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PubMed1989

Ribosomal protein gene cluster of Halobacterium halobium: nucleotide sequence of the genes coding for S3 and L29 equivalent ribosomal proteins.

A 1643 base pair fragment encoding the S3 and L29 equivalent ribosomal proteins has been sequenced from the archaebacterium Halobacterium halobium. The incomplete open reading frame present upstream from the S3 gene encodes a protein homologous to the eubacterial ribosomal protein L22. The initiation codons of the S3 and L29 genes overlap with the termination codons of the upstream genes. A tight physical organization suggests that these genes are transcribed as a polycistronic operon. Peculiarities of the protein structure and gene organization are discussed.

Amino Acid Sequence↗
PubMed1989

Unusual nucleotide sequence heterogeneity of small multicopy pHSB plasmid from Halobacterium strain SB3, an archaebacterium.

A small multicopy plasmid, pHSB, from the Halobacterium strain SB3 is present in the cell as a population of molecules differing from each other by one or several point nucleotide substitutions. At least three sequence versions of the plasmid coexist in the cell. The pHSB primary structure heterogeneity may be a reflection of high genetic instability of the host organism.

Archaea↗
PubMed1989

Expression and regulation of Halobacterium halobium phage phi H genes.

In this paper we describe five distinct modes of phi H gene expression: (i) transcription of phage phi H during lytic growth on the sensitive host bacterium (Halobacterium halobium strain R1); (ii) transcription of the circularized prophage phi H1 in strain R(1)24; (iii) transcription of the L region of phi H present as 12-kilobase-plasmid in the immune strain R1L; (iv) transcription during the lytic growth of phage mutants containing an ISH23/50 in the immune strain R1L; (v) transcription during lytic growth of ISH23/50-insertion mutants in the sensitive host bacterium R1 showing enhancement of early transcripts. The sequential expression of the phage genome is described together with a detailed analysis of the transcription of early lytic, constitutive, and immune genes that map in the L region. The putative promoter sequences determined for several phage genes were compared with the upstream sequences of the H. halobium DNA-dependent RNA polymerase large subunit genes and with the gene for the ribosomal protein S12 homolog of H. halobium. The similarity of these putative promoter elements revealed conserved motifs that are discussed in relation to the TATA-box motif recognized by the eukaryotic DNA-dependent RNA polymerase II.

Bacteriophages↗
PubMed1989

Presence of an intron in elongator methionine-tRNA of Halobacterium volcanii.

The gene for the elongator (internal) methionine transfer RNA (tRNA(mMet)) in the archaebacterium Halobacterium volcanii contains a 75 base pair intron (intervening sequence) and lacks the 3'-terminal CCA sequence of the mature tRNA. There is a single copy of this gene in the genome and it is expressed. Northern hybridization experiments indicate that the precursor is processed to produce mature tRNA and a free intron species. A secondary structure of the transcript can be formed in which the anticodon stem of the tRNA is extended. Two symmetrically placed three-base bulge loops separated by a 4 base pair stem are present in this extension. The cleavage sites for the removal of the intron are placed between the middle and 3' residues of these loops.

Base Sequence↗
PubMed1975

Characterization and composition of the purple and red membrane from Halobacterium cutirubrum;.

The purple membrance (bacteriorhodopsin) isolated from cells of Halobacterium cutirubrum grown anaerobically in the light was shown to contain 77% protein and 20% lipils by weight. The protein component consisted of a single protein moeity, having a molecular weight of (19.6 plus or minus 0.8) times 10-3, complexed with retinal in mole ratio of 2:1, respectively. The protein moeity is not glycosylated but may be phosphorylated (ca. 2 mol of phosphate per mole of protein). The red membrance contains 56%protein and 38% lipids, including bacterioruberins. Several polypeptide components are present including some which may be glycosylated and/or phosphorylated. The lipids of both membranes contained phosphatidyl glycerophosphate (52%) and phosphatidyl glycerol (3-4%) but the sulfated lipid components, glycolipid sulfate and phosphatidyl glycerosulfate, were present exclusively in the purple membrane, the red membrane containing instead two unidentified glycolipids. Neutral lipids (squalenes, vitamin 75-8, etc.) were present in both membranes to the extent of 7-9%.

