The effect of growth temperature on the thermotropic behavior of the membranes of a thermophilic Bacillus. Composition-structure-function relationships

Reizer, Jonathan; Grossowicz, N.; Barenholz, Yechezkel

doi:10.1016/0005-2736(85)90297-4

Cited by 57 publications

(43 citation statements)

References 35 publications

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“…In the two membrane vesicles, the Ap declined with increasing pH from -150 to -160 mV at pH for the two microorganisms resulted in a shift of the thermotropic gel to the liquid-crystalline phase transition temperature. In B. stearothermophilus, the effect of temperature on membrane composition has been studied in great detail (23). It was demonstrated that at various levels alterations occur by variation of the growth temperature.…”

Section: Methodsmentioning

confidence: 99%

“…An increase in phosphatidylglycerol content with a decrease in cardiolipine content occurred at increased growth temperatures. Furthermore, with increasing growth temperatures, a change in the acyl chain composition of all membrane lipids occurred, and a gradual depletion of unsaturated fatty acids, a prominent increase in the iso-anteiso fatty acid ratio, and an increase in the abundance of longer homologs of saturated linear fatty acids were observed (23). The effect of growth temperature on the thermotropic behavior of the membranes in situ can be interpreted as maintenance of the apparent microviscosity (homoviscous adaptation) (23).…”

Section: Methodsmentioning

confidence: 99%

“…Furthermore, with increasing growth temperatures, a change in the acyl chain composition of all membrane lipids occurred, and a gradual depletion of unsaturated fatty acids, a prominent increase in the iso-anteiso fatty acid ratio, and an increase in the abundance of longer homologs of saturated linear fatty acids were observed (23). The effect of growth temperature on the thermotropic behavior of the membranes in situ can be interpreted as maintenance of the apparent microviscosity (homoviscous adaptation) (23). A distinct apparent microviscosity of the membranes of the mesophilic and thermophilic species at their respective growth temperatures appears to be essential, since the apparent microviscosities of the membranes of the two bacteria at their respective growth temperatures are remarkably similar.…”

Section: Methodsmentioning

confidence: 99%

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Comparative study of energy-transducing properties of cytoplasmic membranes from mesophilic and thermophilic Bacillus species

1988

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The properties of enzymes involved in energy transduction from a mesophilic (Bacillus subtilis) and a thermophilic (B. stearothermophilus) bacterium were compared. Membrane preparations of the two organisms contained dehydrogenases for NADH, succinate, L-ac-glycerophosphate, and L-lactate. Maximum NADH and cytochrome c oxidation rates were obtained at the respective growth temperatures of the two bacteria. The enzymes involved in the oxidation reactions in membranes of the thermophilic species were more thermostable than those of the mesophilic species. The apparent microviscosities of the two membrane preparations were studied at different temperatures. At the respective optimal growth temperatures, the apparent microviscosities of the membranes of the two organisms were remarkably similar. The transition from the gel to the liquid-crystalline state occurred at different temperatures in the two species. In the two species, the oxidation of physiological (NADH) and nonphysiological (N,N,N',N'-tetramethyl-p-phenylenediamine or phenazine methosulfate) electron donors led to generation of a proton motive force which varied strongly with temperature. At increasing temperatures, the efficiency of energy transduction declined because of increasing H+ permeability. At the growth temperature, the efficiency of energy transduction was lower in B. stearothermophilus than in the mesophilic species. Extremely high respiratory activities enabled B. stearothermophilus to maintain a high proton motive force at elevated temperatures. The pH dependence of proton motive force generation appeared to be similar in the two membrane preparations. The highest proton motive forces were generated at low external pH, mainly because of a high pH gradient. At increasing external pH, the proton motive force declined.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Comparative study of energy-transducing properties of cytoplasmic membranes from mesophilic and thermophilic Bacillus species

1988

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“…The phospholipid environment in which the enzyme is embedded responds to temperature changes by alterations in its apparent microviscosity [41]. Membranes from B. stearothermophilus grown at 55 "C have a gel-to-liquid-crystalline phase transition in the temperature range 20 -40°C [41]. This phase transition results in drastic changes of the apparent microviscosity of the membrane.…”

Section: Discussionmentioning

confidence: 99%

“…Clearly the phospholipid environment provides no additional protection against thermoinactivation of the enzyme. The phospholipid environment in which the enzyme is embedded responds to temperature changes by alterations in its apparent microviscosity [41]. Membranes from B. stearothermophilus grown at 55 "C have a gel-to-liquid-crystalline phase transition in the temperature range 20 -40°C [41].…”

Section: Discussionmentioning

confidence: 99%

Characterization and application of a thermostable primary transport system: Cytochrome‐C oxidase from Bacillus stearothermophilus

