plant and Cell Physiology , vol.49 , Issue.7 , pp. 1066-1073
    • Ishikawa, N.1    Takabayashi, A.2    Ishida, S.3    Hano, Y.4    Endo, T.5    Sato, F.6
  • 19
    • 1542320967 scopus 로고    scopus 로고
    • Improved Genetic Transformation of the Thermophilic Cyanobacterium, Thermosynechococcus elongatus BP-1
    • DOI 10.1093/pcp/pch015
    • Iwai M, Katoh H, Katayama M, Ikeuchi M (2004) Improved genetic transformation of the thermophilic cyanobacterium, Thermosynechococcus elongatus BP-1. Plant Cell Physiol 45: 171-175. (Pubitemid 38318822)
    • (2004) Plant and Cell Physiology , vol.45 , Issue.2 , pp. 171-175
    • Iwai, M.1    Katoh, H.2    Katayama, M.3    Ikeuchi, M.4
  • 20
    • 30544433196 scopus 로고    scopus 로고
    • Engineering and characterization of a superfolder green fluorescent protein
    • DOI 10.1038/nbt1172, PII NBT1172
    • Pedelacq JD, Cabantous S, Tran T, Terwilliger TC, Waldo GS (2006) Engineering and characterization of a superfolder green fluorescent protein. Nat Biotechnol 24: 79-88. (Pubitemid 43083170)
    • (2006) Nature Biotechnology , vol.24 , Issue.1 , pp. 79-88
    • Pedelacq, J.-D.1    Cabantous, S.2    Tran, T.3    Terwilliger, T.C.4    Waldo, G.S.5
  • 21
    • 0018409915 scopus 로고
    • Generic assignments, strain histories and properties of pure cultures of cyanobacteria
    • Rippka R, Deruelles J, Waterbury JB, Herdman M, Stanier RY (1979) Generic assignments, strain histories and properties of pure cultures of cyanobacteria. Journal of General microbiology 111: 1-61. (Pubitemid 9142236)
    • (1979) Journal of General Microbiology , vol.111 , Issue.1 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3
  • 22
    • 0034617209 scopus 로고    scopus 로고
    • Towards structural determination of the water-splitting enzyme: Purification, crystallization, and preliminary crystallographic studies of photosystem II from a thermophilic cyanobacterium
    • DOI 10.1074/jbc.M001321200
    • Kuhl H, Kruip J, Seidler A, Krieger-Liszkay A, Bunker M, et al. (2000) Towards structural determination of the water-splitting enzyme. Purification, crystallization, and preliminary crystallographic studies of photosystem II from a thermophilic cyanobacterium. J Biol Chem 275: 20652-20659. (Pubitemid 30457652)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.27 , pp. 20652-20659
    • Kuhl, H.1    Kruip, J.2    Seidler, A.3    Krieger-Liszkay, A.4    Bunker, M.5    Bald, D.6    Scheidig, A.J.7    Rogner, M.8
  • 23
    • 80054716347 scopus 로고    scopus 로고
    • Identification of 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 EM, et al. (2011) Identification of 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
  • 24
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H, Beier H, Gross HJ (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8: 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 25
    • 84862178390 scopus 로고    scopus 로고
    • Deletion of psbJ leads to accumulation of Psb27-Psb28 photosystem II complexes in Thermosynechococcus elongatus
    • Nowaczyk MM, Krause K, Mieseler M, Sczibilanski A, Ikeuchi M, et al. (2012) Deletion of psbJ leads to accumulation of Psb27-Psb28 photosystem II complexes in Thermosynechococcus elongatus. Biochim Biophys Acta 1817: 1339-1345.
