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PubMed1978

Identification of Escherichia coli and Bacillus stearothermophilus ribosomal protein binding sites on Escherichia coli 5S RNA.

E coli [32P]-labelled 5S RNA was complexed with E. coli and B. stearothermophilus 50S ribosomal proteins. Limited T1 Rnase digestion of each complex yielded three major fragments which were analysed for their sequences and rebinding of proteins. The primary binding sites for the E. coli binding proteins were determined to be sequences 18 to 57 for E-L5, 58 to 100 for E-L18 and 101 to 116 for E-L25. Rebinding experiments of purified E. coli proteins to the 5S RNA fragments led to the conclusion that E-L5 and E-L25 have secondary binding sites in the section 58 to 100, the primary binding site for E-L18. Since B. stearothermophilus proteins B-L5 and BL22 were found to interact with sequences 18 to 57 to 100 it was established that the thermophile proteins recognize and interact with RNA sequences similar to those of E. coli. Comparison of the E. coli 5S RNA sequence with those of other prokaryotic 5S RNAs reveals that the ribosomal proteins interact with the most conserved sections of the RNA.

Base Sequence↗
PubMed1976

Surface topography of the Bacillus stearothermophilus ribosome.

The surface topography of the intact 70S ribosomes and free 30S and 50S subunits from Bacillus stearothermophilus strain 2184 was investigated by lactoperoxidase-catalyzed iodination. Two-dimensional polyacrylamide gel electrophoresis was employed to separate ribosomal proteins for analysis of their reactivity. Free 50S subunits incorporated about 18% more 125I than did 50S subunits derived from 70S ribosomes, whereas, free 30S subunits and 30S subunits derived from 70S ribosomes incorporated similar amounts of 125I. Iodinated 70S ribosomes and subunits retained 62-78% of the protein synthesis activity of untreated particles and sedimentation profiles showed no gross conformational changes due to iodination. The proteins most reactive to enzymatic iodination were S4, S7, S10 and Sa of the small subunit and L2, L4, L5/9, L6 and L36 of the large subunit. Proteins S2, S3, S7, S13, Sa, L5/9, L10, L11 and L24/25 were labeled substantially more in the free subunits than in the 70S ribosome. Other proteins, including S5, S9, S12, S15/16, S18 and L36 were more extensively iodinated in the 70S ribosomes than in the free subunits. The locations of tyrosine residues in some homologous ribosomal proteins from B. stearothermophilus and E. coli are compared.

Electrophoresis, Polyacrylamide Gel↗
PubMed1988

Effect of growth temperature and media composition on the fatty acid composition of Bacillus stearothermophilus AN 002.

The influence of growth temperature, media composition and cell age on the chemical composition of Bacillus stearothermophilus strain AN 002 has been determined. The total cellular protein decreased and the free amino acid content increased with growth temperature, in both exponential and stationary growth phase. The protein and free amino acid contents of cells were higher in the stationary phase than in the exponential phase, irrespective of growth temperature and media composition. The RNA content was only reduced in cells grown at 55 degrees C. No significant variations were observed in the DNA and carbohydrate contents with respect to growth temperature and cell age. The total lipid and fatty acid compositions on the other hand varied as a function of growth temperature, cell age and media composition. Differences in the relative concentrations of even, odd and branched chain fatty acids were noticed. No variation was observed in the antiiso and unsaturated fatty acids with respect to growth temperature. The unique variations in the fatty acid composition and total lipids at the growth temperature of 50 degrees C and their variations in the stationary growth phase seem to be characteristic for B. stearothermophilus AN 002.

Amino Acids↗
PubMed1983

Activation and germination characteristics observed in endospores of thermophilic strains of Bacillus.

