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Volumn 1817, Issue 2, 2012, Pages 336-352

Cross-species investigation of the functions of the Rhodobacter PufX polypeptide and the composition of the RC-LH1 core complex

Author keywords

LH1 antenna; Light harvesting; Photosynthesis; PufX; Reaction centre; Rhodobacter sphaeroides

Indexed keywords

BACTERIAL PROTEIN; PUFX PROTEIN; REACTION CENTER LH1 PROTEIN; UNCLASSIFIED DRUG;

EID: 84655163769     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2011.10.009     Document Type: Article
Times cited : (28)

References (75)
  • 3
    • 0346874216 scopus 로고    scopus 로고
    • Crystal Structure of the RC-LH1 Core Complex from Rhodopseudomonas palustris
    • DOI 10.1126/science.1088892
    • A.W. Roszak, T.D. Howard, J. Southall, A.T. Gardiner, C.J. Law, N.W. Isaacs, and R.J. Cogdell Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris Science 302 2003 1969 1972 (Pubitemid 37523505)
    • (2003) Science , vol.302 , Issue.5652 , pp. 1969-1972
    • Roszak, A.W.1    Howard, T.D.2    Southall, J.3    Gardiner, A.T.4    Law, C.J.5    Isaacs, N.W.6    Cogdell, R.J.7
  • 6
    • 20444382012 scopus 로고    scopus 로고
    • Watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy
    • DOI 10.1016/j.bbamem.2005.04.005, PII S0005273605001033
    • S. Scheuring, D. Levy, and J.L. Rigaud Watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy Biochim. Biophys. Acta 1712 2005 109 127 (Pubitemid 40799298)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1712 , Issue.2 , pp. 109-127
    • Scheuring, S.1    Levy, D.2    Rigaud, J.-L.3
  • 7
    • 33845698300 scopus 로고    scopus 로고
    • The architecture and function of the light-harvesting apparatus of purple bacteria: From single molecules to in vivo membranes
    • DOI 10.1017/S0033583506004434, PII S0033583506004434
    • R.J. Cogdell, A. Gall, and J. Kohler The architecture and function of the light-harvesting apparatus of purple bacteria: from single molecules to in vivo membranes Q. Rev. Biophys. 39 2006 227 324 (Pubitemid 44963429)
    • (2006) Quarterly Reviews of Biophysics , vol.39 , Issue.3 , pp. 227-324
    • Cogdell, R.J.1    Gall, A.2    Kohler, J.3
  • 8
    • 33748578027 scopus 로고    scopus 로고
    • AFM studies of the supramolecular assembly of bacterial photosynthetic core-complexes
    • DOI 10.1016/j.cbpa.2006.08.007, PII S1367593106001141, Analytical Techniques/Mechanisms
    • S. Scheuring AFM studies of the supramolecular assembly of bacterial photosynthetic core-complexes Curr. Opin. Chem. Biol. 10 2006 387 393 (Pubitemid 44375061)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 387-393
    • Scheuring, S.1
  • 10
    • 77956262050 scopus 로고    scopus 로고
    • Bacterial photosynthesis
    • American Society for Photobiology
    • M.R. Jones Bacterial photosynthesis Photobiological Sciences Online 2009 American Society for Photobiology
    • (2009) Photobiological Sciences Online
    • Jones, M.R.1
  • 12
    • 0030585121 scopus 로고    scopus 로고
    • The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum
    • J. Koepke, X. Hu, C. Muenke, K. Schulten, and H. Michel The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum Structure 4 1996 581 597 (Pubitemid 126657551)
    • (1996) Structure , vol.4 , Issue.5 , pp. 581-597
    • Koepke, J.1    Hu, X.2    Muenke, C.3    Schulten, K.4    Michel, H.5
  • 13
    • 0033081638 scopus 로고    scopus 로고
    • Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides
    • DOI 10.1093/emboj/18.3.534
    • C. Jungas, J.L. Ranck, J.L. Rigaud, P. Joliot, and A. Vermeglio Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides EMBO J. 18 1999 534 542 (Pubitemid 29057238)
    • (1999) EMBO Journal , vol.18 , Issue.3 , pp. 534-542
    • Jungas, C.1    Ranck, J.-L.2    Rigaud, J.-L.3    Joliot, P.4    Vermeglio, A.5
  • 14
    • 1842510034 scopus 로고    scopus 로고
    • Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: The role of PufX
    • DOI 10.1038/sj.emboj.7600092
    • C.A. Siebert, P. Qian, D. Fotiadis, A. Engel, C.N. Hunter, and P.A. Bullough Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: the role of PufX EMBO J. 23 2004 690 700 (Pubitemid 38418737)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 690-700
