| purification and properties of d-glyceraldehyde-3-phosphate dehydrogenase from an extreme thermophile, thermus thermophilus strain hb 8. | 1. d-glyceraldehyde-3-phosphate dehydrogenase from an extreme thermophile, t. thermophilus strain hb8, was purified and crystallized. 2. the enzyme was found to possess remarkable heat stability, being slowly inactivated at 90 degrees c. 3. basic kinetic constants and ph profile are reported. the enzyme was activated 25-fold by 90 mm nh4cl, and also by ethanol up to 5-fold at 30 degrees c. 4. the enzyme was found to be far more resistant to urea or sodium dodecylsulfate than the rabbit enzyme. 5 ... | 1976 | 6270 |
| purification and some properties of nadp+ -specific isocitrate dehydrogenase from an extreme thermophile, thermus flavus at-62. | thermostable nadp+ -specific isocitrate dehydrogenase (ec 1.1.1.42) was purified from crude extract of an extremely thermophilic bacterium thermus flavus at-62 through deae-cellulose column, acetone fractionation, deae-sephadex a-50 column and isoelectric focussing. the enzyme was purified about 500-folds in its specific activity and purity was found to be about 96%. the enzyme was not inactivated after 60 min at 70 degrees c, but 20 and 80% of the activity were lost after 60 min at 80 degrees a ... | 1976 | 7466 |
| enzymatic synthesis of oligonucleotides of defined sequence. the "single addition" of 2(3)-o-dihydrocinnamoyl-nucleoside 5'-diphosphate to a primer oligonucleotide catalyzed by a thermophilic polynucleotide phosphorylase. | several oligonucleotides of defined sequence were synthesized using 2'(3')-o-dihydrocinnamoyl-nucleoside 5'-diphosphates (dhc-ndp) as substrates for polynucleotide phosphorylase ec 2.7.7.8 from thermus thermophilus. the enzyme catalyzed the transfer of one nucleotidyl residue from each of the 2'(3')-o-dihydrocinnamoyl esters of cdp, udp, and gdp to the 3'-terminus of the primer triadenosine diphosphate, (ap)2a. the products were shown to be (ap)3c, (ap)3u, and (ap)3g by enzymatic analysis. | 1976 | 9379 |
| superoxide dismutase from thermus aquaticus. isolation and characterisation of manganese and apo enzymes. | superoxide dismutase has been isolated and characterised from the extreme thermophile thermus aquaticus. the pure enzyme is a reddish-purple manganese-containing protein with a molecular weight of approximately 80000 +/- 5000. combination of gel electrophoresis in dodecylsulphate and amino acid analysis shows that it is composed of four identical subunit polypeptide chains consisting of approximately 186 amino acids. the tetrameric protein contains two atoms of manganese. a stable manganese-free ... | 1977 | 14828 |
| repressible alkaline phosphatase from thermus aquaticus: associated phosphodiesterase activity. | a repressible alkaline phosphatase has been isolated from the extreme bacterial thermophile. thermus aquaticus, and has been purified to homogeneity as judged by disc acrylamide electrophoresis and sodium dodecyl sulfate electrophoresis. upon investigation, the purified enzyme was shown to hydrolyze certain phosphodiesters in addition to a wide variety of phosphomonoesters. the diesters included bis-p-nitro-phenyl phosphate and thymidine 3'-monophospho-p-nitro-phenyl ester. the temperature optim ... | 1977 | 16900 |
| alkaline isomerization of thermoresistant cytochrome c-552 and horse heart cytochrome c studied by absorption and resonance raman spectroscopy. | the structure of the thermoresistant cytochrome c (552, thermus thermophilus) has been investigated at neutral and alkaline ph by absorption and resonance raman spectroscopy and compared with that of horse heart cytochrome c. the ligands of the ferricytochrome c-552 at neutral ph are considered to be histidine and methionine, whereas the ligands of ferrocytochrome c-552 are histidine and another nitrogen base, histidine or lysine. ferric cytochrome c-552 undergoes an alkaline isomerization with ... | 1978 | 23857 |