Amino Acids↗
PubMed1975

Carboxyl-terminal sequences of procaryotic ribosomal proteins from Escherichia coli, Bacillus stearothermophilus, and Halobacterium cutirubrum.

The carboxyl-terminal amino acid sequences of two ribosomal proteins, Escherichia coli L12 and E. coli S4, and the proteins believed to be their equivalents from Bacillus stearothermophilus and Halobacterium cutirubrum, were determined. These proteins are known to be required for peptide chain termination (L12) and in ribosome assembly (S4). The carboxyl-terminal sequences obtained suggest that the E. coli and B. stearothermophilus proteins have retained structural homology in this region, whereas the H. cutirubrum proteins have not.

Amino Acid Sequence↗
PubMed1975

The conservation of amino acids in the n-terminal position of ribosomal and cytosol proteins from Escherichia coli, Bacillus stearothermophilus, and Halobacterium cutirubrum.

Alanine, methionine, and serine are the predominant N-terminal residues in the cytosol and ribosomal protein fractions from the thermophile Bacillus stear othermophilus and the extreme halophile Halobacterium cutirubrum, a similar situation to that previously found in Escherichia coli. In all three bacteria the N-terminal residues of the 30S ribosomal proteins are mainly alanine greater than methionine greater than serine whereas in the 50S ribosomal proteins from E. coli and B. stearothermophilus the predominant residues are methionine greater than alanine greater than serine suggesting conservation of specific N-terminal residues in these ribosomal proteins. However, the 50S ribosomal proteins from H. cutirubrum showed serine as the major N-terminal residue.

Amino Acid Sequence↗
PubMed1976

Enzymatic synthesis of C40 carotenes by cell-free preparation from Halobacterium cutirubrum.

[14C]Mevalonate or (14C)isopentenyl pyrophosphate was found to be converted to transphytoene, trans-phytofluene, lycopene, and beta-carotene by a cell-free 270 000 X g supernatant fraction prepared from Halobacterium cutirubrum cells that were broken by manual grinding with glass beads. Incubations were done under N2 in the dark at 37 degrees C in 4 M NaCl in presence of FAD, NADP, and MgCl2; ATP was also added when mevalonate was the substrate. This system was also capable of converting trans-(14C)phytoene to beta-carotene via the intermediates trans-phytofluene, zeta-carotene, neurosporene, lycopene, and gamma-carotene. Each of these labelled intermediates on incubation separately with the same enzyme system was shown to be converted to the intermediates farther down the pathway. The results of this study show that the biosynthetic pathway for the formation of C40 carotenes in H. cutirubrum proceeds as follows: isopentenyl pyrophosphate leads to trans-phytoene leads to trans-phytofluene leads to zeta-carotene leads to neurosporene leads to lycopene leads to gamma-carotene leads to beta-carotene. This pathway differs from that in higher plants in that the cis isomers of phytoene and phytofluene are not on the main pathway of carotene biosynthesis, as they are in higher plants. Furthermore, trans-phytoene, which has not been reported to have any role in higher plants, appears to be the main intermediate in carotene biosynthesis in H. cutirubrum.

Carotenoids↗
PubMed1976

Effect of nicotine on biosynthesis of C50 carotenoids in Halobacterium cutirubrum.

The major carotenoids in pigmented extreme halophiles are the hydroxylated C50 red pigments bacterioruberin (major, 84%) and monoanhydrobacterioruberin (minor, 14%). When cells of Halobacterium cutirubrum were grown in the presence of nicotine they accumulated lycopene and bisanhydrobacterioruberin; maximal accumulation (80% lycopene, 20% bisanhydrobacterioruberin) occurred at 3mM nicotine. Removal of nicotine resulted in the reformation of monoanhydrobacterioruberin and bacterioruberin at the expense of lycopene and bisanhydrobacterioruberin. Thus nicotine does not inhibit the addition of the two extra isoprene units plus two hydroxyl groups (at C1 and C1') to a C40 carotenoid skeleton. It does, however, inhibit the hydration steps at C3'' and C3''' that convert bisanhydrobacterioruberin to monoanhydrobacterioruberin and finally bacterioruberin. These results support the view that the C50 carotenoids can be formed from a C40 carotene, lycopene.

