Zur Taxonomie von Rhodopseudomonas palustris

Zusammenfassung Eine Reihe von Rhodopseudomonas palustris-Stämmen aus verschiedenen Herkünften wurden vergleichend unter Verwendung folgender Merkmale untersucht: Substratverwertung, in vivo-Absorptionsspektrum und Serologie der O-Antigene. Die gegen 2 Stämme gerichteten Antiseren zeigen hohe Spezifität. Die Verwendbarkeit der serologischen Kreuzreaktion für taxonomische Untersuchungen bei photosynthetischen Bakterien wird diskutiert.

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On the taxonomy of Rhodopseudomonas palustris

Summary Strains of Rhodopseudomonas palustris isolated from different habitats were compared with respect to their taxonomic features. All strains grew very well on formiate, acetate, propionate, butyrate, aspartate, inositol, ethanol, fructose, and p-amino-benzoate, respectively, as single carbon source. Most of the strains were able to use benzoic acid or glucose, too. But alanine was not found to be a good substrate. The maxima of the bacteriochlorophyll in-vivo-absorption spectra were estimated to be 376, 589, 802–805, and 858–875 nm. The shift of the infrared peak in the different strains is loosely correlated with the change of the carotenoid in vivo spectrum, the maxima of which were measured to be 470–480 nm (shoulder) 495–505 nm, and 520–545 nm (shoulder). Antisera were prepared against the strains 1e5 and 11/1. It was demonstrated that these antisera were directed against the lipopolysaccharides (O-antigen) of these bacteria. The antigen of 1e5 does not cross react with the antigen of 11/1. Strain 1e5 is the only one of 17 strains tested which is sensitive to the bacteriophage Rp1. The antigen of this strain cross reacted only with the antigen of strain K1. In contrast, the antigen of strain 11/1 cross reacted in some degree with most of the tested strains of Rps. palustris. No or very weak cross reaction was observed between the antigens of Rps. palustris (1e5, 11/1) and Rps. capsulata, Rps. spheroides, or R. rubrum, respectively. In contrast to 11/1 only heat-killed cells of strain 1e5 were agglutinated by anti-1e5.

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Im Text verwendete Abkürzungen LPS Lipopolysaccharid - R Rhodospirillum - Rps. Rhodopseudomonas - i.m. intramuskulär - s.c. subcutan - i.v. intravenös     

Rhodospirillum salexigens,spec. nov., an obligatory halophilic phototrophic bacterium

The name Rhodospirillum salexigens, spec. nov., was proposed for the strain WS 68, isolated by W. R. Sistrom at the Oregon coast from salt water. The spiral-shaped phototrophically or chemotrophically growing, salt demanding bacterium contains intracytoplasmic membranes arranged parallel to the cytoplasmic membrane. Bacteriochlorophyll a and spirilloxanthin are the major pigments. Growth occurs between 20 and 45°C at a neutral pH. The DNA base composition was 64 mol % guanine plus cytosine. The cell wall contains peptidoglycan and proteins but no glycolipids.     

Characterization of a new membrane-bound cytochrome c of Rhodopseudomonas capsulata

A cytochrome c (cyt. c) was solubilized with Triton-X-100 and co-purified with cytochrome c oxidase from membranes of chemotrophically grown cells of Rhodopseudomonas capsulata. Cyt. c and cytochrome oxidase were separated on Sephadex G-50 columns. Antibodies against cytochrome c2 from the same bacterium did not cross react with the membrane-bound cyt. c. The IEP of the membrane-bound cyt. c was found to be pH 8.2, the midpoint potential was 234 +/- 11 mV at pH 7.0. This cyt. c binds CO. The native cyt. c is a dimer with an apparent Mr of 25000 containing 2 mol heme per mol dimer, which is believed to function as an electron donor for the high-potential cytochrome c oxidase.     

Beiträge zur Cytologie der Blaualgen

Zusammenfassung Mit Hilfe von Ultradünnschnitten wurde die Substruktur von Phormidium frigidum Fritsch, Phormidium retzii Gom., Oscillatoria limosa Ag., Anabaena variabilis Kütz und Cylindrospermum licheniforme Kütz untersucht.Das Chromatoplasma besteht aus submikroskopischen Lamellen, die bei den einzelnen Arten charakteristische Lamellensysteme bilden. Größere Unterschiede in der Ausbildung und Anordnung der Lamellen bestehen zwischen den Vertretern der Oscillatoriaceen und der Nostocaceen.Das Centroplasma läßt auch im submikroskopischen Bereich keine Abgrenzung gegen das Chromatoplasma erkennen. Es ist dadurch gekennzeichnet, daß das Plasma hier kompakter gelagert ist und die für das Chromatoplasma typischen Lamellen fehlen. Das Grundplasma ist körnig und läßt gewisse kettenförmige Strukturen erkennen.     