Vrij

Heyne

Konings

1989

European Journal of Biochemistry

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Cytochrome-c oxidase from Bacillus stearothermophilus has been purified to homogeneity by detergent extraction followed by DEAE-cellulose, hydroxyapatite-and gel-filtration chromatography. The enzyme is a typical cytochrome-aa3-type oxidase which binds carbon monoxfde and is sensitive to classical oxidase inhibitors like cyanide and azide. The purified enzyme is composed of three different subunits (57, 37 and 22 kDa). The subunit with intermediate molecular mass contains a covalently attached heme-c moiety. The enzyme appeared to be extremely thermostable (inactivation temperature = 81 "C). Highest turnover rates of the reconstituted enzyme were obtained with Saccharomyces cerevisiae cytochrome c or reduced forms of non-physiological electron donors like N,N,N',N'-tetramethyl-p-phenylenediamine and phenazine methosulphate. The reconstituted enzyme can generate a proton-motive force consisting of a high membrane potential and trans-membrane pH gradient. The high electro-motive force of the enzyme (dp = -180 to -200 mV) indicates that this enzyme functions as a high-capacity electrogenic proton pump.Liposomes containing the purified thermostable and thermoactive cytochrome-c oxidase were fused with membranes from the fermentative bacterium Clostridium acetobutylicurn. In the hybrid system a high protonmotive force can be generated upon oxidation of reduced N,N,N,N'-tetramethyl-p-phenylenediamine by the incorporated oxidase which subsequently can be used to drive secondary transport of amino acids. This demonstrates the applicability of the cytochrome-c oxidase to study solute transport in membranes of fermentative bacteria.Bacterial cytoplasmic membranes are equipped with energy-transducing enzymes, capable of converting redox, chemical or light-energy into electrochemical energy [l -31. The electrochemical energy generated by these enzymes fulfills an essential role in many bioenergetic processes [4].In the past decade several bacterial membrane-bound energy-converting enzymes have been isolated and extensively characterized [5 -171. The structural simplicity of these bacterial enzymes in comparison to their eukaryotic counterparts offers attractive possibilities to study the molecular mechanism(s) of energy transduction. Energy-converting enzymes from thermophilic bacteria possess an additional attractive feature, i. e. their enhanced (therm0)stability [18]. This is especially convenient in the purification and the utilization of these enzymes. Some membrane-bound energy-converting enzymes (cytochrome-c oxidases) from thermophilic bacteria, like Thermus thermophilus HB-8 and Bacillus PS3 have already Correspondence to W . N . Konings, Laboratorium voor Microbiologie, Rijksuniversiteit Groningen, Biologisch Centrum,

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Thermal regulation of phospholipid fluidity in Corynebacterium glutamicum

Hänel¹,

Brezesinski²,

Hilliger³

et al. 1986

J. Basic Microbiol.

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Increasing temperatures of cultivation caused the cellular phospholipid content of C. glutamicum to decrease significantly. Simultaneously, the melting point of phospholipid fractions, i. e. the temperature of the ordered-disordered phase transition, increased. A hypothetical connection between the cellular phospholipid composition and the temperature-depended lysine efflux is discussed.Most bacteria alter their membrane lipid composition, and hence membrane fluidity, in response to changes in growth temperature. These alterations are often in the fatty acyl constituents of phospholipids and glycolipids and include changes in the saturation or length of fatty acyl chains in addition to variations in the proportion of cyclic or branched fatty acids (RUSSEL 1984). Normal cell function requires membrane lipid bilayers to be in a largely fluid state (MENDOZA and &ONAN 1983). However, a t low temperatures, membrane lipid bilayers undergo reversible order-disorder phase transitions as demonstrated by several methods (e. g. differential scanning calorimetry) (LEONARD et aZ. 1981). I n a recent paper concerning the influence of temperature on the lysine formation of C . glutarnicum, we reported on a decrease of the proportion of unsaturated fatty acids in the whole lipid fraction of this microorganism when grown a t increasing temperatures (HILLIGER et at. 1984). Furthermore, it was shown using freeze-fracture electron microscopy that, after quenching of the bacteria from temperatures below their growth temperature, the intramembraneous particles segregate and particle-free smooth areas of different sizes appear. Segregation started a t higher temperatures when C . glutarnicurn was grown a t higher temperatures (RICHTER et al. 1985). Such morphological pertubations may be induced by the order-disorder transitions of the paraffin chains within the hydrophobic core of the membrane (LEONARD et al. 1981). The aim of this work was to demonstrate directly such transitions of the cellular phospholipid fraction as a function of growth temperature by using differential scanning calorimetry (DSC). Materials and methodsStrain and conditions of cultivation: Corynebaeterium glutamicum 9366 resistant to S-2-aminoethyl-L-cysteine and requiring homoserine was grown for 48 h in a mineral salt medium containing (g/l) : sucrose 75, (NH,),S04 30, KH,PO, 2, CaCO, 10, MgSO, -7 H,O 0.3, Peso,. 7 H,O 0.02, MnSO, 0.02, L-methionine 0.5, L-threonine 0.7, thiamine 0.01, biotin 0.0001, pH 7.0. Cultivations were carried out on rotary shakers (180 r.p.m., 5 om-strokes) in 500-ml flasks containing 50 ml medium at various temperatures as indicated.Extraction of lipids and thin-layer chromatography : Extraction of lipids and thin-layer chromatography were performed as described previously (GRHFE et al. 1982). Diphosphatidylglycerol (DPG) and phosphatidylglycerol (PG) were identified through parallel application of commercial samples of the two phospholipids (KOCH-LIGHT Ltd., England). Lipid phosphorus was estimated according to HESSE and GELLER (1965)....

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The effect of growth temperature on the thermotropic behavior of the membranes of a thermophilic Bacillus. Composition-structure-function relationships

Cited by 57 publications

References 35 publications

Comparative study of energy-transducing properties of cytoplasmic membranes from mesophilic and thermophilic Bacillus species

Comparative study of energy-transducing properties of cytoplasmic membranes from mesophilic and thermophilic Bacillus species

Characterization and application of a thermostable primary transport system: Cytochrome‐C oxidase from Bacillus stearothermophilus

Thermal regulation of phospholipid fluidity in Corynebacterium glutamicum

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