| metabolic function of the glyoxylic shunt in an extreme thermophilic strain of the genus thermus. | | 1976 | 64177 |
| physiology of thermophilic bacteria. | | 1979 | 95242 |
| studies on bacterial pyruvate kinase: properties of the enzyme from pseudomonas aeruginosa and thermus thermophilus. | | 1979 | 121876 |
| a thermostable phosphofructokinase from the extreme thermophile thermus x-1. | | 1975 | 128320 |
| [several cytologic features of the thermophilic bacteria thermus flavus and thermus ruber]. | the extreme thermophilic bacterium thermus flavus 71 and the obligate thermophilic bacterium thermus ruber 40 have been isolated from hot springs of kamchatka and tadjikistan, and their fine structure has been studied. this cells are similar in structure to gram-negative bacteria, they do not form spores or flagella, and their cell walls and cytoplasmic membrane are clearly visible under the electron microscope since the cells of t . flavus contain a yellow carotenoid pigment and the cells of t. ... | 1977 | 142194 |
| studies on nadp-+-specific isocitrate dehydrogenase from an extreme thermophile, thermus flavus at-62. | 1. nadp-+-specific isocitrate dehydrogenase [ec 1.1.1.42] was partially purified by about 440-fold from an extreme thermophile, thermus flavus at-62. 2. remarkable thermostability of the enzyme was confirmed. the enzyme was not inactivated after 60 min at 70 degrees, and the activity was lost only slowly at 80 degrees. above 90 degrees, however, rapid inactivation was observed. 3. the dehydrogenase was susceptible to concerted inhibition by oxaloacetate plus glyoxylate. in the presence of oxaloa ... | 1975 | 166075 |
| studies on a thermophilic rna polymerase which is active only on poly d(a-t) and poly dadt. | two types of rna polymerases [ec 2.7.7.6], polymerases a and b, exist in thermophilic bacteria, thermus thermophilus hb8. polymerase b is apparently like the core enzyme of polymerase a but is active only when an alternating copolymer of deoxyadenylic and deoxythymidylic acids (poly d(a-t)) or a mixture of homopolymers of deoxyadenylic acid and deoxythymidylic acid (poly dadt) is used as a template. polymerase b was further characterized to elucidate its relation to polymerase a and to determine ... | 1975 | 175054 |
| glyceraldehyde 3-phosphate dehydrogenase from an extreme thermophile, thermus aquaticus. | | 1976 | 181263 |
| kinetic studies on redox reactions of hemoproteins. i. reduction of thermoresistant cytochrome c-552 and horse heart cytochrome c by ferrocyanide. | the oxidation-reduction reaction of horse heart cytochrome c and cytochrome c (552, thermus thermophilus), which is highly thermoresistant, was studied by temperature-jump method. ferrohexacyanide was used as reductant. (formula: see text.) thermodynamic and activation parameters of the reaction obtained for both cytochromes were compared with each other. the results of this showed that (1) the redox potential of cytochrome c-552, + 0.19 v, is markedly less than that of horse heart cytochrome c. ... | 1977 | 195599 |
| purification and some properties of cytochrome c-552 from an extreme thermophile, thermus thermophilus hb8. | a c-type cytochrome, cytochrome c-552, from a soluble fraction of an extreme thermophile, thermus thermophilus hb8, was highly purified and its properties investigated. the absorption peaks were at 552, 522, and 417 nm in the reduced form, and at 408 nm in the oxidized form. the isoelectric point was at ph 10.8, the midpoint redox potential was about +0.23 v, and the molecular weight was about 15,000. the cytochrome c-552 was highly thermoresistant. the cytochrome reacted rapidly with pseudomona ... | 1977 | 199583 |
| cytochrome c-550 from a thermophilic bacterium ps3. | | 1979 | 223548 |