The properties of endospores of some thermophilic strains of Bacillus were examined. Included were strains isolated from thermal pools and springs in Yellowstone National Park, a strain of B. thermodenitrificans and two strains of B. stearothermophilus, ATCC 7953 (smooth) and T-10. The spores of thermophilic strains of Bacillus contained relatively high levels of dipicolinic acid ranging from 11-14.8% of the spore dry weight, while the calcium levels were similar to those observed in other bacterial endospores including mesophilic bacilli and thermophilic actinomycetes. Spore populations of thermophilic bacilli could not be effectively germinated in solutions of sodium phosphate alone but germinated well in solutions supplemented with one of a variety of organic compounds. Solutions containing L-valine or L-leucine were particularly effective. A wide range of pH permitted the germination of fractions of spore populations, however, optimum germination was observed only at pH values of 6.0 and above. A range in incubation temperatures of less than 25 degrees C permitted 50% or more of the spores of each of the organisms to germinate. Freshly prepared spore did not germinate, but these spores germinated rapidly and completely if they were heated for 30 min at 100 degrees C just prior to germination testing, i.e., the spores were heat activatable. However, spores of thermophilic bacilli could also be activated by shifting them to and holding them at temperatures below their optimum growth temperature of 65 degrees C. Of the ten temperatures tested, ranging from 4 degrees C through 50 degrees C, the optimum reduced temperature for spore activation was 30 degrees C.

Bacillus↗
PubMed1978

Calcium uptake and survival of Bacillus stearothermophilus.

The calcium transport in resting vegetative cells of Bacillus stearothermophilus was studied by determining the retention of 45Ca in a membrane filter assay. The kinetics of death by vegetative cells, when suspended in buffer at 55 degrees C, was also investigated. The calcium influx required the presence of an energy source, e.g. glucose-1-phosphate and the system exhibited saturation kinetics. The requirements for survival of the thermophilic cells reflected those of the calcium transport system. Thus, cells treated with nitrogen gas showed an increased thermal stability and a decreased efflux of calcium. The initial velocity of calcium influx correlated linearly with the survival of the cells after 1 min heating at 55 degrees C. Lanthanum inhibited calcium influx and reduced survival. Magnesium did not inhibit calcium influx and could replace calcium as a stabilizing agent. The results suggest that the thermophilic cells are not intrinsically heat stable but survive due to a high cellular concentration of divalent ions.

Aerobiosis↗
PubMed1981

The stringent response to unacylated tRNA, energy-and temperature-downshift in Bacillus stearothermophilus.

The response of the thermophile Bacillus stearothermophilus to inhibition of tRNA acylation, energy starvation and temperature downshift was characterized. We found that B. stearothermophilus, like other prokaryotic organisms, reacts with the so-called stringent response, which includes the accumulation of the unusual nucleotides guanosine 3',5' bis (diphosphate) [ppGpp] and guanosine 3'-diphosphate, 5'-tri-phosphate [pppGpp] and concomitantly the reduction of RNA synthesis and growth rate. The amount of (p)ppGpp formed depended on the cause of the stringent response: when tRNA acylation was inhibited (p)ppGpp synthesis was much higher than after energy starvation or temperature downshift whereas RNA synthesis was totally blocked in each case.

Energy Metabolism↗
PubMed1980

The production of alpha-amylase in batch and chemostat culture by Bacillus stearothermophilus.

The production of alpha-amylase (alpha-1,4-glucan 4-glucanohydrolase; EC 3.2.1.1) by a strain of Bacillus stearothermophilus isolated from leaf litter was investigated in a tryptone-maltose medium at 55 degrees C in batch and chemostat culture. Amylase production was growth-limited and restricted to the exponential phase in batch culture. The enzyme yield was reduced by 40% when the culture pH was maintained at pH 7.2. Amylase production in chemostat culture was influenced by the growth rate throughout the dilution rate range used.

Amylases↗
PubMed1976

Altered phospholipid metabolism in a temperature-sensitive mutant of a thermophilic bacillus.

The phospholipid metabolism of a temperature-sensitive mutant of a thermophilic bacillus was studied after the shift from a permissive (58 degrees C) to a restrictive (65 degrees C) growth temperature. During the short period of growth of the mutant at 65 degrees C, the proportions of cardiolipin and its 3-acyl derivative (lyso-cardiolipin) increased, and the proportions of phosphatidylglycerol and phosphatidylethanolamine decreased on cell dry weight basis. In 32P incorporation and turnover experiments, phosphatidylglycerol showed the most rapid uptake and loss of the label. Turnover of cardiolipin, limited to a short period, ceased 18 min after the shift, as did the turnover of phosphatidylethanolamine. In the absence of net phospholipid synthesis, there was a quantitative conversion of phosphatidylglycerol to cardiolipin and an increase in the proportion of lyso-cardiolipin. Chloramphenicol, added to the medium at the time of the shift, reduced the rate of phospholipid synthesis, prevented the increase in the proportions of cardiolipin and lyso-cardiolipin, and slowed the decrease in the proportions of the other two phospholipids. The results indicated a defect in the regulatory mechanism(s) of phospholipid metabolism in the mutant at the restrictive temperature.