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 1339-1345
    • Nowaczyk, M.M.1    Krause, K.2    Mieseler, M.3    Sczibilanski, A.4    Ikeuchi, M.5
  • 26
    • 0032127262 scopus 로고    scopus 로고
    • Automation of specimen selection and data acquisition for protein electron crystallography
    • DOI 10.1016/S0304-3991(98)00022-9, PII S0304399198000229
    • Oostergetel GT, Keegstra W, Brisson A (1998) Automation of specimen selection and data acquisition for protein electron crystallography. Ultramicroscopy 74: 47-59. (Pubitemid 28352516)
    • (1998) Ultramicroscopy , vol.74 , Issue.1-2 , pp. 47-59
    • Oostergetel, G.T.1    Keegstra, W.2    Brisson, A.3
  • 27
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, et al. (2007) EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157: 38-46. (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 28
    • 0033486045 scopus 로고    scopus 로고
    • Supramolecular organization of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes
    • Boekema EJ, Van Roon H, Van Breemen JF, Dekker JP (1999) Supramolecular organization of photosystem II and its light-harvesting antenna in partially solubilized photosystem II membranes. Eur J Biochem 266: 444-452.
    • (1999) Eur J Biochem , vol.266 , pp. 444-452
    • Boekema, E.J.1    Van Roon, H.2    Van Breemen, J.F.3    Dekker, J.P.4
  • 30
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • DOI 10.1093/nar/25.24.4876
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4882. (Pubitemid 28022245)
    • (1997) Nucleic Acids Research , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 31
  • 32
    • 69249212321 scopus 로고    scopus 로고
    • Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: A historical perspective
    • Guex N, Peitsch MC, Schwede T (2009) Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: a historical perspective. Electrophoresis 30 Suppl 1: S162-173.
    • (2009) Electrophoresis , vol.30 , Issue.SUPPL. 1
    • Guex, N.1    Peitsch, M.C.2    Schwede, T.3
  • 35
    • 38549111794 scopus 로고    scopus 로고
    • Expression and use of superfolder green fluorescent protein at high temperatures in vivo: A tool to study extreme thermophile biology
    • DOI 10.1111/j.1462-2920.2007.01482.x
    • Cava F, de Pedro MA, Blas-Galindo E, Waldo GS, Westblade LF, et al. (2008) Expression and use of superfolder green fluorescent protein at high temperatures in vivo: a tool to study extreme thermophile biology. Environ Microbiol 10: 605-613. (Pubitemid 351160902)
    • (2008) Environmental Microbiology , vol.10 , Issue.3 , pp. 605-613
    • Cava, F.1    De Pedro, M.A.2    Blas-Galindo, E.3    Waldo, G.S.4    Westblade, L.F.5    Berenguer, J.6
  • 36
    • 33750514379 scopus 로고    scopus 로고
    • Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy
    • DOI 10.1016/j.bbabio.2006.05.042, PII S0005272806001769
    • Arteni AA, Zhang P, Battchikova N, Ogawa T, Aro EM, et al. (2006) Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy. Biochim Biophys Acta 1757: 1469-1475. (Pubitemid 44666665)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.11 , pp. 1469-1475
    • Arteni, A.A.1    Zhang, P.2    Battchikova, N.3    Ogawa, T.4    Aro, E.-M.5    Boekema, E.J.6
  • 37
    • 84903825375 scopus 로고    scopus 로고
    • NdhP Is an Exclusive Subunit of Large Complex of NADPH Dehydrogenase Essential to Stabilize the Complex in Synechocystis sp. Strain PCC 6803
    • Zhang J, Gao F, Zhao J, Ogawa T, Wang Q, et al. (2014) NdhP Is an Exclusive Subunit of Large Complex of NADPH Dehydrogenase Essential to Stabilize the Complex 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
  • 38
    • 77953136730 scopus 로고    scopus 로고
    • Small single transmembrane domain (STMD) proteins organize the hydrophobic subunits of large membrane protein complexes
    • Zickermann V, Angerer H, Ding MG, Nubel E, Brandt U (2010) Small single transmembrane domain (STMD) proteins organize the hydrophobic subunits of large membrane protein complexes. FEBS Lett 584: 2516-2525.
    • (2010) FEBS Lett , vol.584 , pp. 2516-2525
    • Zickermann, V.1    Angerer, H.2    Ding, M.G.3    Nubel, E.4    Brandt, U.5


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