Carotenoids↗
PubMed1980

Evolutionary relationship between Halobacterium cutirubrum and eukaryotes determined by use of aminoacyl-tRNA synthetases as phylogenetic probes.

The cross-species reactivities between tRNAs and aminoacyl-tRNA synthetases have been employed as a basis to estimate the relatedness of various prokaryotes to the eukaryotes. The tRNA of Halobacterium cutirubrum, unlike that of other prokaryotes tested, including Agrobacterium tumefaciens, Arthrobacter luteus, Bacillus subtilis, Bacillus stearothermophilus, Escherichia coli, Micrococcus luteus, Myxococcus xanthus, Rhodopseudomonas spheroides, and Thermus aquaticus, was found to share with yeast, rat liver, and wheat germ tRNA a distinct preference for aminoacylation by eukaryotic synthetases from yeast as opposed to prokaryotic synthetases from either E. coli or R. spheroides. These results suggest that phylogenetically H. cutirubrum is more closely related to the eukaryotes than to the eubacteria.

Amino Acyl-tRNA Synthetases↗
PubMed1982

A calorimetric study of the thermal transitions of Halobacterium cutirubrum.

The thermal transitions of Halobacterium cutirubrum have been examined by differential scanning calorimetry. Two distinct peaks corresponding to the denaturation of two major protein components were observed in the heating curves. One of the peaks has been assigned to the denaturation of the envelope glycoprotein. The variations of the denaturation temperatures with the addition of glucose, glycerol, NaNO3, and NaSCN are consistent with the previous proposal that hydrophobic interactions are essential in stabilizing the glycoprotein.

Calorimetry, Differential Scanning↗
PubMed1984

Purification, properties, and N-terminal amino acid sequence of certain 50S ribosomal subunit proteins from the archaebacterium Halobacterium cutirubrum.

Sixteen ribosomal proteins (r-proteins) from the 50S ribosomal subunit of the archaebacterium Halobacterium cutirubrum have been purified and their amino acid composition and partial N-terminal amino acid sequence have been determined. These proteins as a group are much more acidic than the large subunit r-proteins from eubacteria or eukaryotes. Little sequence homology is evident between the 50S subunit archaebacterial r-proteins and the equivalent proteins from the eubacterium Escherichia coli.

Amino Acid Sequence↗
PubMed2003

Osmotic shock induces the presence of glycocardiolipin in the purple membrane of Halobacterium salinarum.

In the purple membrane (PM) of Halobacterium salinarum is present a phospholipid dimer consisting of sulfo-triglycosyl-diether (S-TGD-1) esterified to the phosphate group of phosphatidic acid (PA), i.e., S-TGD-1-PA, called glycocardiolipin (GlyC) (Corcelli, A., M. Colella, G. Mascolo, F. P. Fanizzi, and M. Kates. A novel glycolipid and phospholipid in the purple membrane. 2000. Biochemistry. 39: 3318-3326). The GlyC content of whole cells, PM, and other cell fractions of H. salinarum have been analyzed. GlyC is a nonabundant phospholipid in H. salinarum cells, and it represents one of the major phospholipids of isolated PM. In this report, we show that a) GlyC is formed during the isolation of PM, b) GlyC increase in H. salinarum cells is specifically induced by osmotic shock, and c) in correspondence with GlyC increase, a decrease of S-TGD-1 levels occurs. The changes in membrane lipid composition observed during the isolation of PM are due to de novo synthesis of GlyC from S-TGD-1.

Cardiolipins↗
PubMed1997

Effects of 60Co gamma-rays, ultraviolet light, and mitomycin C on Halobacterium salinarium and Thiobacillus intermedius.

Lethal effects of 60Co gamma-rays, UV light, and mitomycin C on two kinds of bacteria, Halobacterium salinarium which grows in highly concentrated salt media and Thiobacillus intermedius which requires reduced sulfur compounds, were studied and compared with those on Escherichia coli B/r. D37 values for H. salinarium, T. intermedius and E. coli B/r were 393, 150, and 92 Gy, respectively, by exposure to 60Co gamma-rays. They were 212, 38, and 10 J/m2, respectively, by exposure to UV light and 2.36, 0.25, and 0.53 microgram/ml/h, respectively, by exposure to mitomycin C. Against these agents, H. salinarium was much more resistant than T. intermedius and E. coli B/r.