    • Siebert, C.A.1    Qian, P.2    Fotiadis, D.3    Engel, A.4    Hunter, C.N.5    Bullough, P.A.6
  • 15
    • 20344374627 scopus 로고    scopus 로고
    • The 8.5 A projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides
    • DOI 10.1016/j.jmb.2005.04.032, PII S0022283605004419
    • P. Qian, C.N. Hunter, and P.A. Bullough The 8.5 angstrom projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides. J. Biol. Chem. 349 2005 948 960 (Pubitemid 40779618)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.5 , pp. 948-960
    • Qian, P.1    Hunter, C.N.2    Bullough, P.A.3
  • 17
    • 0942287196 scopus 로고    scopus 로고
    • Structural Role of PufX in the Dimerization of the Photosynthetic Core Complex of Rhodobacter sphaeroides
    • DOI 10.1074/jbc.M310050200
    • S. Scheuring, F. Francia, J. Busselez, B.A. Melandri, J.L. Rigaud, and D. Levy Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides J. Biol. Chem. 279 2004 3620 3626 (Pubitemid 38140603)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3620-3626
    • Scheuring, S.1    Francia, F.2    Busselez, J.3    Melandri, B.A.4    Rigaud, J.-L.5    Levy, D.6
  • 18
    • 12544254339 scopus 로고    scopus 로고
    • Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy
    • S. Scheuring, J. Busselez, and D. Levy Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy J. Biol. Chem. 280 2005 1426 1431
    • (2005) J. Biol. Chem. , vol.280 , pp. 1426-1431
    • Scheuring, S.1    Busselez, J.2    Levy, D.3
  • 19
    • 78649905308 scopus 로고    scopus 로고
    • Native architecture of the photosynthetic membrane from Rhodobacter veldkampii
    • L.N. Liu, J.N. Sturgis, and S. Scheuring Native architecture of the photosynthetic membrane from Rhodobacter veldkampii J. Struct. Biol. 173 2011 138 145
    • (2011) J. Struct. Biol. , vol.173 , pp. 138-145
    • Liu, L.N.1    Sturgis, J.N.2    Scheuring, S.3
  • 20
    • 36749102634 scopus 로고    scopus 로고
    • Structural Basis for the PufX-Mediated Dimerization of Bacterial Photosynthetic Core Complexes
    • DOI 10.1016/j.str.2007.09.026, PII S0969212607004182
    • J. Busselez, M. Cottevieille, P. Cuniasse, F. Gubellini, N. Boisset, and D. Levy Structural basis for the PufX-mediated dimerization of bacterial photosynthetic core complexes Structure 15 2007 1674 1683 (Pubitemid 350213415)
    • (2007) Structure , vol.15 , Issue.12 , pp. 1674-1683
    • Busselez, J.1    Cottevieille, M.2    Cuniasse, P.3    Gubellini, F.4    Boisset, N.5    Levy, D.6
  • 21
    • 46349084478 scopus 로고    scopus 로고
    • Structure, function and interactions of the PufX protein
    • K. Holden-Dye, L.I. Crouch, and M.R. Jones Structure, function and interactions of the PufX protein Biochim. Biophys. Acta 1777 2008 613 630
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 613-630
    • Holden-Dye, K.1    Crouch, L.I.2    Jones, M.R.3
  • 22
    • 0032475815 scopus 로고    scopus 로고
    • Projection structures of three photosynthetic complexes from Rhodobacter sphaeroides: LH2 at 6 A, LH1 and RC-LH1 at 25 A
    • DOI 10.1006/jmbi.1998.2050
    • T. Walz, S.J. Jamieson, C.M. Bowers, P.A. Bullough, and C.N. Hunter Projection structures of three photosynthetic complexes from Rhodobacter sphaeroides: LH2 at 6 Å, LH1 and RC-LH1 at 25 Å J. Mol. Biol. 282 1998 833 845 (Pubitemid 28442350)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.4 , pp. 833-845
    • Walz, T.1    Jamieson, S.J.2    Bowers, C.M.3    Bullough, P.A.4    Hunter, C.N.5
  • 23
    • 0036683068 scopus 로고    scopus 로고
    • Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrum at 8.5 A resolution
    • DOI 10.1093/emboj/cdf410
    • S.J. Jamieson, P. Wang, P. Qian, J.Y. Kirkland, M.J. Conroy, C.N. Hunter, and P.A. Bullough Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrum at 8.5 Å resolution. EMBO J. 21 2002 3927 3935 (Pubitemid 34857426)
    • (2002) EMBO Journal , vol.21 , Issue.15 , pp. 3927-3935
    • Jamieson, S.J.1    Wang, P.2    Qian, P.3    Kirkland, J.Y.4    Conroy, M.J.5    Hunter, C.N.6    Bullough, P.A.7
  • 25
    • 0347717833 scopus 로고    scopus 로고