| exchange integral for a variety of tetranuclear ferredoxins. | the temperature dependence of epr spectra of oxidized [4fe-4s](-1,-2) ferredoxins (previously designated hipip) and a reduced [4fe-4s](-2,-3) ferredoxin have been analyzed so as to determine the energy of a low-lying excited electronic state. the values obtained were: center s-3 from beef heart, 44 cm-1; center s-3 from mung bean, 53 cm-1; the [4fe-4s](-1,-2) ferredoxin from thermus thermophilus, 78 cm-1; center n-2 of nadh ubiquinone reductase, 83 cm-1. increasing axial distortion in the epr sp ... | 1979 | 226131 |
| denaturation of thermophilic ferricytochrome c-552 by acid, guanidine hydrochloride, and heat. | the denaturation of thermus thermophilus cytochrome c-552 by acid, guanidine hydrochloride, and heat was studied by measuring the changes in absorption and circular dichroism. cytochrome c-552 was remarkably resistant to acid; the pk of the transition from the low- to the high-spin form was roughly 0.3. the effect of guanidine hydrochloride on the heme iron-methionine bond of thermus and horse cytochromes c was also investigated; a comparison of the free-energy changes for the displacement of th ... | 1979 | 229899 |
| a double-alpha c-type cytochrome, cytochrome c-555, 549, from an extreme thermophile, thermus thermophilus hb8. | a "double-alpha" c-type cytochrome, cytochrome c-555, 549, was isolated from the membrane fraction of an extreme thermophile, thermus thermophilus hb8, and highly purified by chromatographies on deae-cellulose and sephadex g-75 and by isoelectric focusing. the absorption maxima were at 554.8, 548.6, 522, and 417 nm in the reduced form, and at 528, 409, and 360 nm in the oxidized form. the double alpha-peak of this cytochrome was enhanced at liquid nitrogen temperature. the cytochrome contained o ... | 1979 | 231033 |
| a thermostable sequence-specific endonuclease from thermus aquaticus. | a sequence-specific endonuclease, taq i, of novel specificity has been partially purified from an extreme thermophile, thermus aquaticus. the enzyme cleaves bacteriophage lambda dna at many (greater than 30) sites and bacteriophage psix174 rf dna at 10 sites. the enzyme is active at temperatures up to 70 degrees. the cleavage sites on psix174 rf dna have been mapped. the sequence recognized and cleaved by taq i has been shown to be the symmetrical tetranucleotide: (formula: see text). | 1977 | 265518 |
| structural fluctuation of the polypeptide-chain elongation factor tu. a comparison of factors from escherichia coli and thermus thermophilus hb8. | the kinetics of hydrogen-deuterium exhcange in the polypeptide chain elongation factor tu (ef tu) from escherichia coli and that from thermus thermophilus hb8 has been examined in aqueous solutions at various ph and temperatures by means of infrared absorption measurements. the free ef-tu from e. coli has a greater reaction rate at all ph values and at every temperature than that of the gtp-bound or gdp-bound ef-tu. the free ef-tu from t. thermophilus, on the other hand, has an alomst equal reac ... | 1977 | 334541 |
| purification and properties of the polypeptide chain release factor (rf-4) from an extreme thermophile, thermus thermophilus hb8. | the polypeptide chain release factor 1 (rf-1) has been purified from an extreme thermophile, thermus thermophilus hb8. the purification procedure included steps of aqueous two-phase partition, ammonium sulfate fractionation, and column chromatographies on deae-sephadex, sephadex g-150, and cm-sephadex. the preparation was more than 90% pure as judged by polyacrylamide gel electrophoresis. the specific activity was about 3.3 pmol of formyl-[3h]-methionine released in 1 min at 25 degrees c per mic ... | 1977 | 334756 |
| reversible thermal unfolding of thermostable phosphoglycerate kinase. thermostability associated with mean zero enthalpy change. | | 1977 | 338921 |
