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PubMed1980

Electric field promotion of the bacteriorhodopsin BR570 to BR412 photoconversion in films of Halobacterium halobium purple membranes.

The combined action of electric field (105-107 V x m-1) and light (380-580 nm, 80 W x m-2) activating the photoenergetic reaction of bacteriorhodopsin (BR) in dry films of purple membranes from Halobacterium halobium was studied. A new stimulating effect of the field on the BR412 intermediate accumulation in the normal photochromic cycle of BR570 has been observed. The formation of the product BR412 is supposed to be accompanied by specific rearrangements of certain charged, polar and polarizable groups in the BR pigment-protein matrix. Such an intrinsic polarization could be promoted by an external electric field, the displacement vector of those groups being oriented in the direction of the filed. The dielectric polarization properties of the purple membranes have been demonstrated by electret-thermal analysis.

Bacteriorhodopsins↗
PubMed1977

Light-driven sodium transport in sub-bacterial particles of Halobacterium halobium.

Light-induced Na+ efflux was observed in sub-bacterial particles of Halobacterium halobium loaded and suspended in 4 M NaCl solution. The Na+ efflux was not ATP driven, since ATPase inhibitors were without effect or even enhanced efflux at low light intensity. Uncouplers, on the other hand, inhibited Na+ efflux, the inhibition being complete at low light intensity. The Na+ efflux was accompanied by proton influx. Both processes were dependent on light intensity, unaffected or enhanced by ATPase inhibitors and similarly affected by uncouplers. Proton influx was not observed in particles loaded with 4 M KCl instead of 4 M NaCl. Na+ transport in the dark could be induced by artificial formation of a pH difference across the membrane; changing the sign of the pH difference reversed the direction of the Na+ transport. Proton influx in the dark followed the artificial formation of a sodium gradient [Na+]in less than [Na+]out). These results may be explained by a Na+/H+ antiport mechanism. The fluxes of Na+ and H+ were of comparable magnitude, but the initial rate of Cl- efflux in the same experiment was one-third of the initial rate of Na+ efflux. Consequently Cl- is not regarded as a participant in the Na+ efflux mechanism.

Arsenates↗
PubMed1986

Current-voltage characteristics of planar lipid membranes with attached Halobacterium cell-envelope vesicles.

We have studied the photoactivity of a system consisting of large, planar, essentially solvent free bilayers bearing adsorbed cell-envelope vesicles prepared from Halobacterium halobium (strain L 33). The system was made conductive by addition of a proton carrier (SF-6847). We observed photocurrents which were linearly dependent upon transmembrane voltage. Current-voltage curves were found to be well described by an equivalent circuit with the following significant parameters: planar bilayer conductance, planar bilayer-vesicle contact area conductance, cell-envelope vesicle conductance, and chloride pump equivalent voltage-generator potential. These parameters are uniquely obtained as a result of a few independent current measurements. The stationary photovoltage was dependent upon chloride concentration, and from this dependence an active transport (pump) affinity of the system for chloride was calculated to be about 50 mM.

Bacteriorhodopsins↗
PubMed1992

The essential role of specific Halobacterium halobium polar lipids in 2D-array formation of bacteriorhodopsin.

The mechanism whereby bacteriorhodopsin (BR), the light driven proton pump from the purple membrane of Halobacterium halobium, arranges in a 2D-hexagonal array, has been studied in bilayers containing the protein, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and various fractions of H. halobium membrane lipids, by freeze fracture electron microscopy and examination of optical diffractograms of the micrographs obtained. Electron micrographs of BR/DMPC complexes containing the entire polar lipid component of H. halobium cell membranes or the total lipid component of the purple membrane, with a protein-to-total lipid molar ratio of less than 1:50 and to which 4 M NaCl had been added, revealed that trimers of BR formed into an hexagonal 2D-array similar to that found in the native purple membrane, suggesting that one or more types of the purple membrane polar lipids are required for array formation. To support this suggestion, bacteriorhodopsin was purified free of endogenous purple membrane lipids and reconstituted into lipid bilayer complexes by detergent dialysis. The lipids used to form these complexes are 1,2-dimyristoyl-sn-glycerol-phosphocholine (DMPC) as the major lipid and, separately, each of the individual lipid types from the H. halobium cell membranes, namely 2,3-di-O-phytanyl-sn-glycero-1-phosphoryl-3'-sn-glycerol 1'-phosphate (DPhPGP), 2,3-di-O-phytanyl-sn-glycero-1-phosphoryl-3'-sn-glycerol 1'-sulphate (DPhPGS), 2,3-di-O-phytanyl-sn-glycero-1-phosphoryl-3'-sn-glycerol (DPhPG) and 2,3-di-O-phytanyl-1-O-[beta-D-Galp-3-sulphate-(1----6)-alpha-D- Manp-(1----2)-alpha-D-Glcp]-sn-glycerol (DPhGLS). When examined by freeze-fracture electron microscopy, only the complexes containing 2,3-di-O-phytanyl-sn-glycero-1-phosphoryl-3'-sn-glycerol- 1'-phosphate or 2,3-di-O-phytanyl-sn-glycero-1-phosphoryl-3'-sn-glycerol-1'-sulphate, at high protein density (less than 1:50, bacteriorhodopsin/phospholipid, molar ratio) and to which 4 M NaCl had been added, showed well defined 2D hexagonal arrays of bacteriorhodopsin trimers similar to those observed in the purple membrane of H. halobium.