    • Structural Analysis of the Reaction Center Light-harvesting Complex I Photosynthetic Core Complex of Rhodospirillum rubrum Using Atomic Force Microscopy
    • DOI 10.1074/jbc.M310382200
    • D. Fotiadis, P. Qian, A. Philippsen, P.A. Bullough, A. Engel, and C.N. Hunter Structural analysis of the reaction center light-harvesting complex I photosynthetic core complex of Rhodospirillum rubrum using atomic force microscopy J. Biol. Chem. 279 2004 2063 2068 (Pubitemid 38084478)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 2063-2068
    • Fotiadis, D.1    Qian, P.2    Philippsen, A.3    Bullough, P.A.4    Engel, A.5    Hunter, C.N.6
  • 26
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • S. Scheuring, and J.N. Sturgis Chromatic adaptation of photosynthetic membranes Science 309 2005 484 487
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 27
    • 28944431668 scopus 로고    scopus 로고
    • Architecture of the native photosynthetic apparatus of Phaeospirillum molischianum
    • DOI 10.1016/j.jsb.2005.10.002, PII S1047847705002261
    • R.P. Goncalves, A. Bernadac, J.N. Sturgis, and S. Scheuring Architecture of the native photosynthetic apparatus of Phaeospirillum molischianum J. Struct. Biol. 152 2005 221 228 (Pubitemid 41785519)
    • (2005) Journal of Structural Biology , vol.152 , Issue.3 , pp. 221-228
    • Goncalves, R.P.1    Bernadac, A.2    Sturgis, J.N.3    Scheuring, S.4
  • 28
    • 0024197376 scopus 로고
    • Pleiotropic effects of localized Rhodobacter capsulatus puf operon deletions on production of light-absorbing pigment-protein complexes
    • G. Klug, and S.N. Cohen Pleiotropic effects of localized Rhodobacter capsulatus puf operon deletions on production of light-absorbing pigment-protein complexes J. Bacteriol. 170 1988 5814 5821
    • (1988) J. Bacteriol. , vol.170 , pp. 5814-5821
    • Klug, G.1    Cohen, S.N.2
  • 29
    • 0025139203 scopus 로고
    • Complementation of a reaction center-deficient Rhodobacter sphaeroides pufLMX deletion strain in trans with pufBALM does not restore the photosynthesis-positive phenotype
    • J.W. Farchaus, H. Gruenberg, and D. Oesterhelt Complementation of a reaction center-ceficient Rhodobacter sphaeroides pufLMX deletion strain in trans with pufBALM does not restore the photosynthesis-positive phenotype J. Bacteriol. 172 1990 977 985 (Pubitemid 20070409)
    • (1990) Journal of Bacteriology , vol.172 , Issue.2 , pp. 977-985
    • Farchaus, J.W.1    Gruenberg, H.2    Oesterhelt, D.3
  • 30
    • 0026534726 scopus 로고
    • Pleiotropic effects of PufX gene deletion on the structure and function of the photosynthetic apparatus of Rhodobacter capsulatus
    • T.G. Lilburn, C.E. Haith, R.C. Prince, and J.T. Beatty Pleiotropic effects of PufX gene deletion on the structure and function of the photosynthetic apparatus of Rhodobacter capsulatus Biochim. Biophys. Acta 1100 1992 160 170
    • (1992) Biochim. Biophys. Acta , vol.1100 , pp. 160-170
    • Lilburn, T.G.1    Haith, C.E.2    Prince, R.C.3    Beatty, J.T.4
  • 31
    • 78249258718 scopus 로고    scopus 로고
    • Experimental evidence that the membrane-spanning helix of PufX adopts a bent conformation that facilitates dimerisation of the Rhodobacter sphaeroides RC-LH1 complex through N-terminal interactions
    • E.C. Ratcliffe, R.B. Tunnicliffe, I.W. Ng, P.G. Adams, P. Qian, K. Holden-Dye, M.R. Jones, M.P. Williamson, and C.N. Hunter Experimental evidence that the membrane-spanning helix of PufX adopts a bent conformation that facilitates dimerisation of the Rhodobacter sphaeroides RC-LH1 complex through N-terminal interactions Biochim. Biophys. Acta 1807 2011 95 107
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 95-107
    • Ratcliffe, E.C.1    Tunnicliffe, R.B.2    Ng, I.W.3    Adams, P.G.4    Qian, P.5    Holden-Dye, K.6    Jones, M.R.7    Williamson, M.P.8    Hunter, C.N.9
  • 32
    • 85047694996 scopus 로고    scopus 로고
    • Role of the N- and C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides
    • DOI 10.1046/j.1432-1327.2002.02834.x
    • F. Francia, J. Wang, H. Zischka, G. Venturoli, and D. Oesterhelt Role of the N- and C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides Eur. J. Biochem. 269 2002 1877 1885 (Pubitemid 34429669)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.7 , pp. 1877-1885
