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PubMed1988

Stimulation of an alpha like DNA polymerase by v-myc related protein of Halobacterium halobium.

Partial DNA sequencing of a genomic clone of the archaebacterium Halobacterium halobium, which hybridized with an avian v-myc probe, showed especially the presence, in the organism of one of the conserved regions through myb, myc and adenovirus E1a oncogenes. The archaebacterial deduced amino acid sequence displayed significant homology with the v-myc gene product. In accordance with the partial DNA sequencing which assured a sufficient homology to have similar epitopes, a protein having a molecular weight of 70,000 and possessing high antigenicity with a polyclonal antiserum against avian v-myc protein was isolated and purified from H. halobium extracts. The purified v-myc like protein stimulated in vitro DNA synthesis carried out by the alpha like DNA polymerase of H. halobium.

Amino Acid Sequence↗
PubMed1980

Photosensory retinal pigments in Halobacterium halobium.

In Halobacterium halobium, nicotine is known to block the synthesis of retinal. Cells grown in the presence of nicotine do not show any photophobic response. Addition of retinal1 or retinal2 restored the photophobic responses to light-increase in the UV and to light-decrease in the green-yellow part of the spectrum. The action spectra of the two retinal2-photosystems were red-shifted by 15--20 nm, compared with the corresponding retinal1 systems. We conclude that each of the two photosystems PS 370 and PS 565, has its own photosensory pigment with retinal as the chromophoric group.

Animals↗
PubMed1989

Motor responses of Halobacterium halobrium to sinusodial light stimuli.

Sinusoidal light stimuli have been used to elicit photoresponses in Halobacterium halobium at various periods of the stimulus. Cycle histograms and histograms of the times between consecutive reversals are used to illustrate the responses, and the method used to obtain sinusoidally modulated intense light (with periods up to 1 s) is described.

Cell Movement↗
PubMed1978

Non-aerated cultivation of Halobacterium cutirubrum and its effect on cellular squalenes.

Halobacterium cutirubrum was successfully cultivated under aerobic and microaerobic conditions. The early stationary phase of growth was obtained at 2.2 days and 45--55 days for aerated and non-aerated cultures, respectively. The dry cell yields were 0.7--1.2 gm/1 in all preparations grown to early stationary growth phase. The cellular ratio of squalene to dihydro- and tetra-hydrosqualene decreased proportionately with decreased aeration rates.

Anaerobiosis↗
PubMed1976

Regulation of cell volume and ion concentrations in a Halobacterium.

Changes in cell volume and ion content of a Halobacterium species are described in terms of the NaCl concentration (0.5--3.5M) and pH(4-8) of the suspending medium. Cell volume, per unit content of protein of bacteria in stationary phase cultures, rose as the [NaCl] of the growth medium was increased. Logarithmic-phase bacteria shrank as the pH fell from 7 to 5.5. These changes are characteristic of bacteria with a moderate or rapid rate of O2 consumption. Starving (i.e. nonmetabolizing) bacteria, on the other hand, did not change in size within the above ranges of [NaCl] and pH. At lower values, however, such bacteria swelled and eventually lysed. Effects of low pH on cell ions are compared in metabolizing and starving bacteria, and it is shown that changes in the state of the cell K are correlated with movements of cell Na. It appears that the cell K is used to maintain cell [Na] below the NaCl concentration of the medium. The results are explained in terms of a model involving interactions between polyelectrolytes, salts and water in the concentrated cytoplasm of these halophilic organisms.

Bacterial Proteins↗
PubMed1995

Unfolding of tertiary structure of Halobacterium halobium flagellins does not result in flagella destruction.

The structure of Halobacterium halobium R1M1 flagella is investigated by the methods of scanning microcalorimetry, circular dichroism, and electron microscopy. It is shown that melting curves of flagella in solutions with a different concentration of NaCl display only one peak of heat capacity that corresponds to one cooperatively melting domain. It is found that flagella do not dissociate after melting. The possible structural organization of archaebacterial flagella is discussed.