| an enhanced thermostability in thermophilic 5-s ribonucleic acids under physiological salt conditions. | the secondary structure of 5-s rrnas of thermus aquaticus (an extreme thermophile), bacillus stearothermophilus (a moderate thermophile) and escherichia coli (a mesophile) was compared using thermal denaturation techniques under varying ionic conditions. at a low ionic strength (10 mm k+), the tm of t. aquaticus 5-s rna differed by only 1 degrees c from that of e. coli rna and the molecule was fully denatured well below the optimum growth temperature of the thermophile. the internal na+, k+ and ... | 1978 | 363159 |
| [the role of 2-thioribothymidine in the t psi c region of trna from an extreme thermophile on the thermal stability and the functional efficiency of the trna molecule (author's transl)]. | | 1978 | 364538 |
| studies on polypeptide-chain-elongation factors from an extreme thermophile, thermus thermophilus hb8. 2. catalytic properties. | catalytic properties of the elongation factors from thermus thermophilus hb8 have been studied and compared with those of the factors from escherichia coli. 1. the formation of a ternary guanine-nucleotide . ef-tu . ef-ts complex was demonstrated by gel filtration of the t. thermophilus ef-tu . ef-ts complex on a sephadex g-150 column equilibrated with guanine nucleotide. the occurrence of this type of complex has not yet been proved with the factors from e. coli. 2. the dissociation constants f ... | 1978 | 367783 |
| [trna-methylase study of the extreme thermophile, thermus flavus]. | trna methylases were studied in the extreme thermophilic culture of thermus flavus, strain 71. like e. coli, the culture contained only those trna methylases which catalysed the formation of m1a and m7g. mg2+, ca2+ and na+ ions activated trna methylases of thermus flavus in the series mg greater than ca greater than na while mn2+ ions inhibited the enzyme. the activity of trna methylases was higher in t. flavus than in e. coli, and required less protein and time for exhaustive methylation of trn ... | 1979 | 375041 |
| role of ribothymidine in the thermal stability of transfer rna as monitored by proton magnetic resonance. | in order to elucidate the functional role of the modified uridines at position 54 of trna, the 270 mhz high-field proton nmr spectra of methionine trnas from e. coli, from a mutant thereof, and from t. thermophilus, containing ribothymidine, uridine and 2-thioribothymidine, respectively, have been measured as a function of temperature. a comparison of the nmr melting profiles of the minor nucleosides from these trnas shows that the melting temperature of uridine containing trna is 6 degrees c lo ... | 1979 | 377228 |
| kietics of thermal unfolding and refolding of thermostable phosphoglycerate kinase. | the kinetics of denaturation by guanidine hydrochloride (guhcl) of a thermostable phosphoglycerate kinase (pgk) extracted from thermus thermophilus and of yeast pgk at neutral ph were studied by circular dichroism. denaturation by guhcl proceeded as a first-order reaction. the activation free energy of the denaturation reactions (delta gf not identical to ) in the absence of guhcl was estimated to be 32.7 kcal/mol for t. thermophilus pgk and 27.9 kcal/mol for yeast pgk (at 25 degrees c). measure ... | 1979 | 387749 |
| immunological properties of heat-killed thermophilic bacteria. | | 1979 | 393965 |
| simple efficient methods for the isolation of malate dehydrogenase from thermophilic and mesophilic bacteria. | malate dehydrogenase from a number of bacteria drawn from several genera and representing the mesophilic, moderately thermophilic and extremely thermophilic classes was isolated by procedures which involve only a small number of steps (in most cases only two), of which the key one is affinity chromatography on 5'-amp--sepharose and/or on nad+--hexane--agarose. electrophoretic analysis of the native enzymes in polyacrylamide gel and of the denaturated enzymes in sodium dodecyl sulphate/polyacryla ... | 1979 | 435244 |