Cobalt Radioisotopes↗
PubMed1998

Protective roles of bacterioruberin and intracellular KCl in the resistance of Halobacterium salinarium against DNA-damaging agents.

Halobacterium salinarium, a member of the extremely halophilic archaebacteria, contains a C50-carotenoid namely bacterioruberin. We have previously reported the high resistance of this organism against the lethal actions of DNA-damaging agents including ionizing radiation and ultraviolet light (UV). In this study, we have examined whether bacterioruberin and the highly concentrated salts in this bacterium play protective roles against the lethal actions of ionizing radiation, UV, hydrogen peroxide, and mitomycin-C (MMC). The colourless mutant of H. salinarium deficient in bacterioruberin was more sensitive than the red-pigmented wild-type to all tested DNA-damaging agents except MMC. Circular dichroism (CD) spectra of H. salinarium chromosomal DNA at various concentrations of KCl (0-3.5 M) were similar to that of B-DNA, indicating that no conformational changes occurred as a result of high salt concentrations. However, DNA strand-breaks induced by ionizing radiation were significantly reduced by the presence of either bacterioruberin or concentrated KCl, presumably due to scavenging of free radicals. These results suggest that bacterioruberin and intracellular KCl of H. salinarium protect this organism against the lethal effects of oxidative DNA-damaging agents.

Carotenoids↗
PubMed2005

Microcalorimetric studies of the action of Er3+ on Halobacterium halobium R1 growth.

A microcalorimetric technique was used to evaluate the influence of Er3+ on Halobacterium halobium R1 growth. By means of a LKB-2277 Bioactivity Monitor ampoule method, we obtained the thermogenic curves of H. halobium R1 growth at 37 degrees C. In order to analyze the results, the relationship between k and C was obtained. The addition of Er3+ in low concentration cause a decrease of the maximum heat production P max and growth rate constants k; however, Er3+ in a high concentration might promote growth of H. halobium R1. When Er3+ is in a much higher concentration, the growth of H. halobium R1 is inhibited completely. For comparison, the shapes of H. halobium R1 cells were observed by means of transmission electron microscope (TEM). According to the thermogenic curves and TEM photos of H. halobium R1 under different conditions, it is clear that the metabolic mechanism of H. halobium R1 growth has been changed with the addition of Er3+.

Calorimetry↗
PubMed2003

Microcalorimetric studies of the action of Na2SeO3 on the growth of Halobacterium halobium R1.

The effect of Na2SeO3 on the growth of Halobacterium halobium R1 was investigated by means of microcalorimetry at 37 degrees C. The biological response to toxicants is observed as the inhibition of the rate constant of growth of living cells. A low concentration of Na2SeO3 stimulated the growth of H. halobium R1, and a high concentration of Na2SeO3 inhibited the growth of H. halobium R1. Toxicity may be expressed as the half-inhibition concentration (IC50). The rate constants of growth (k) and the concentrations of Na2SeO3 (c) shows a linear relationship: k = 1.790 x 10(-6) -- 2.27 x 10(-3) c. The value of IC50 obtained from the accompanying figure of I-c is 679 microg/mL.

Algorithms↗
PubMed2003

Effects of iron limitation on the respiratory chain and the membrane cytochrome pattern of the Euryarchaeon Halobacterium salinarum.

The effects of iron limitation on the electron transport chain of the extremely halophilic Euryarchaeon Halobacterium salinarum were analyzed. When iron was growth-limiting, the respiratory rates as well as the inhibition pattern of the membranes were significantly different from membranes of iron replete cells. Changes in the availability of iron cause the formation of different respiratory pathways including different entry sites for electrons, different terminal oxidases of the respiratory chain, and drastic changes of the cytochrome composition and of the relative amounts of cytochromes. Under iron-limiting conditions, mainly low-potential cytochromes were measured. EPR spectroscopic studies revealed that the amount of proteins containing iron-sulfur clusters is reduced in membranes under iron-limiting growth conditions. Taken together, our results strongly suggest for the first time an important role of iron supply for the bioenergetics of an Archaeon.

Antimycin A↗