Bacteriorhodopsins↗
PubMed1994

Acylation of proteins of the archaebacteria Halobacterium cutirubrum and Methanobacterium thermoautotrophicum.

Although the membrane lipids of extremely halophilic archaebacteria are exclusively derived from diphytanylglycerol diether, which is non-acylated, small amounts of fatty acids have been detected in these organisms. These fatty acids are formed by the action of a fatty acid synthase (FAS), shown to be present in the extreme halophile Halobacterium cutirubrum, despite the fact that only a fraction of the activity of FAS remains at the high salt concentration (> 4 M) present in the cytoplasm. It has now been demonstrated that fatty acids do not occur in lipid-bound form but largely in the form of acylated proteins in the red membrane of H. cutirubrum. In contrast, the bacteriorhodopsin of the purple membrane of this extreme halophile does not appear to be acylated. The thermophilic methanogen, Methanobacterium thermoautotrophicum had a much higher fatty acid synthase activity than the extreme halophile, and the synthase activity of the methanogen was optimal under its normal (anaerobic) growth conditions. The methanogen also utilized the resulting fatty acids to acylate its membrane proteins. The major fatty acids in both organisms were palmitic and stearic acids with small amounts of myristic and 18:1 acids, and these were bound to protein through both ester and amide linkages.

Acylation↗
PubMed1995

Over-expression of a new photo-active halorhodopsin in Halobacterium salinarium.

The gene of haloopsin (hop) from halobacterial strain shark was cloned and its nucleotide sequence was determined. The deduced amino acid sequence of shark halorhodopsin (HR) showed that its homology with halobium HR was 62%. The gene product seems to be HR having several positively charged residues that are conserved in all known HRs. The gene encoding shark hop as well as that encoding halobium hop were successfully expressed in Halobacterium salinarium (halobium) by using a plasmid shuttle vector containing the bacterioopsin (bop) promoter. The expression level of shark HR is almost the same as that for halobium HR with the same shuttle vector containing the bop promoter. Under the physiological conditions, the anion pumping activity of the shark HR expressed in H. salinarium was almost the same as that for halobium HR; however, the anion selectivity and half-maximal anion transport were different. Furthermore, its absorption maximum in the absence of chloride shifted to approx. 596 nm in contrast to that for halobium HR. The half-lifetimes of HR520 formation for shark HR and halobium HR were almost the same; however, the half-lifetime of its decay was approx. 6-times faster for shark HR than it was for halobium HR at a high chloride concentration (1000 mM). Even at a low chloride concentration (50 mM), HR520 and HR640 intermediates could be detected for shark HR, and the half-lifetime of HR640 decay was found to be approx. 25 ms. In the presence of nitrate, the half-lifetime of HR565 recovery for shark HR was approx. 10-times slower than that for halobium HR. Some of amino acid substitutions between shark HR and halobium HR may affect the anion selectivity and the photoreaction of HR.

Amino Acid Sequence↗
PubMed1979

Purification and properties of alanine dehydrogenase from Halobacterium salinarium.