    • Francia, F.1    Wang, J.2    Zischka, H.3    Venturoli, G.4    Oesterhelt, D.5
  • 33
    • 79959277653 scopus 로고    scopus 로고
    • Monomeric RC-LH1 core complexes retard LH2 assembly and intracytoplasmic membrane formation in PufX-minus mutants of Rhodobacter sphaeroides
    • P.G. Adams, D.J. Mothersole, I.W. Ng, J.D. Olsen, and C.N. Hunter Monomeric RC-LH1 core complexes retard LH2 assembly and intracytoplasmic membrane formation in PufX-minus mutants of Rhodobacter sphaeroides Biochim. Biophys. Acta 1807 2011 1044 1055
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 1044-1055
    • Adams, P.G.1    Mothersole, D.J.2    Ng, I.W.3    Olsen, J.D.4    Hunter, C.N.5
  • 34
    • 15744405284 scopus 로고    scopus 로고
    • - membranes
    • DOI 10.1074/jbc.M412089200
    • F. Comayras, C. Jungas, and J. Lavergne Functional consequences of the organization of the photosynthetic apparatus in Rhodobacter sphaeroides: II. A study of PufX-membranes J. Biol. Chem. 280 2005 11214 11223 (Pubitemid 40418428)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11214-11223
    • Comayras, F.1    Jungas, C.2    Lavergne, J.3
  • 35
    • 0028972070 scopus 로고
    • Role of PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 1. PufX is required for efficient light-driven electron transfer and photophosphorylation under anaerobic conditions
    • W.P. Barz, F. Francia, G. Venturoli, B.A. Melandri, A. Vermeglio, and D. Oesterhelt Role of PufX protein in photosynthetic growth of Rhodobacter sphaeroides.1. PufX Is required for efficient light-driven electron-transfer and photophosphorylation under anaerobic conditions Biochemistry 34 1995 15235 15247 (Pubitemid 3005528)
    • (1995) Biochemistry , vol.34 , Issue.46 , pp. 15235-15247
    • Barz, W.P.1    Francia, F.2    Venturoli, G.3    Melandri, B.A.4    Vermeglio, A.5    Oesterhelt, D.6
  • 36
    • 0028863491 scopus 로고
    • Role of the PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 2. PufX is required for efficient ubiquinone ubiquinol exchange between the reaction-center QB site and the cytochrome bc1 complex
    • W.P. Barz, A. Vermeglio, F. Francia, G. Venturoli, B.A. Melandri, and D. Oesterhelt Role of the PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 2. PufX is required for efficient ubiquinone ubiquinol exchange between the reaction-center QB site and the cytochrome bc1 complex Biochemistry 34 1995 15248 15258
    • (1995) Biochemistry , vol.34 , pp. 15248-15258
    • Barz, W.P.1    Vermeglio, A.2    Francia, F.3    Venturoli, G.4    Melandri, B.A.5    Oesterhelt, D.6
  • 37
    • 0033603006 scopus 로고    scopus 로고
    • The reaction center-LH1 antenna complex of Rhodobacter sphaeroides contains one PufX molecule which is involved in dimerization of this complex
    • F. Francia, J. Wang, G. Venturoli, B.A. Melandri, W.P. Barz, and D. Oesterhelt The reaction center-LH1 antenna complex of Rhodobacter sphaeroides contains one PufX molecule which is involved in dimerization of this complex Biochemistry 38 1999 6834 6845
    • (1999) Biochemistry , vol.38 , pp. 6834-6845
    • Francia, F.1    Wang, J.2    Venturoli, G.3    Melandri, B.A.4    Barz, W.P.5    Oesterhelt, D.6
  • 38
    • 0442298612 scopus 로고    scopus 로고
    • Phylogenetic distribution of unusual triheme to tetraheme cytochrome subunit in the reaction center complex of purple photosynthetic bacteria
    • DOI 10.1023/B:PRES.0000011922.56394.92
    • Y. Tsukatani, K. Matsuura, S. Masuda, K. Shimada, A. Hiraishi, and K.V.P. Nagashima Phylogenetic distribution of unusual triheme to tetraheme cytochrome subunit in the reaction center complex of purple photosynthetic bacteria Photosynth. Res. 79 2004 83 91 (Pubitemid 38184777)
    • (2004) Photosynthesis Research , vol.79 , Issue.1 , pp. 83-91
    • Tsukatani, Y.1    Matsuura, K.2    Masuda, S.3    Shimada, K.4    Hiraishi, A.5    Nagashima, K.V.P.6
  • 41
    • 0031936540 scopus 로고    scopus 로고
    • Demonstration of the key role played by the PufX protein in the functional and structural organization of native and hybrid bacterial photosynthetic core complexes