| purification and properties of phosphoglycerate kinase from thermus thermophilus strain hb8. | (1) a glycolytic enzyme, phosphoglycerate kinase [ec 2.7.2.3], was purified from cells of an extreme thermophile, thermus thermophilus strain hb8. the enzyme was resistant to heat, and no loss of activity was observed after incubation for 10--20 min at 79 degrees c. (2) catalytic properties such as ph optimum (ph 6--8.5), kinetic parameters (km=0.28 mm for atp, 1.79 mm for glycerate 3-phosphate), substrate specificity and inhibitors of the enzyme were investigated and compared with those of phos ... | 1979 | 457645 |
| a new polyamine, thermospermine, 1,12-diamino-4,8-diazadodecane, from an extreme thermophile. | a new polyamine has been extracted from an extreme thermophile, thermus thermophilus, and its chemical structure was determined as 1,12-diamino-4,8-diazadodecane, nh2(ch2)3nh(ch2)3nh(ch2)4nh2, based on its proton nmr, 13c nmr, and mass spectra. a trivial name "thermospermine" is proposed for the new compound. | 1979 | 479149 |
| regulatory characteristics of phosphoenolpyruvate carboxylase from the extreme thermophile, thermus aquaticus. | phosphoenolpyruvate carboxylase from the extremely thermophilic bacterium, thermus aquaticus yt-1, exhibits a virtually absolute requirement for acetyl coa and there is strong positive cooperativity in the interaction of this activator with the enzyme. several tricarboxylic acid cycle intermediates inhibit the enzyme. these findings suggest an anaplerotic role for the enzyme and an allosteric modulation of its activity by acetyl coa and tricarboxylic acid cycle intermediates. | 1979 | 497233 |
| protein turnover in the extreme thermophile thermus aquaticus. | protein turnover in the extreme bacterial thermophile thermus aquaticus was examined in exponential cultures at 75 degrees c. the relative amount of [3h]leucine incorporated into trichloroacetic acid-insoluble material was stable in pulse-chase experiments assayed over 2.5 h. the trichloroacetic acid-insoluble radioactive leucine was stable upon the addition of chloramphenicol, which blocks protein synthesis in t. aquaticus. the specific activity of a phosphate-repressible alkaline phosphatase, ... | 1979 | 500561 |
| involvement of histidine residues in the substrate binding of elongation factor tu from thermus thermophilus: proton nuclear magnetic resonance and photooxidation study. | | 1979 | 507806 |
| cd and nmr studies on the conformational thermostability of 2-thioribothymidine found in the t psi c loop of thermophile trna. | | 1979 | 518660 |
| addition of short guanylyl blocks to oligonucleotide primers with a thermophilic polynucleotide phosphorylase. its application to the synthesis of oligonucleotides containing guanylyl residues. | polynucleotide phosphorylase from thermus thermophilus catalyzed the addition of short guanylyl blocks from gdp to the 3'-hydroxyl termini of oligonucleotide primers at low temperature in a simple reaction mixture. polyguanylic acid formation was inhibited at 37 degrees c, but the addition of one or two guanylyl residues to oligonucleotide primers proceeded in high yields. the reaction was applied to the synthesis of oligonucleotides containing guanylyl residues at the 3'-end. using (ap)2a and ( ... | 1979 | 521440 |
| glycolipis in prokaryotic cells. | | 1977 | 598568 |
| [speroplast behavior in cultures of thermus ruber]. | spheroplasts spontaneously originating in cultures of thermus ruber, which are cultivated on potato-peptone media, are capable of growth and multiplication. they may reach 10 mc in diameter. spheroplasts multiply by budding which can be preceded with inner division or budding; as a result 2--9 and more protoplast bodies are formed under the "envelope" of a spheroplast. self-reproduction of spheroplasts is most active in a semiliquid potato-meat-peptone medium containing 0.2--0.3 per cent of agar ... | 1977 | 600101 |