Amino Acid Sequence↗
PubMed1993

Identification and analysis of the gas vesicle gene cluster on an unstable plasmid of Halobacterium halobium.

In our efforts to elucidate the mechanism of high-frequency mutation of Halobacterium halobium to a gas vesicle deficient state, we discovered insertions, deletions, inversions, and complex DNA rearrangements associated with a large endogenous plasmid, pNRC100. The rearrangements are mostly IS element-mediated, and when they occur in a region of pNCRC100 containing a cluster of thirteen genes, gas vesicle mutants result. We have characterized the structure and expression of this gas vesicle protein (gvp) gene cluster and demonstrated its requirement for gas vesicle synthesis and cell flotation by genetic transformation.

Archaeal Proteins↗
PubMed1998

A 71-kDa protein from Halobacterium salinarium belongs to a ubiquitous P-loop ATPase superfamily with head-rod-tail structure.

The nucleotide sequence of a genomic fragment from Halobacterium salinarium containing an open reading frame encoding a protein with a calculated molecular mass of 71 kDa was determined. Database searches revealed that this protein, Hp71, has similarities to eukaryotic cytoskeletal proteins. Heterologous production of Hp71 in Escherichia coli allowed the isolation of anti-Hp71 antibodies. The antibodies were used (1) to verify the production of Hp71 in H. salinarium and (2) to determine its cytoplasmic localization by immune electron microscopy. Homologous overproduction of Hp71 in H. salinarium and heterologous production in Haloferax volcanii resulted in modifications of cell morphology from rods to extended rods, and from pleiomorphic cells to rods, respectively. Structure prediction methods indicated that Hp71 has a head-rod-tail configuration, including an N-terminal domain with a nucleotide binding motif (P-loop), and an extended discontinuous coiled-coil domain of 330 amino acids. To identify related proteins, the complete genomes of Haemophilus influenzae, Mycoplasma genitalium, and Methanococcus jannaschii were searched for deduced proteins with extended coiled-coil domains. Only one or two proteins were found for each organism, showing that Hp71 is one of only a few prokaryotic intracellular proteins with extended coiled-coil domains. The phenotype upon overproduction and the similarity of Hp71 to the SMC superfamily of P-loop head-rod-tail proteins (named after SMC1, which is involved in the "stability of minichromosomes" in yeast) indicate that Hp71 might be involved in cytoskeleton formation and/or chromosome partitioning in H. salinarium.

Adenosine Triphosphatases↗
PubMed2002

Increased stability of malate dehydrogenase from Halobacterium salinarum at low salt concentration in reverse micelles.

The stability of malate dehydrogenase (hMDH) from Halobacterium salinarum in aqueous medium at low salt concentrations (1 and 0.5 M NaCl) was studied at 4 degrees and 25 degrees C. The results showed that hMDH was more stable at the higher salt concentration and the low temperature. hMDH was introduced into reverse micelles of hexadecyltrimethylammonium bromide in cyclohexane with 1-butanol as co-surfactant. The hMDH stability in this system was studied at two omega(0) ([H(2)O]/[surfactant]) values and the effects of salt concentration, presence of substrate and dilution before or after its introduction into reverse micelles were examined. The results showed that the half-life of hMDH dissolved in buffer with 1 M NaCl was 12-50 days in reverse micelles (depending on the various conditions), in contrast to only about 1 day in aqueous medium at 25 degrees C. These observations indicate that reverse micelles provide a microenvironment that allows a much greater stability of this enzyme compared with an aqueous medium.

1-Butanol↗
PubMed2003

Purification and biological characterization of halocin C8, a novel peptide antibiotic from Halobacterium strain AS7092.