    • T.K. Fulcher, J.T. Beatty, and M.R. Jones Demonstration of the key role played by the PufX protein in the functional and structural organization of native and hybrid bacterial photosynthetic core complexes J. Bacteriol. 180 1998 642 646 (Pubitemid 28100548)
    • (1998) Journal of Bacteriology , vol.180 , Issue.3 , pp. 642-646
    • Fulcher, T.K.1    Beatty, J.T.2    Jones, M.R.3
  • 42
    • 0026586530 scopus 로고
    • Mutants of Rhodobacter sphaeroides lacking one or more pigment-protein complexes and complementation with reaction-centre, LH1, and LH2 genes
    • M.R. Jones, G.J. Fowler, L.C. Gibson, G.G. Grief, J.D. Olsen, W. Crielaard, and C.N. Hunter Mutants of Rhodobacter sphaeroides lacking one or more pigment-protein complexes and complementation with reaction-centre, LH1, and LH2 genes Mol. Microbiol. 6 1992 1173 1184
    • (1992) Mol. Microbiol. , vol.6 , pp. 1173-1184
    • Jones, M.R.1    Fowler, G.J.2    Gibson, L.C.3    Grief, G.G.4    Olsen, J.D.5    Crielaard, W.6    Hunter, C.N.7
  • 43
    • 0000948757 scopus 로고
    • Transfer of genes coding for apoproteins of reaction center and light-harvesting LH1 complexes to Rhodobacter sphaeroides
    • C.N. Hunter, and G. Turner Transfer of genes coding for apoproteins of reaction center and light-harvesting LH1 complexes to Rhodobacter sphaeroides J. Gen. Microbiol. 134 1988 1471 1480
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1471-1480
    • Hunter, C.N.1    Turner, G.2
  • 44
    • 0019354993 scopus 로고
    • Generation of succinyl-coenzyme-a in photosynthetic bacteria
    • J.T. Beatty, and H. Gest Generation of succinyl-coenzyme-a in photosynthetic bacteria Arch. Microbiol. 129 1981 335 340
    • (1981) Arch. Microbiol. , vol.129 , pp. 335-340
    • Beatty, J.T.1    Gest, H.2
  • 45
    • 0026038339 scopus 로고
    • DNA sequencing and complementation/deletion analysis of the bchA-puf operon region of Rhodobacter sphaeroides: In vivo mapping of the oxygen-regulated puf promoter
    • C.N. Hunter, P. Mcglynn, M.K. Ashby, J.G. Burgess, and J.D. Olsen DNA sequencing and complementation deletion analysis of the bcha-puf operon region of Rhodobacter sphaeroides- in vivo mapping of the oxygen-regulated puf promoter Mol. Microbiol. 5 1991 2649 2661 (Pubitemid 21895998)
    • (1991) Molecular Microbiology , vol.5 , Issue.11 , pp. 2649-2661
    • Hunter, C.N.1    McGlynn, P.2    Ashby, M.K.3    Burgess, J.G.4    Olsen, J.D.5
  • 46
    • 77956262848 scopus 로고    scopus 로고
    • Dimerisation of the Rhodobacter sphaeroides RC-LH1 photosynthetic complex is not facilitated by a GxxxG motif in the PufX polypeptide
    • L.I. Crouch, K. Holden-Dye, and M.R. Jones Dimerisation of the Rhodobacter sphaeroides RC-LH1 photosynthetic complex is not facilitated by a GxxxG motif in the PufX polypeptide Biochim. Biophys. Acta 1797 2010 1812 1819
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1812-1819
    • Crouch, L.I.1    Holden-Dye, K.2    Jones, M.R.3
  • 47
    • 0028331145 scopus 로고
    • Site-specific mutagenesis of the reaction centre from Rhodobacter sphaeroides studied by Fourier transform Raman spectroscopy: Mutations at tyrosine M210 do not affect the electronic structure of the primary donor
    • M.R. Jones, M. Heer-Dawson, T.A. Mattioli, C.N. Hunter, and B. Robert Site-specific mutagenesis of the reaction centre from Rhodobacter sphaeroides studied by Fourier transform Raman spectroscopy: mutations at tyrosine M210 do not affect the electronic structure of the primary donor FEBS Lett. 339 1994 18 24
    • (1994) FEBS Lett. , vol.339 , pp. 18-24
    • Jones, M.R.1    Heer-Dawson, M.2    Mattioli, T.A.3    Hunter, C.N.4    Robert, B.5
  • 48
    • 33748284893 scopus 로고    scopus 로고
    • Functional and structural analysis of the photosynthetic apparatus of Rhodobacter veldkampii
    • DOI 10.1021/bi0610000
    • F. Gubellini, F. Francia, J. Busselez, G. Venturoli, and D. Levy Functional and structural analysis of the photosynthetic apparatus of Rhodobacter veldkampii Biochemistry 45 2006 10512 10520 (Pubitemid 44320467)
    • (2006) Biochemistry , vol.45 , Issue.35 , pp. 10512-10520
    • Gubellini, F.1    Francia, F.2    Busselez, J.3    Venturoli, G.4    Levy, D.5
  • 49
    • 0026741627 scopus 로고