| isolation of extrachromosomal deoxyribonucleic acids from extremely thermophilic bacteria. | eight strains of thermophilic bacteria were examined for the presence of covalently closed circular deoxyribonucleic acid molecules by caesium chloride-ethidium bromide density gradient centrifugation. four of the eight strains tested, thermus flavus bs1, at61, at62 and thermus thermophilus hb8 carried covalently closed circular dna molecules. thermus flavus bs1 haboured two species of plasmids with molecular weights of 6.1 x 10(6) and 17.0 x 10(6) as determined by electron microscopy. thermus t ... | 1978 | 632802 |
| purification and properties of superoxide dismutase from thermus thermophilus hb8. | manganese-containing superoxide dismutase was isolated from an extreme thermophile, thermus thermophilus hb8. about 150 mg of the enzyme was obtained from 500 g of wet cells. the enzyme was easily crystallized in octahedra from ammonium sulfate solution. the molecular weight of the enzyme was determined to be 8.2 x 10(4) and 8.4 x 10(4) by sedimentation equilibrium and gel-filtration, respectively. the enzyme contains 2 atoms of manganese per mole and consists of four subunits of identical molec ... | 1978 | 659388 |
| [nucleotide makeup of the dna of thermophilic bacteria of the genus thermus]. | the nucleotide composition of dna was determined in extreme thermophilic and obligate thermophilic nonsporeforming bacteria belonging to a new genus thermus. the gc content (in mol%) in the dna of exteme thermophilic bacteria varied from 65.3 to 70.8 per cent depending on the strain. the amount of gc (in mol% in the dna of obligate thermophilic and extreme thermophilic bacteria of the thermus genus was higher than that in the dna of sporeforming obligate thermophilic bac. coagulans. bac. circula ... | 1978 | 661633 |
| purification and properties of an extracellular exonuclease from thermus thermophilus hb8. | an extracellular exonuclease has been found and purified about 10,000-fold from the culture broth of an extreme thermophile, thermus thermophilus hb8. the enzyme had an isoelectric point at ph 5.1 and seems to be of a multimolecular type, with molecular weights estimated to be ca. 530,000 (peak i) and around 330,000 (peak ii) by gel filtration. the properties of the most highly purified enzyme fraction, peak i were investigated. the enzyme requires divalent cations (mg2+ greater than sn2+ greate ... | 1978 | 670151 |
| membrane properties of an extreme thermophile. i. detection of the phase transition and its dependence on growth temperature. | phase transition was detected by a fluorescence polarization technique in the membrane of thermus thermophilus hb8: it was found to be a function of cell growth temperature when the cell growth temperature was varied between 50-80 degrees c. a systematic relation between the phase transition temperature and the growth temperature was observed. differential scanning calorimetry was also applied. the phase transition was found to take place between 34 and 55 degrees c for cells grown at 50 degrees ... | 1978 | 670160 |
| membrane properties of an extreme thermophile. ii. membrane functions underlying leucine transport and their relation with thermotropic phase transitions. | various membrane properties of thermus thermophilus hb8 were studied in order to elucidate the mechanism and implication of cell adaptation to a high temperature environment. 1. the profile of temperature dependence of the amino acid uptake rates was similar for the membrane obtained from cells grown at both 61 degrees c and 77 degrees c. 2. the remaining uptake activity after heat treatment paralleled the membrane potential generating ability, as measured by auramine o fluorescence response to ... | 1978 | 670161 |
| anomalous citrate synthase from thermus aquaticus. | | 1978 | 670934 |
| [thermophilic bacteria, thermus ruber, that produce a bright orange pigment]. | a non-sporeforming gram-negative bacterium isolated from soils of africa was shown to belong to the species thermus ruber in its morphologo-cytological and physiologobiochemical properties. it differed from the thermus ruber species described elsewhere (loginova et al., 1975; loginova and egorova, 1975) only on colour: the former contained a bright-red pigment while the latter produced bright-orange pigments. | 1978 | 672696 |
