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PubMed1976

[Reconstruction of the function of membrane potential formation by isolated pigment-protein complexes of Rhodospirillum rubrum].

The pigment-protein complexes, containing the photosynthetic reaction centers and chlorophyll antenna, were isolated from non-sulfur purple bacteria Rhodospirillum rubrum, by use of cholate. Absorption spectra and quantum yield of photo-oxidation of bacteriochlorophyll P870 of complexes were similar to those of chromatophores. The procedure of reconstitution of proteoliposomes from phospholipids and complexes was proposed. The proteoliposomes incubated with CoQ6 and TMPD upon illumination are generating the transmembrane electric potential difference (plus inside proteoliposomes). The electric potential difference was registered by three independent methods: by transmembrane electrophoresis of penetrating anions PCB-, by direct measurement with using voltmeter in system "proteoliposome--planar membrane" and electrochromic absorption band shifts of bacteriochlorophyll.

Chemical Phenomena↗
PubMed1996

Mutation of Tyr235 in the NAD(H)-binding subunit of the proton-translocating nicotinamide nucleotide transhydrogenase of Rhodospirillum rubrum affects the conformational dynamics of a mobile loop and lowers the catalytic activity of the enzyme.

The Tyr residue in the mobile loop region of the soluble, domain I polypeptide (called Ths) of the proton-translocating transhydrogenase from Rhodospirillum rubrum has been substituted by Asn and by Phe. The recombinant proteins were expressed at high levels in Escherichia coli and purified to homogeneity. The two well defined resonances at 6.82 and 7.12ppm, observed in the one-dimensional proton NMR spectrum of wild-type protein, and previously attributed to the Tyr residue, were absent in both mutants. In the Tyr235 --> Phe mutant Ths, they were replaced by two new resonances at 7.26 and 7.33 ppm, characteristic of a Phe residue. In both mutants, narrow resonances attributable to Met residues (and in the Tyr235 --> Phe mutant, resonances attributable to Ala residues) were shifted relative to the wild type, but other features in the NMR spectra were unaffected. The conformational dynamics of the mobile loop closure in response to nucleotide binding by the protein were altered in the two mutants. The fluorescence emission from Trp72 was unaffected by both Tyr substitutions, and the fluorescence was still quenched by NADH. The mutant Ths proteins bound to chromatophore membranes depleted of their native Ths with undiminished affinity. In these reconstituted systems, the Km values for thio-NADP+ and NADH, during light-driven transhydrogenation, were similar to those of wild-type, but the kcat values were decreased about 2-fold. In reverse transhydrogenation, the Kmvalues for NADPH were slightly decreased in the mutants relative to wild-type, but those for acetyl pyridine adenine dinucleotide were increased about 10- and 13-fold, respectively, and the kcat values were decreased about 2- and 5-fold, respectively, in the Tyr235 --> Phe and Tyr235 --> Asn mutants. It is concluded that Tyr235 may contribute to the process of nucleotide binding and that substitution of this residue prevents proper functioning of the mobile loop in catalysis.

Asparagine↗
PubMed1996

Localization of mRNAs for insulin-like growth factor-I (IGF-I), IGF-I receptor, and IGF binding proteins in rat eye.

PURPOSE: To localize mRNAs for insulin-like growth factor (IGF)-I, IGF-I receptor (IGF-IR), and IGF binding protein (BP)-1 to IGFBP-6 in the rat eye. METHODS: cDNA sequences for IGF-I, IGF-IR, and IGFBP-1 to IGFBP-6 were used to synthesize 35S-CTP labeled antisense and sense probes for in situ hybridization on 5-microns sections of the rat eye, including the retina, choroid, sclera, ciliary body, and cornea. RESULTS: IGF-I mRNA was demonstrated over ganglion cells of the retina and endothelial cells of the choroid and ciliary processes. IGF-IR mRNA showed more extensive distribution, localizing to the retinal ganglion cell layer, inner nuclear layer, and outer limiting membrane and also the outer nonpigmented epithelium of the ciliary processes and cornea, conjunctiva, and lens. IGFBP-2 mRNA localized to outer nonpigmented epithelia of the ciliary processes and the germinal layer of corneal epithelium as well as iris, conjunctiva, and sclera. Messenger RNAs for IGFBP-3 to IGFBP-6 localized to choroidal endothelial cells and chromatophores and also to the inner pigmented epithelium of the ciliary processes. Messenger RNAs for IGFBP-5 and IGFBP-6 were seen in the inner and outer nuclear layers of the neural retina. IGFBP-1 mRNA was not detected within the rat eye. CONCLUSIONS: Using in situ hybridization, we have demonstrated mRNAs for IGF-I, IGF-IR, and IGFBP-2 to IGFBP-6 in specific histologic layers of the retina, choroid, ciliary body, and cornea in the rat. The characterization of the IGF system in vivo suggests specific roles in the normal eye and provides a basis for studying the IGF system in eye pathology.

Animals↗
PubMed1995

Tissue distribution and subcellular localization of Na+ channel mRNA in the nervous system of the squid, Loligo opalescens.

Recent cloning of a putative Na+ channel alpha subunit cDNA, GFLN1, from the squid stellate ganglion has allowed us to study the expression of this ion channel at a cellular level. In situ hybridizations with a probe derived from and specific to 3' untranslated and coding sequence of GFLN1 were used to determine its tissue distribution as well as its subcellular localization. In sections of the stellate ganglion, the probe labeled all of the cells in the giant fiber lobe (GFL) and most cells in the cellular layer of the main ganglion. In these non-GFL portions of the stellate ganglion, labeling was particularly intense in the ventral large cells and weak or absent in the dorsal small cells. In the optic lobe, only a select group of cells, the second-order visual giant neurons, were intensely labeled. These results are consistent with electrophysiological data that show GFL-like Na+ currents in rare large cells dissociated from the optic lobe and in most but not all cells from the non-GFL part of the stellate ganglion. In sections of the subesophageal mass of the central nervous system, strong labeling for GFLN1 mRNA occurred in the fin lobe, posterior chromatophore lobe, central and latero-ventral palliovisceral lobes, and posterior pedal lobe. In all cases, labeling was detected only in the cellular layer of these tissues and never in nerves or neuropil. In situ hybridization with dissociated GFL neurons maintained in primary culture verified that Na+ channel mRNA is confined to the cell body. These results indicate that GFLN1 is expressed predominately in large cells with large or long axons, and that this mRNA is restricted to the cell bodies of these neurons.

Animals↗
PubMed1998

Effect of modification of histidine residues on organization of the pigment--protein complexes of chromatium minutissimum

The effect of diethyl pyrocarbonate on chromatophores and isolated pigment--protein complexes of Chromatium minutissimum was studied. It is shown that modification of histidine residues results in the destruction of the core antenna LHI (B880) and in a spectral shift from 850 to 830 nm in the peripheral antenna LHII (B800-850). In the purple sulfur bacterium Chromatium minutissimum the pigment--protein complexes B800-B850 (peripheral antenna, LHII) and B880 (core antenna, LHI) collect and transmit the absorbed light energy to the reaction centers. The composition of pigments and proteins as well as primary structure of the majority of polypeptides in both types of complexes from various photosynthetic bacteria have been determined.

Journal Article↗