    • Construction and characterization of a mutant of Rhodobacter sphaeroides with the reaction center as the sole pigment-protein complex
    • M.R. Jones, R.W. Visschers, R. van Grondelle, and C.N. Hunter Construction and characterization of a mutant of Rhodobacter sphaeroides with the reaction center as the sole pigment-protein complex Biochemistry 31 1992 4458 4465
    • (1992) Biochemistry , vol.31 , pp. 4458-4465
    • Jones, M.R.1    Visschers, R.W.2    Van Grondelle, R.3    Hunter, C.N.4
  • 50
    • 0028101094 scopus 로고
    • The Rhodobacter sphaeroides PufX protein is not required for photosynthetic competence in the absence of a light harvesting system
    • DOI 10.1016/0014-5793(94)00701-2
    • P. McGlynn, C.N. Hunter, and M.R. Jones The Rhodobacter sphaeroides PufX protein is not required for photosynthetic competence in the absence of a light harvesting system FEBS Lett. 349 1994 349 353 (Pubitemid 24264772)
    • (1994) FEBS Letters , vol.349 , Issue.3 , pp. 349-353
    • McGlynn, P.1
  • 51
    • 0001753915 scopus 로고
    • Oligomerization states and associations of light-harvesting pigment protein complexes of Rhodobacter sphaeroides as analyzed by lithium dodecyl-sulfate polyacrylamide-gel electrophoresis
    • C.N. Hunter, J.D. Pennoyer, J.N. Sturgis, D. Farrelly, and R.A. Niederman Oligomerization states and associations of light-harvesting pigment protein complexes of Rhodobacter sphaeroides as analyzed by lithium dodecyl-sulfate polyacrylamide-gel electrophoresis Biochemistry 27 1988 3459 3467
    • (1988) Biochemistry , vol.27 , pp. 3459-3467
    • Hunter, C.N.1    Pennoyer, J.D.2    Sturgis, J.N.3    Farrelly, D.4    Niederman, R.A.5
  • 52
    • 12244267987 scopus 로고    scopus 로고
    • Roseobacter-like bacteria in Red and Mediterranean Sea aerobic anoxygenic photosynthetic populations
    • DOI 10.1128/AEM.71.1.344-353.2005
    • A. Oz, G. Sabehi, M. Koblizek, R. Massana, and O. Beja Roseobacter-like bacteria in Red and Mediterranean Sea aerobic anoxygenic photosynthetic populations Appl. Environ. Microbiol. 71 2005 344 353 (Pubitemid 40116288)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.1 , pp. 344-353
    • Oz, A.1    Sabehi, G.2    Koblizek, M.3    Massana, R.4    Beja, O.5
  • 53
    • 28644435670 scopus 로고    scopus 로고
    • Aerobic anoxygenic photosynthesis genes and operons in uncultured bacteria in the Delaware River
    • DOI 10.1111/j.1462-2920.2005.00883.x
    • L.A. Waidner, and D.L. Kirchman Aerobic anoxygenic photosynthesis genes and operons in uncultured bacteria in the Delaware River Environ. Microbiol. 7 2005 1896 1908 (Pubitemid 41752379)
    • (2005) Environmental Microbiology , vol.7 , Issue.12 , pp. 1896-1908
    • Waidner, L.A.1    Kirchman, D.L.2
  • 54
    • 77953946504 scopus 로고    scopus 로고
    • Occurrence and sequence of Sphaeroides Heme Protein and diheme cytochrome C in purple photosynthetic bacteria in the family Rhodobacteraceae
    • T.E. Meyer, J.A. Kyndt, M.A. Cusanovich, Occurrence and sequence of Sphaeroides Heme Protein and diheme cytochrome C in purple photosynthetic bacteria in the family Rhodobacteraceae, BMC Biochem 11 (2010) 24.
    • (2010) BMC Biochem , vol.11 , pp. 24
    • Meyer, T.E.1    Kyndt, J.A.2    Cusanovich, M.A.3
  • 55
    • 0037047004 scopus 로고    scopus 로고
    • Isolation, size estimates, and spectral heterogeneity of an oligomeric series of light-harvesting 1 complexes from Rhodobacter sphaeroides
    • DOI 10.1021/bi011663b
    • W.H. Westerhuis, J.N. Sturgis, E.C. Ratcliffe, C.N. Hunter, and R.A. Niederman Isolation, size estimates, and spectral heterogeneity of an oligomeric series of light-harvesting 1 complexes from Rhodobacter sphaeroides Biochemistry 41 2002 8698 8707 (Pubitemid 34743310)
    • (2002) Biochemistry , vol.41 , Issue.27 , pp. 8698-8707
    • Westerhuis, W.H.J.1    Sturgis, J.N.2    Ratcliffe, E.C.3    Hunter, C.N.4    Niederman, R.A.5
  • 56
    • 0023972876 scopus 로고
    • Physiological and structural analysis of light-harvesting mutants of Rhodobacter sphaeroides
    • P.J. Kiley, A. Varga, and S. Kaplan Physiological and structural analysis of light-harvesting mutants of Rhodobacter sphaeroides J. Bacteriol. 170 1988 1103 1115