Halocins are bacteriocin-like proteins or peptides produced by many species of the family Halobacteriaceae. Halocin C8, excreted by the Halobacterium strain AS7092, is a single 6.3-kDa polypeptide with an isoelectric point of 4.4, which is sensitive to proteinase K but not to trypsin. Halocin C8 is quite stable, as it can be desalted, boiled, frozen, subjected to organic solvents, and stored in culture supernatant at 4 degrees C or in dH(2)O at -20 degrees C for more than 1 year without losing activity. The purification of this halocin was achieved by combination of tangential flow filtration (TFF), Sephadex G50 and DEAE-sepharose chromatography. The N-terminal amino acid sequence was also determined by Edman degradation. Halocin C8 appeared to have a very wide activity spectrum, including most haloarchaea and even some haloalkaliphilic rods. When a sensitive strain of Halorubrum saccharovorum was exposed to halocin C8, the treated cells swelled at the initial stage, the cell wall appeared to be nicked and the cytoplasm was then extruded out, and the whole cell was eventually completely lysed. These results indicate that halocin C8 is a novel microhalocin and its primary target might be located in the cell wall of the sensitive cells.

Amino Acid Sequence↗
PubMed1998

Kreb's TCA cycle in Halobacterium salinarum investigated by 13C nuclear magnetic resonance spectroscopy.

Kreb's tricarboxylic (TCA) cycle was studied in Halobacterium salinarum cells grown in the presence of glucose or alanine. The cells were incubated with 13C-labeled substrate and the labeling pattern of various carbon positions in glutamate was monitored by 13C-NMR spectroscopy. [2-13C]pyruvate, when used as a substrate, led mainly to signals for C-1 and C-5 glutamate, with some C-3 glutamate. [3-13C]pyruvate as a substrate produced signals, mainly C-2, C-3, and C-4 glutamate, with some C-1 and C-5 glutamate. The multiplicity of the signals and observation of a C-1 signal in this case indicates extensive cycling of the label in the TCA cycle. Isotopomer analysis of glutamate labeling suggested that of the total pyruvate entering the TCA cycle, the flux through pyruvate:ferredoxin oxidoreductase was 90% while that through pyruvate carboxylase was 10%. Only 53% of the total acetyl-CoA was produced from the added labeled pyruvate, the rest being generated endogenously. In the presence of nitrogen, mainly transamination reaction products were formed in the case of both these substrates.

Alanine↗
PubMed2000

Archaeal promoter-directed expression of the Halobacterium salinarum catalase-peroxidase gene.

The Halobacterium salinarum catalase-peroxidase gene was subcloned into shuttle vectors pWL102 and pWL202 and expressed under the control of different archaeal promoters. When Hbt. salinarum was transformed with the catalase-peroxidase gene under the control of its own promoter, catalase-peroxidase activity increased twofold. Catalase-peroxidase activity increased threefold when Hbt. salinarum was transformed with the catalase-peroxidase gene under the control of a tRNA promoter. This bifunctional enzyme in Hbt. salinarum was not induced by environmental stresses such as H2O2, intense light, darkness, high temperature, low temperature, redox inhibitors, heavy metals, or ions.

Base Sequence↗
PubMed2001

Isolation of the fibrocrystalline body, a structure present in haloarchaeal species, from Halobacterium salinarum.

An organized structure, the fibrocrystalline body (FB), has been isolated from the archaeon Halobacterium salinarum. The structure is also present in, and can be isolated from, other extreme halophilic archaea. FB is present in the cytoplasm during the exponential growth and early stationary phases. This structure is affected by vincristine, an antitumoral drug, which targets tubulin. The drug causes fragmentation of the FB, changes in the cell shape, and growth inhibition. Taken together, these results point toward an important role in the life of the cell for this highly organized structure.

Archaea↗
PubMed2006

Expression and regulation pattern of ferritin-like DpsA in the archaeon Halobacterium salinarum.