The transepithelial potential difference in the gills of the fiddler crab,Uca tangeri: Influence of some inhibitors

Summary Euryhaline Crustacea living in dilute media, counterbalance the salt loss by active absorption of NaCl across the gill epithelium. To investigate the mechanisms involved in salt absorption, transeptithelial potential difference (PD_te) was measured in isolated, perfused gills of the fiddler crab,Uca tangeri. The influence of some specific inhibitors of epithelial ion transport on the PD_te was tested.With symmetrical conditions on both sides of the epithelium, the posterior gills ofUca tangeri showed a spontaneous PD_te of +5 to +10 mV, that is an active transport potential which was positive on the bath side as referred to the hemolymph side. This potential decreased considerably after application of KCN or 2,4-dinitrophenol (DNP) to the perfusion saline.Omission of K⁺ from the perfusion saline or addition of ouabain led to a reversible drop of the PD_te, suggesting that the absorption of Na⁺ and also of Cl^– is driven by the (Na⁺+K⁺)ATPase located in the basolateral membrane of the epithelial cells.Perfusion of the hemolymph space with saline containing diphenylamine-2-carboxylate (DPC) or the loop diuretic furosemide resulted in a decrease of the PD_te.After application of amiloride to the bath saline the PD_te increased. Half-maximum response to amiloride was reached at a concentration of about 10^–5 mol·l^–1. This suggests that one of the Na⁺ pathways across the apical membrane may consist of Na⁺ channels.Abbreviations PD _te transepithelial potential difference - DPC diphenylamine-2-carboxylate - R _ps resistance of perfusate shunt - R _te transepithelial resistance - R _in input resistance - DNP 2,4-dinitrophenol Parts of this study have been reported at the 1st Congress of Comparative Physiology and Biochemistry, Liège 1984, and at the Vth European Colloquium on Renal Physiology, Frankfurt, 1985     

Redox-controlled,in vivo and in vitro phosphorylation of the α subunit of the light-harvesting complex I in Rhodobacter capsulatus

Labelling of Rhodobacter capsulatus cells with (³²P)Pi in a phototrophic culture results in phosphorylation of a membrane-bound polypeptide identified as the subunit of the LHI antenna complex of the photosynthetic apparatus. Phosphorylation of the same polypeptide was also observed by incubation of chromatophores with (³²P)ATP or under conditions of photophosphorylation with ADP and (³²P)Pi. The identity of the phosphorylated LHI- subunit was demonstrated by N-terminal protein sequencing of the phosphorylated polypeptide and by failure of labelling in LHI-defective mutants. Pre-aeration of the samples or addition of the oxidant potassium ferrcyanide stimulated the kinase activity whereas the presence of soluble cytoplasmic proteins impaired phosphorylation in an in vitro assay. No effect resulted from addition of reductants to the assay medium. The results indicate the presence of a membrane-bound protein kinase in R. capsulatus that phosphorylates the subunit of the LHI antenna complex under redox control.Abbreviations Pi inorganic phosphate - SDS-PAGE sodium dodecyl-sulfate polyacrylamide gel electrophoresis     

Kinetic studies on formation of cytochrome oxidase of Rhodopseudomonas capsulata after a shift from phototrophic to chemotrophic growth.

Rhodopseudomonas capsulata cells were shifted from phototrophic (anaerobic, light) to chemotrophic (semiaerobic, dark, 10% air saturation) growth conditions. During the adaptation period of 4 h, the bacteriochlorophyll content of cells and membranes decreased, and a newly synthesized 65-kilodalton polypeptide of the cytochrome oxidase was incorporated into the membrane fraction. The enzymatic activity of the cytochrome oxidase increased strongly after a lag time of 2 h. The amount of cytochrome oxidase protein does not follow the same kinetics. The relative amount of a membrane-bound cytochrome c of low molecular weight, which has been proposed to be a donor for the cytochrome oxidase, increased during adaptation.     

Fusion of liposomes and chromatophores of Rhodopseudomonas capsulata: effect on photosynthetic energy transfer between B875 and reaction center complexes.

The photosynthetic chromatophore membranes of Rhodopseudomonas capsulata were fused with liposomes to investigate the effects of lipid dilution on energy transfer between the bacteriochlorophyll-protein complexes of this membrane. Phosphatidylcholine-containing liposomes were mixed with chromatophores at pH 6.0 to 6.2, and the mixture was fractionated on discontinuous sucrose gradients into four membrane fractions with lipid-to-protein ratios that varied 11-fold. Freeze-fracture electron microscopy revealed that the fractions contained closed vesicles formed by the fusion of liposomes to chromatophores. Particles with 9-nm diameters on the P fracture faces did not appear to change in size with increasing lipid content, but the number of particles per membrane area decreased proportionally with increases in the lipid-to-protein ratio. The bacteriochlorophyll-to-protein ratios, electrophoretic polypeptide profiles on sodium dodecyl sulfate-polyacrylamide gels, and light-induced absorbance changes at 595 nm caused by photosynthetic reaction centers were not altered by fusion. The relative fluorescence emission intensities due to the B875 light-harvesting complex increased significantly with increasing lipid content, but no increases in fluorescence due to the B800-B850 light-harvesting complex were observed. Electron transport rates, measured as succinate-cytochrome c reductase activities, decreased with increased lipid content. The results indicate an uncoupling of energy transfer between the B875 light-harvesting and reaction center complexes with lipid dilution of the chromatophore membrane.