    • (1988) J. Bacteriol. , vol.170 , pp. 1103-1115
    • Kiley, P.J.1    Varga, A.2    Kaplan, S.3
  • 57
    • 46649110611 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of a membrane-bending complex: The RC-LH1-PufX core dimer of Rhodobacter sphaeroides
    • P. Qian, P.A. Bullough, and C.N. Hunter Three-dimensional reconstruction of a membrane-bending complex: the RC-LH1-PufX core dimer of Rhodobacter sphaeroides J. Biol. Chem. 283 2008 14002 14011
    • (2008) J. Biol. Chem. , vol.283 , pp. 14002-14011
    • Qian, P.1    Bullough, P.A.2    Hunter, C.N.3
  • 58
    • 0029792822 scopus 로고    scopus 로고
    • Formation of the light-harvesting complex I (B870) of anoxygenic phototrophic purple bacteria
    • DOI 10.1007/s002030050370
    • G. Drews Formation of the light-harvesting complex I (B870) of anoxygenic phototrophic purple bacteria Arch. Microbiol. 166 1996 151 159 (Pubitemid 26306743)
    • (1996) Archives of Microbiology , vol.166 , Issue.3 , pp. 151-159
    • Drews, G.1
  • 60
    • 0019171764 scopus 로고
    • Rhodopseudomonas blastica sp.nov.: A member of the Rhodospirillaceae
    • K. Eckersley, and C.S. Dow Rhodopseudomonas blastica Sp-Nov - a member of the Rhodospirillaceae J. Gen. Microbiol. 119 1980 465 473 (Pubitemid 11216709)
    • (1980) Journal of General Microbiology , vol.119 , Issue.2 , pp. 465-473
    • Eckersley, K.1    Dow, C.S.2
  • 61
    • 0027485443 scopus 로고
    • Is intracytoplasmic membrane structure a generic criterion? It does not coincide with phylogenetic interrelationships among phototrophic purple nonsulfur bacteria
    • H. Kawasaki, Y. Hoshino, A. Hirata, and K. Yamasato Is intracytoplasmic membrane structure a generic criterion? It does not coincide with phylogenetic interrelationships among phototrophic purple nonsulfur bacteria Arch. Microbiol. 160 1993 358 362 (Pubitemid 23290216)
    • (1993) Archives of Microbiology , vol.160 , Issue.5 , pp. 358-362
    • Kawasaki, H.1    Hoshimo, Y.2    Hirata, A.3    Yamasato, K.4
  • 62
    • 72249117552 scopus 로고    scopus 로고
    • A glycophorin A-Like framework for the dimerization of photosynthetic core complexes
    • J. Hsin, C. Chipot, and K. Schulten A glycophorin A-Like framework for the dimerization of photosynthetic core complexes JACS 131 2009 17096-+.
    • (2009) JACS , vol.131 , pp. 17096
    • Hsin, J.1    Chipot, C.2    Schulten, K.3
  • 63
    • 0027050182 scopus 로고
    • Sequence specificity in the dimerization of transmembrane α-helices
    • DOI 10.1021/bi00166a002
    • M.A. Lemmon, J.M. Flanagan, H.R. Treutlein, J. Zhang, and D.M. Engelman Sequence specificity in the dimerization of transmembrane alpha-helices Biochemistry 31 1992 12719 12725 (Pubitemid 23027049)
    • (1992) Biochemistry , vol.31 , Issue.51 , pp. 12719-12725
    • Lemmon, M.A.1    Flanagan, J.M.2    Treutlein, H.R.3    Zhang, J.4    Engelman, D.M.5
  • 65
    • 0029885004 scopus 로고    scopus 로고
    • Directed mutagenesis of the Rhodobacter capsulatus puhA gene and Orf 214: Pleiotropic effects on photosynthetic reaction center and light-harvesting 1 complexes
    • D.K. Wong, W.J. Collins, A. Harmer, T.G. Lilburn, and J.T. Beatty Directed mutagenesis of the Rhodobacter capsulatus puhA gene and orf 214: pleiotropic effects on photosynthetic reaction center and light-harvesting 1 complexes J. Bacteriol. 178 1996 2334 2342 (Pubitemid 26123499)
    • (1996) Journal of Bacteriology , vol.178 , Issue.8 , pp. 2334-2342
    • Wong, D.K.-H.1    Collins, W.J.2    Harmer, A.3    Lilburn, T.G.4    Beatty, J.T.5
  • 66
    • 37749024601 scopus 로고    scopus 로고
    • The PucC protein of Rhodobacter capsulatus mitigates an inhibitory effect of light-harvesting 2 alpha and beta proteins on light-harvesting complex 1
    • P.R. Jaschke, H.N. Leblanc, A.S. Lang, and J.T. Beatty The PucC protein of Rhodobacter capsulatus mitigates an inhibitory effect of light-harvesting 2 alpha and beta proteins on light-harvesting complex 1 Photosynth. Res. 95 2008 279 284
    • (2008) Photosynth. Res. , vol.95 , pp. 279-284
    • Jaschke, P.R.1    Leblanc, H.N.2    Lang, A.S.3    Beatty, J.T.4
  • 67
    • 0032483080 scopus 로고    scopus 로고