Very recently, an iron-rich protein, DpsA, was isolated from the extreme halophilic euryarchaeon Halobacterium salinarum JW5 and characterized. The amino acid sequence of DpsA is related to Dps proteins which belong structurally to the ferritin superfamily but differ from ferritins in their function and regulation. Employing Northern and Western blot analysis, the expression of DpsA in H. salinarum was examined throughout all growth phases and under a variety of growth conditions (iron deficiency, iron supplied growth, oxidative stress). DpsA shows increasing expression of dpsA mRNA in iron rich media and under conditions of oxidative stress (H2O2), whereas under iron deficient conditions mRNA-levels decrease. This is in contrast to Dps-type proteins the transcription of which is induced under conditions of iron starvation. Northern blot experiments show that the expression pattern of halobacterial DpsA is the same as that found in the few bacterial non-heme ferritin the expression pattern of which has been analyzed so far. Based on Western-blot analysis post-transcriptional regulation, typical of mammalian ferritins, can be excluded. This protein exhibits features of a non-heme type bacterial ferritin although it shares only little sequence similarity with Ftn from E. coli.

Amino Acid Sequence↗
PubMed2005

Expression and regulation pattern of ferritin-like DpsA in the archaeon Halobacterium Salinarum.

Very recently, an iron-rich protein, DpsA, was isolated from the extreme halophilic euryarchaeon Halobacterium salinarum JW5 and characterized. The amino acid sequence of DpsA is related to Dps proteins which belong structurally to the ferritin superfamily but differ from ferritins in their function and regulation. Employing Northern and Western blot analysis, the expression of DpsA in H. salinarum was examined throughout all growth phases and under a variety of growth conditions (iron deficiency, iron supplied growth, oxidative stress). DpsA shows increasing expression of dpsA mRNA in iron-rich media and under conditions of oxidative stress (H(2)O(2)), whereas under iron-deficient conditions mRNA-levels decrease. This is in contrast to Dps-type proteins the transcription of which is induced under conditions of iron starvation. Northern blot experiments show that the expression pattern of halobacterial DpsA is the same as that found in the few bacterial non-heme ferritin the expression pattern of which has been analyzed so far. Based on Western-blot analysis post-transcriptional regulation, typical of mammalian ferritins, can be excluded. This protein exhibits features of a non-heme type bacterial ferritin although it shares only little sequence similarity with Ftn from E. coli.

Amino Acid Sequence↗
PubMed1986

Isolation of ribosomal subunits from an extremely halophilic archaebacterium Halobacterium halobium by hydrophobic interaction chromatography.

A new method was developed for a simple, rapid, and effective preparation of ribosomal subunits from the extremely halophilic archaebacterium Halobacterium halobium using hydrophobic interaction chromatography on phenyl-Sepharose CL-4B. One milliliter of swollen gel matrix (total bed volume) bound up to 15 A260 units of 70 S ribosomes. By a stepwise reduction of the ionic strength first 50 S and then 30 S subunits were solubilized and differentially eluted. The pooled fractions containing 50 S and 30 S subunits, respectively, were adjusted to higher ionic strength and concentrated by ultrafiltration. The yield of purified (30 S + 50 S) subunits was up to 60% of the input of 70 S ribosomes. Poly(U)-dependent polyphenylalanine synthesis assay demonstrated that the subunits were as active as native 70 S ribosomes. 30 S and 50 S subunits of nonhalophilic Escherichia coli, however, were not isolated separately by the application of this method.

Cell Fractionation↗
PubMed1984

Partial purification and reconstitution of the aspartate transport system from Halobacterium halobium.

Membrane vesicles of Halobacterium halobium R1Wrm bind to an aspartic acid-agarose affinity column. After disruption of the bound vesicles by low ionic strength, a protein fraction is eluted from the column with 2.5% cholate in 3 M NaCl. When this fraction is reconstituted with soybean lipids to form proteoliposomes, the proteoliposomes exhibit active aspartate accumulation. Aspartate transport in the reconstituted system is driven by a chemical sodium gradient (out greater than in), exhibits sensitivity to an electrical potential, and is specific for L-aspartate. These characteristics are consistent with observations on aspartate transport in intact membrane vesicles of H. halobium. Initial aspartate transport rates in the reconstituted system are about ninefold enhanced over the native system. The system developed should be useful in future purification schemes and studies of the molecular details of membrane transport.

Aspartic Acid↗