Cardiolipins↗
PubMed1976

Effect of temperature on the viability of Bacillus stearothermophilus.

One of the obligate thermophilic bacteria, Bacillus stearothermophilus, was unable to grow at temperatures below 35 degrees C. About 80% of the population in the bacterial culture died at the temperatures, and the same extent of loss in either of the activities of oxygen consumption or synthesis of protein or nucleic acid of the organisms was observed. With the progress of death of the organisms, reduced nicotinamide-adenine dinucleotide came to be oxidized by the organisms, enzymes such as fructose-1,6-diphosphate aldolase, when the organisms were washed with phosphate buffer, were leaked out of the organisms, and an increasing amount of ribonucleoprotein was released into the culture medium. The change of the membrane state was then suggested to be one of the possible causes for the death of the organisms at the temperatures.

Bacterial Proteins↗
PubMed1988

Localized insertion of new S-layer during growth of Bacillus stearothermophilus strains.

Bacillus stearothermophilus strains PV 72 and ATCC 12980 carry a crystalline surface layer (S-layer) with hexagonal (p6) and oblique (p2) symmetry, respectively. Sites of insertions of new subunits into the regular lattice during cell growth have been determined by the indirect fluorescent antibody technique and the protein A/colloidal gold technique. During S-layer growth on both bacillus strains the following common features were noted: 1. shedding of intact S-layer or turnover of individual subunits was not seen; 2. new S-layer was deposited in helically-arranged bands over the cylindrical surface of the cell at a pitch angle related to the orientation of the lattice vectors of the crystalline array; 3. little or no S-layer was inserted into pre-existing S-layer at the poles, and 4. septal regions and, subsequently, newly formed cell poles were covered with new S-layer protein.

Bacterial Proteins↗
PubMed1989

Replacement of potassium ions by ammonium ions in different micro-organisms grown in potassium-limited chemostat culture.

The biomass concentration extant in potassium-limited cultures of either Klebsiella pneumoniae or Bacillus stearothermophilus (when growing at a fixed temperature and dilution rate in a glucose/ammonium salts medium) increased progressively as the medium pH value was raised step-wise from 7.0 to 8.5. Because the macromolecular composition of the organisms did not vary significantly, this increase in biomass could not be attributed to an accumulation of storage-type polymers but appeared to reflect a pH-dependent decrease in the cells' minimum K+ requirement. Significantly, this effect of pH was not evident with cultures in which no ammonium salts were present and in which either glutamate or nitrate was added as the sole nitrogen source; however, it was again manifest when various concentrations of NH4Cl were added to the glutamate-containing medium. This suggested a functional replacement of K+ by NH4+, a proposition consistent with the close similarity of the ionic radii of the potassium ion (1.33 A) and the ammonium ion (1.43 A). At pH 8.0, and with a medium containing both glutamate (30 mM) and NH4Cl (100 mM), cultures of B. stearothermophilus would grow without added potassium at a maximum rate of 0.7 h-1. Under these conditions the cells contained maximally 0.1% (w/w) potassium (derived from contaminating amounts of this element in the medium constituents), a value which should be compared with one of 1.4% (w/w) for cells growing in a potassium-limited medium containing initially 0.5 mM K+.(ABSTRACT TRUNCATED AT 250 WORDS)

Culture Media↗
PubMed1987

The active site of manganese-containing superoxide dismutase from Bacillus stearothermophilus studied by 1H and 19F magnetic relaxation.

The dependence of the magnetic relaxation rates of 1H and 19F- on temperature, frequency, pH and N-3 concentration, were measured in solutions of Manganese-containing superoxide dismutase of Bacillus stearothermophilus, and were compared to activity measurements, in order to obtain some information on the structure and dynamics at Mn(III) present in the active site of the enzyme. The experimental data lead us to hypothesize the presence of two binding sites in the coordination sphere of the enzyme bound Mn(III), which are accessible to water and anions and have different chemical and spectroscopic properties. NMR measurements carried out in the presence of competitive inhibitors and the pH dependence of both NMR relaxation rates suggest that F-, N-3 and OH- ions bind to one site, while a water molecule binds to the other one. The stability constant values of the complexes between these anions and the enzyme are reported. The influence of the anions on activity and the pH dependence of NMR parameters are discussed.