| a comparative analysis of extreme thermophilic bacteria belonging to the genus thermus. | several extreme thermophilic gram negative bacteria found in a thermally polluted river in belgium have been compared with thermus strains isolated from widely distant geographical areas. this analysis has become possible after the design of a new culture medium (162). all strains examined (including the isolate successively denominated flavobacterium thermophilum and thermus thermophilus) were found to be morphologically identical with strain yt-1 of thermus aquaticus. the cells are immotile, r ... | 1978 | 678024 |
| an isochizomer of taqi from thermus thermophilus hb8. | a site-specific endonuclease has been isolated from thermus thermophilus hb8 and named tthhb8i. it recognizes the same sequences as taqi from thermus aquaticus yt-1 does. the amount of tthhb8i in the cells was comparable to that of taqi. t. thermophilus hb8 has an advantage over t. aquaticus yt-1 for preparation of a taqi-like enzyme since it is easier to obtain t. thermophilus hb8 cells in quantity. | 1978 | 730757 |
| studies on polypeptide-chain-elongation factors from an extreme thermophile, thermus thermophilus hb8. 1. purification and some properties of the purified factors. | polypeptide chain elongation factors have been purified from an extreme thermophile, thermus thermophilus hb8. by chromatography on a deae-sephadex column, the factors were separated into two peaks; peak i contained a complex of ef-tu and ef-ts, while peak ii was composed of ef-tu.gdp and ef-g. these factors were subsequently purified to homogeneous states and crystallized. the ef-tu . ef-ts complex could be resolved into ef-tu and ef-ts by chromatography on a sephadex g-200 column in the presen ... | 1978 | 738277 |
| conformational stability of lactate dehydrogenase from bacillus thermus-aquaticus [proceedings]. | | 1978 | 744388 |
| proton magnetic resonance spectra of trna-met-f from thermus thermophilus. | 220 mhz proton magnetic resonance spectra of trnas in bulk and trna-met-f from thermus thermophilus have been measured and compared with those of trnas from e. coli. temperature dependences and chemical shift positions of the bulk trnas are well explained by the difference in their gc contents. it is known that the base sequence of the double helical regions in the cloverleaf structure of t. thermophilus trna-met-f is different from that of e. coli trna-met-f only at two positions in tpsicarm; o ... | 1977 | 325519 |
| an endonucleolytic activity of nuclease tt1 specific for superhelical dna. | highly purified nuclease tt1 from t. thermophilus hb8 acts on a linear single- and double-stranded dna as an exonuclease and produces 5'-mononucleotides either from the 5'- or 3'-terminus. it was found that the enzyme also possesses an endonuclease activity specific for superhelical (form i) and single-stranded circular dna. form i of various kinds of dna (phi x174, pm2, co1e1 and rf 1010 etc.) is nicked to yield first relaxed circles (form ii) and then nicked at the opposite site to yield unit ... | 1979 | 232756 |
| reversible thermal unfolding of thermostable cytochrome c-552. | | 1978 | 209196 |
| a single cleavage of simian virus 40 (sv40) dna by a site specific endonuclease from thermus aquaticus, taq i. | a site specific endonuclease from thermus aquaticus, taq i, cleaves simian virus 40 (sv40) dna at a single site. the cleavage site was localized on the physical map by double digestions, using the previously characterized fragments produced by digestion with hae ii, hae iii, alui, hhai, hinfi, or bsti. the taq i site is located at the position that is 56.5% of the unit length from the eco ri site. | 1978 | 204628 |