    • Isolation of the PufX protein from Rhodobacter capsulatus and Rhodobacter sphaeroides: Evidence for its interaction with the α- polypeptide of the core light-harvesting complex
    • DOI 10.1021/bi980657l, PII S0006296098006576
    • P.A. Recchia, C.M. Davis, T.G. Lilburn, J.T. Beatty, P.S. Parkes-Loach, C.N. Hunter, and P.A. Loach Isolation of the PufX protein from Rhodobacter capsulatus and Rhodobacter sphaeroides: evidence for its interaction with the alpha-polypeptide of the core light-harvesting complex Biochemistry 37 1998 11055 11063 (Pubitemid 28368932)
    • (1998) Biochemistry , vol.37 , Issue.31 , pp. 11055-11063
    • Recchia, P.A.1    Davis, C.M.2    Lilburn, T.G.3    Beatty, J.T.4    Parkes-Loach, P.S.5    Hunter, C.N.6    Loach, P.A.7
  • 68
    • 0035873776 scopus 로고    scopus 로고
    • Role of the core region of the PufX protein in inhibition of reconstitution of the core light-harvesting complexes of Rhodobacter sphaeroides and Rhodobacter capsulatus
    • DOI 10.1021/bi002580i
    • P.S. Parkes-Loach, C.J. Law, P.A. Recchia, J. Kehoe, S. Nehrlich, J. Chen, and P.A. Loach Role of the core region of the PufX protein in inhibition of reconstitution of the core light-harvesting complexes of Rhodobacter sphaeroides and Rhodobacter capsulatus Biochemistry 40 2001 5593 5601 (Pubitemid 32440863)
    • (2001) Biochemistry , vol.40 , Issue.19 , pp. 5593-5601
    • Parkes-Loach, P.S.1    Law, C.J.2    Recchia, P.A.3    Kehoe, J.4    Nehrlich, S.5    Chen, J.6    Loach, P.A.7
  • 69
    • 33645100807 scopus 로고    scopus 로고
    • The photosynthetic apparatus of Rhodopseudomonas palustris: Structures and organization
    • S. Scheuring, R.P. Goncalves, V. Prima, and J.N. Sturgis The photosynthetic apparatus of Rhodopseudomonas palustris: structures and organization J. Mol. Biol. 358 2006 83 96
    • (2006) J. Mol. Biol. , vol.358 , pp. 83-96
    • Scheuring, S.1    Goncalves, R.P.2    Prima, V.3    Sturgis, J.N.4
  • 71
    • 33845433893 scopus 로고    scopus 로고
    • The solution structure of the PufX polypeptide from Rhodobacter sphaeroides
    • DOI 10.1016/j.febslet.2006.11.065, PII S0014579306014062
    • R.B. Tunnicliffe, E.C. Ratcliffe, C.N. Hunter, and M.P. Williamson The solution structure of the PufX polypeptide from Rhodobacter sphaeroides FEBS Lett. 580 2006 6967 6971 (Pubitemid 44909143)
    • (2006) FEBS Letters , vol.580 , Issue.30 , pp. 6967-6971
    • Tunnicliffe, R.B.1    Ratcliffe, E.C.2    Hunter, C.N.3    Williamson, M.P.4
  • 72
    • 33947631898 scopus 로고    scopus 로고
    • Solution structure of the Rhodobacter sphaeroides PufX membrane protein: Implications for the quinone exchange and protein-protein interactions
    • DOI 10.1021/bi0618060
    • Z.Y. Wang, H. Suzuki, M. Kobayashi, and T. Nozawa Solution structure of the Rhodobacter sphaeroides PufX membrane protein: Implications for the quinone exchange and protein-protein interactions Biochemistry 46 2007 3635 3642 (Pubitemid 46493464)
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3635-3642
    • Wang, Z.-Y.1    Suzuki, H.2    Kobayashi, M.3    Nozawa, T.4
  • 73
    • 0032494286 scopus 로고    scopus 로고
    • The LH1-RC core complex of Rhodobacter sphaeroides: Interaction between components, time-dependent assembly, and topology of the PufX protein
    • DOI 10.1016/S0005-2728(98)00131-5, PII S0005272898001315
    • R.J. Pugh, P. McGlynn, M.R. Jones, and C.N. Hunter The LH1-RC core complex of Rhodobacter sphaeroides: interaction between components, time-dependent assembly, and topology of the PufX protein Biochim. Biophys. Acta 1366 1998 301 316 (Pubitemid 29164404)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1366 , Issue.3 , pp. 301-316
    • Pugh, R.J.1    McGlynn, P.2    Jones, M.R.3    Hunter, C.N.4
  • 74
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • A. Bairoch, and R. Apweiler The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000 Nucleic Acids Res. 28 2000 45 48 (Pubitemid 30047711)
    • (2000) Nucleic Acids Research , vol.28 , Issue.1 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 75
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25 1997 4876 4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5


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