Bacterial Proteins↗
PubMed1986

Structural and chemical characterization of S-layers of selected strains of Bacillus stearothermophilus and Desulfotomaculum nigrificans.

The structures, amino acid- and neutral sugar compositions of the crystalline surface layers (S-layers) of four selected strains each of Bacillus stearothermophilus and Desulfotomaculum nigrificans were compared. Among the four strains of each species a remarkable diversity in the molecular weights of the S-layer subunits and in the geometry and constants of the S-layer lattices was apparent. The crystalline arrays included hexagonal (p6), square (p4) and oblique (p2) lattices. In vitro self-assembly of isolated S-layer subunits (or S-layer fragments) led to the formation of flat sheets or open-ended cylindrical assembly products. The amino acid composition of the S-layers exhibited great similarities and was predominantly acidic. With the exception of the S-layers of two strains of B. stearothermophilus (where only traces of neutral sugars could be detected), all other S-layer proteins seemed to be glycosylated. Among these strains significant differences in the amount and composition of the glycan portions were found. Based on this diversity interesting questions may be asked about the biological significance of the carbohydrate units of glycoproteins in prokaryotic organisms.

Amino Acids↗
PubMed1993

The complete primary structure of ribosomal protein L1 from Thermus thermophilus.

The primary structure of the 23S rRNA binding ribosomal protein L1 from the 50S ribosomal subunit of Thermus thermophilus ribosomes has been elucidated by direct protein sequencing of selected peptides prepared by enzymatic and chemical cleavage of the intact purified protein. The polypeptide chain contains 228 amino acids and has a calculated molecular mass of 24,694 D. A comparison with the primary structures of the corresponding proteins from Escherichia coli and Bacillus stearothermophilus reveals a sequence homology of 49% and 58%, respectively. With respect to both proteins, L1 from T. thermophilus contains particularly less Ala, Lys, Gln, and Val, whereas its content of Glu, Gly, His, Ile, and Arg is higher. In addition, two fragments obtained by limited proteolysis of the intact, unmodified protein were characterized.

Amino Acid Sequence↗
PubMed1984

Effect of mercaptoethylamine on DNA degradation in thermophilic bacteria bac. Stearothermophilus exposed to gamma-, UV-radiation or methylnitrosourea.

The effect of mercaptoethylamine (MEA) on degradation of DNA in thermophilic bacteria Bac. stear. exposed to gamma-, UV-rays or methylnitrosourea (MNU) was studied. Using centrifugation on alkaline and neutral sucrose gradients, it was shown that MEA inhibits the accumulation of breaks in the DNA of Bac. stear. It also lowers the level of DNA degradation in toluene-treated cells of Bac. stear. under the action of the intrinsic nuclease, reduces the activity of the endonuclease specific for apurinic DNA, as well as that of S1-nuclease and DNase-I in vitro. The inhibition in the accumulation of DNA breaks is assumed to be due to a decrease of the endonuclease activity in the cells of thermophilic bacteria.

Cobalt Radioisotopes↗
PubMed1976

A comparison of the 16S ribosomal RNAs from mesophilic and thermophilic bacilli: some modifications in the Sanger method for RNA sequencing.

Two modifications in the Sanger two dimensional electrophoretic procedure for RNA analysis are reported. One increases resolution on the primary fingerprint to the point that digests of large RNAs, of the size 1500-3000 nucleotides yield well resolved fingerprint patterns. The other is a novel endonucleolytic procedure that proves useful in determining sequences of the large oligonucleotides produced by T1 ribonuclease. These modifications have been used in determining the catalogs of oligomers produced by T1 ribonuclease digestion of 16S rRNAs from three related organisms, Bacillus subtilis, B.pumilus and B.stearothermophilus. The possible effects of adaptation to a thermophilic niche on ribosomal RNA primary structure and the phylogenetic relatedness of the two mesophilic Bacilli are discussed.

Animals↗