1. L-Alanine dehydrogenase (L-alanine:NAD+ oxidoreductase (deaminating), EC 1.4.1.1) was purified about 500-fold from Halobacterium salinarium. 2. The enzyme appears to be homogeneous in polyacrylamide gel electrophoresis. The apparent molecular weight is about 60 000. 3. Activity and stability of the enzyme are largely affected by different salts. Full activity of the NADH-dependent reductive amination of pyruvate occurs at 4.3 M NaCl. This activation can be achieved also by KCl and several other salts instead of NaCl. 4. The NAD+-dependent oxidative deamination of L-alanine occurs only in the presence of high concentrations of KCl. This reaction is not stimulated by NaCl. The Km values for the substrates NADH, pyruvate and NH+4 are also salt dependent. 5. The thermal stability of the enzyme is considerably higher in the presence of high concentrations of NaCl than in the presence of KCl. 6. The enzyme is completely inactivated by the removal of salt. Full reactivation is achieved by addition of salt in the presence of 2-mercaptoethanol. Inactivation proceeds about ten times faster than reactivation. The inactivation after the withdrawal of salt and the reactivation following the readdition of salt show a characteristic hysteresis loop.

Alanine↗
PubMed1975

Isolation and characterization of C50-carotenoid pigments and other polar isoprenoids from Halobacterium cutirubrum.

The polar acetone-soluble lipids of Halobacterium cutirubrum were found to contain (in addition to the previously reported vitamin MK-8 and retinal) neo-bacterioruberin U, bacterioruberin, monoanhydrobacterioruberin, bis-anhydrobacterioruberin, an isomer of geranylgeraniol (with one internal cis-isoprene residue), 2,3,-di-O-phytanyl-sn-glycerol and two unidentified polar isoprenoids. All compounds were isolated in pure form by column and thin-layer chromatography, quantitated and characterized by their visible, ultraviolet, infrared, proton magnetic resonance and mass spectra and the spectra of their acetyl or silyl derivatives and/or dehydrated products.

Carotenoids↗
PubMed1993

The glycolipid of Halobacterium trapanicum.

The structural elucidation of the polar lipids in Halobacterium trapanicum is reported with particular emphasis on a new sulfated disaccharide derivative of 2,3-di-O-phytanyl-sn-glycerol. The full structural designation of this glycolipid is 2,3-di-O-phytanyl-1-O- (mannopyranosyl-(2-sulfate)-alpha-D-1-2-glucopyranosyl-alpha-D)-sn-glyce rol. The value of glycolipid structures in the taxonomy of halophilic Archaea is also discussed.

Carbohydrate Sequence↗
PubMed1976

Thermal denaturation and photochemistry of bacteriorhodopsin from Halobacterium cutirubrum as monitored by resonance Raman spectroscopy.

Resonance Raman studies of the thermal denaturation of bacteriorhodopsin from Halobacterium cutirubrum show that the N-retinylidenelysine moiety present in the chromophore is N-protonated. This corroborates an earlier suggestion of Lewis et al. ((1974) Proc. Natl. Acad. Sci. U.S., 71, 4462-4466). The widely differing excitation profiles of two -C=C- stretching modes are explained in terms of the light-initiated reaction cycle in the molecule. Glutaraldehyde fixation of bacteriorhodopsin has no effect on the intensity ratio of the two modes, suggesting that no large motion of the protein is necessary for the photoreaction cycle to occur.

Bacteriorhodopsins↗
PubMed1980

Sequence homologies in the N-terminal region of the ribosomal 'A' proteins from Methanobacterium Thermoautotrophicum and Halobacterium cutirubrum.

The ribosomal 'A' protein from the methanogen, Methanobacterium thermoautotrophicum, has been isolated and purified. The amino acid composition and mobility on two-dimensional gels indicates that this protein shows characteristics similar to the equivalent protein from the extreme halophile, Halobacterium cutirubrum, and is significantly different from the equivalent protein from other bacteria. The first 48 residues of the methanogenic 'A' protein were sequenced and showed a large amount of sequence homology to the H. cutirubrum 'A' protein. When the sequences of these two proteins were compared to the 'A' protein from other procaryotes (eubacteria), much less homology was evident. These results support the hypothesis (Woese, C.R. and Fox, G.F., (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5088-5090) of two procaryotic lines of evolutionary descent, the eubacteria and the archaebacteria, the latter including the methanogens and the extreme halophiles. The sequence data from the 'A' proteins also indicate that, phylogenetically, the archaebacteria are much closer to the cytoplasmic components of eucaryotes than they are to the eubacteria (or 'true bacteria').

Amino Acid Sequence↗
PubMed1981

Isoelectric forms of bacteriorhodopsin from Halobacterium halobium.

