Two-dimensional crystallization of the light-harvesting I-reaction centre photounit from Rhodospirillum rubrum.

A stoichiometric unit of the light-harvesting complex I and the reaction centre (LHI-RC complex) has been isolated from a carotenoid-less mutant of the purple non-sulphur bacterium Rhodospirillum rubrum by mild solubilization of photosynthetic membranes with the phospholipid detergent diheptylphosphatidylcholine. Dialysis of the isolated LHI-RC complexes in the presence of added dioleoyl-sn-phosphatidylcholine produced ordered two-dimensional crystals. Digital image processing revealed that the LHI-RC are packed together in a square lattice (a = b = 16.3 nm). The dimensions of the LHI ring are essentially identical with those determined from two-dimensional (2D) crystals of purified carotenoid-containing light-harvesting I complexes after analysis by cryo-electron microscopic techniques or from negatively stained 2D crystals of purified LHI complexes from a carotenoid-less mutant. Each LHI ring of the LHI-RC complex contains a central diffuse stain-excluding region, which is assigned to the reaction centre. The analysis of the LHI-RC 2D crystals strongly suggests that the geometry and subunit stoichiometry of the LHI ring is unaffected by the presence of a reaction centre that can probably assume various orientations within the ring.

[1]  Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum. , 1995, Journal of molecular biology.

[2]  R. Picorel,et al.  Rotational mobility of the photoreaction center in chromatophore membranes of Rhodospirillum rubrum , 1981 .

[3]  P. Bullough,et al.  The 8.5 A projection map of the light‐harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits. , 1995, The EMBO journal.

[4]  R. Ghosh,et al.  Characterization of Rhodospirillum rubrum ST2. A new Tn5-induced carotenoid-less mutant for functional studies , 1996 .

[5]  R. Ghosh,et al.  Protein phosphorylation in Rhodospirillum rubrum: purification and characterization of a water-soluble B873 protein kinase and a new component of the B873 complex, Ω, which can be phosphorylated , 1994 .

[6]  P R Smith,et al.  A study of the structure of the T-layer of Bacillus brevis. , 1973, Journal of supramolecular structure.

[7]  T. G. Monger,et al.  Singlet-triplet fusion in Rhodopseudomonas sphaeroides chromatophores. A probe of the organization of the photosynthetic apparatus. , 1977, Biochimica et biophysica acta.

[8]  A. Hoenger,et al.  Two-dimensional crystallization of the light-harvesting complex from Rhodospirillum rubrum. , 1993, Journal of molecular biology.

[9]  D. Oesterhelt,et al.  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. , 1995, Biochemistry.

[10]  D. Engelman,et al.  Membrane protein folding and oligomerization: the two-stage model. , 1990, Biochemistry.

[11]  K. Miller.  Three-dimensional structure of a photosynthetic membrane , 1982, Nature.

[12]  D. Oesterhelt,et al.  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. , 1995, Biochemistry.

[13]  N. W. Isaacs,et al.  Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria , 1995, Nature.

[14]  T O Yeates,et al.  Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[15]  H. Hauser,et al.  Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity. , 1994, Biochemistry.

[16]  P. Loach,et al.  Quantitative dissolution of the membrane and preparation of photoreceptor subunits from Rhodopseudomonas spheroides. , 1970, Biochemistry.

[17]  A. Crofts,et al.  Complexes or super complexes: inhibitor titrations show that electron transfer in chromatophores from Rhodobacter sphaeroides involves a dimeric UQH2:cytochrome c2 oxidoreductase, and is delocalized. , 1991, Biochemical Society transactions.

[18]  R. Grondelle.  Excitation energy transfer, trapping and annihilation in photosynthetic systems , 1985 .

[19]  K. Schulten,et al.  The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum. , 1996, Structure.

[20]  C. Bauer,et al.  Analysis of the Rhodobacter capsulatus puf operon. Location of the oxygen-regulated promoter region and the identification of an additional puf-encoded gene. , 1988, The Journal of biological chemistry.

[21]  K. Mühlethaler,et al.  The preparation and characterisation of native photoreceptor units from the thylakoids of Rhodopseudomonas viridis , 1984, The EMBO journal.

[22]  P. Corriveau,et al.  The structural genes coding for the L and M subunits of Rhodospirillum rubrum photoreaction center. , 1988, The Journal of biological chemistry.

[23]  H. Osiewacz,et al.  Genome analysis of filamentous fungi : identification of a highly conserved simple repetitive sequence in different strains of Podospora anserina , 1996 .

[24]  G. Mclendon,et al.  Electron transfer in inorganic, organic, and biological systems. , 1991 .

[25]  A. Verméglio,et al.  Electron transfer between primary and secondary donors in Rhodospirillum rubrum: evidence for a dimeric association of reaction centers. , 1990, Biochemistry.

[26]  E. Wehrli,et al.  The structure of the photoreceptor unit of Rhodopseudomonas viridis , 1984, The EMBO journal.

[27]  M. Michel-beyerle.  Antennas and Reaction Centers of Photosynthetic Bacteria , 1985 .

[28]  T. Walz,et al.  The three‐dimensional structure of human erythrocyte aquaporin CHIP. , 1994, The EMBO journal.

[29]  D. Oesterhelt,et al.  A Rhodobacter sphaeroides puf L, M and X deletion mutant and its complementation in trans with a 5.3 kb puf operon shuttle fragment , 1989, The EMBO journal.

[30]  W. Baumeister,et al.  Stoichiometric model of the photosynthetic unit of Ectothiorhodospira halochloris. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[31]  R. W. Visschers,et al.  Structural characterization of the B800-850 and B875 light-harvesting antenna complexes from Rhodobacter sphaeroides by electron microscopy , 1993 .

[32]  W. R. Sistrom,et al.  CONTROL OF SYNTHESIS OF REACTION CENTER BACTERIOCHLOROPHYLL IN PHOTOSYNTHETIC BACTERIA , 1972, Photochemistry and photobiology.

[33]  R. Ghosh,et al.  Characterization of Rhodospirillum rubrum ST2. A new Tn5-induced [Transposon5 induced] carotenoid-less mutant for functional studies , 1996 .

[34]  H. Zuber.  Structure of Antenna Polypeptides , 1985 .

[35]  G. Montoya,et al.  Two-dimensional structure of light harvesting complex II (LHII) from the purple bacterium Rhodovulum sulfidophilum and comparison with LHII from Rhodopseudomonas acidophila. , 1996, Structure.

[36]  T. Donohue,et al.  Transcriptional analysis of puf operon expression in Rhodobacter sphaeroides 2.4.1 and an intercistronic transcription terminator mutant. , 1989, The Journal of biological chemistry.

[37]  J. Deisenhofer,et al.  Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution , 1985, Nature.

[38]  M. Kataoka,et al.  Structural order in chromatophore membranes of Rhodospirillum rubrum , 1976, Nature.

[39]  P. Loach,et al.  Quantitative dissolution of the membrane and preparation of photoreceptor subunits from Rhodospirillum rubrum. , 1970, Biochemistry.