Isoelectric focusing was performed on bacteiorhodopsin isolated from Halobacterium halobium, R1 strain, solubilized in Nonidet P-40, on sucrose density gradient stabilized columns. When 560 nm absorbance was monitored, four forms of bacteriorhodopsin were observed, having isoelectric points (pI) of: A. 3.93; B, 4.43; C, 5.03; D, 5.49. Instability of some of the isoelectric forms during the very process of electrofocusing was observed. When focused over a period of 6 days, the relative abundance of the forms changed although their pI values remains constant. Refocusing of the isolated forms A or B led to the production f form C. The latter species was stable to refocusing. Form B was unstable to storage either as an aqueous suspension of the purple membrane or as a detergent extract. Each of the forms had the absorption spectrum typical for bacteriorhodopsin and each showed identical patterns after sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

Bacteriorhodopsins↗
PubMed1990

Solubilization and functional reconstitution of the DCCD-sensitive Na+/H(+)-antiporter from Halobacterium halobium.

Na+/H+ exchange activity was solubilized from Halobacterium halobium with octyl-beta-D-glucoside (OG) and was reconstituted into the bacterio-rhodopsin incorporated liposomes (BR-liposomes) by the detergent-dialysis method. Light illumination stimulated uphill 22Na+ uptake into the reconstituted conjugate proteoliposomes. The 22Na+ uptake was FCCP-sensitive and was dependent on the amounts of OG-extract applied. On the other hand, the proteoliposomes reconstituted with the membrane fraction pretreated with N,N'-dicyclohexylcarbodiimide (DCCD) did not exhibit the light-dependent 22Na+ uptake, thus, DCCD-sensitive. When the reconstituted proteoliposome was incubated with [14C]DCCD, radio-labels appeared slightly on 50K but mainly on 11K-Dalton component, which are the same components labeled in the intact membrane vesicles. It is concluded that halobacterial DCCD-sensitive Na+/H(+)-antiporter was solubilized and reconstituted in the conjugate BR-liposomes with preserved functional unit.

Bacteriorhodopsins↗
PubMed1987

Primary structures of three highly acidic ribosomal proteins S6, S12 and S15 from the archaebacterium Halobacterium marismortui.

The amino acid sequences of three extremely acidic ribosomal proteins, S6, S12, and S15, from Halobacterium marismortui have been determined. The sequences were obtained by the sequence analysis of peptides derived by enzymatic digestion with trypsin. Stapylococcus aureus protease and chymotrypsin, as well as by cleavage with dilute HCl. The proteins, S6, S12 and S15, consist of 116, 147 and 102 amino acid residues, and have molecular masses of 12,251, 16,440 and 11,747 Da, respectively. Comparison of the amino acid sequences of these proteins with ribosomal protein sequences of other organisms revealed that halobacterial protein S12 has homology with the eukaryotic protein S16A from Saccharomyces cerevisiae, while S15 is significantly related to the Xenopus laevis S19 protein. No homology was found between these halobacterial proteins and any eubacterial ribosomal proteins.

Amino Acid Sequence↗
PubMed1988

Amino acid sequences of ribosomal proteins S11 from Bacillus stearothermophilus and S19 from Halobacterium marismortui. Comparison of the ribosomal protein S11 family.

The complete amino acid sequences of ribosomal proteins S11 from the Gram-positive eubacterium Bacillus stearothermophilus and of S19 from the archaebacterium Halobacterium marismortui have been determined. A search for homologous sequences of these proteins revealed that they belong to the ribosomal protein S11 family. Homologous proteins have previously been sequenced from Escherichia coli as well as from chloroplast, yeast and mammalian ribosomes. A pairwise comparison of the amino acid sequences showed that Bacillus protein S11 shares 68% identical residues with S11 from Escherichia coli and a slightly lower homology (52%) with the homologous chloroplast protein. The halophilic protein S19 is more related to the eukaryotic (45-49%) than to the eubacterial counterparts (35%).

Amino Acid Sequence↗
PubMed1988

The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui.

The complete amino acid sequences of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui were determined. The sequences were established by manual sequencing of peptides produced with several proteases as well as by cleavage with dilute HCl. Proteins L16, L23 and L33 consist of 119, 154 and 69 amino acid residues, and their molecular masses are 13,538, 16,812 and 7620 Da, respectively. The comparison of their sequences with those of ribosomal proteins from other organisms revealed that L23 and L33 are related to eubacterial ribosomal proteins from Escherichia coli and Bacillus stearothermophilus, while protein L16 was found to be homologous to a eukaryotic ribosomal protein from yeast. These results provide information about the special phylogenetic position of archaebacteria.

Amino Acid Sequence↗