| c-type cytochromes isloated from an extreme thermophile, thermus thermophilus hb8. | two cytochromes of the c-type, c-554 and c-549, were isolated from the soluble fraction of an extreme thermophile, thermus thermophilus hb8. highly purified cytochrome c-554 had absorption maxima at 554, 522, and 417 nm in the reduced state, and at 410 nm in the oxidized state. the alpha-band of the reduced state resembled that of "split-alpha" cytochromes. the isoelectric point was at ph 4.9, and the molecular weight was about 29,000. cytochrome c-549, partially purified, had absorption maxima ... | 1978 | 204627 |
| activation of thermus phosphofructokinase by monovalent cations. | the presence of the monovalent cations tl+, nh+4, k+, rb+ or cs+, in decreasing order of potency, produce a marked equivalent increase in the specific enzyme activity of phosphofructokinase (atp:d-fructose-6-phosphate 1-phosphotransferase, ec 2.7.1.11) purified from extreme thermophile, thermus x-1. by contrast, the monovalent cations li+, na+ or ch3nh+3 produce no detectable catalyitic activation at concentrations up to 100 mm. the relative potency of these cations suggests that each polypeptid ... | 1979 | 157165 |
| [distribution of highly thermophilic, nonsporulating bacteria in the hot springs of tadzhikistan]. | extreme-thermophilic non-sporeforming bacteria belonging to the thermus genus are widely distributed in hot springs (40-90 degrees c) of tadzhikistan. their content was highest (1.8-10(4)--6.0-10(4) cells per gram of ooze) in springs with the temperature of water of 50-60 degrees c, and decreased (to 8.0-10(2)--4.0-10(3) cells per gram of ooze) in springs with the same temperature of water but with a low content of ooze. the number of the cells was even less (5.0-10(2)--4.0-10(3) per gram of ooz ... | 1975 | 128687 |
| nucleotide sequence of formylmethionine trna from an extreme thermophile, thermus thermophilus hb8. | the nucleotide sequence of formylmethionine trna from an extreme thermophile, thermus thermophilus hb8, was determined by a combination of classical methods using unlabeled samples to determine the sequences of the oligonucleotides of rnase t1 and rnase a digests and a rapid sequencing gel technique using 5'-32p labeled samples to determine overlapping sequences. formylmethionine trna from t. thermophilus is composed of two species, trnaf1met and trnaf2met. their nucleotide sequences are almost ... | 1979 | 115855 |
| studies on polypeptide-chain-elongation factors from an extreme thermophile, thermus thermophilus hb8. 3. molecular properties. | molecular properties of the polypeptide chain elongation factors from thermus thermophilus hb8 have been investigated and compared with those from escherichia coli. 1. as expected, the factors purified from t. thermophilus were exceedingly heat-stable. even free ef-tu not complexed with gdp was stable after heating for 5 min at 60 degrees c. 2. gdp binding activity of t. thermophilus ef-tu was also stable in various protein denaturants, such as 5.5 m urea, 1.5 m guanidine-hcl, and 4 m licl. 3. ... | 1978 | 33049 |
| thermothrix thioparus gen. et sp. nov. a facultatively anaerobic facultative chemolithotroph living at neutral ph and high temperature. | thermothrix thioparus gen. et ep. nov. occurs naturally in a new mexico hot spring at a temperature of 74 degrees c, a ph of 7.0, and a hs- concentration of 1 mg/litre. the organism is gram-negative, non-motile, 0.5-1.0 x 3-20 mum, and forms cell chains up to 1 cm in length. the resulting filaments do not possess a sheath. sulfur is deposited extracellularly. the organism was isolated using an autotrophic medium with hs- as the energy source and no3- as the terminal electron acceptor. anaerobica ... | 1976 | 10063 |
| deoxyribonucleic acid polymerase from the extreme thermophile thermus aquaticus. | a stable deoxyribonucleic acid (dna) polymerase (ec 2.7.7.7) with a temperature optimum of 80 degrees c has been purified from the extreme thermophile thermus aquaticus. the enzyme is free from phosphomonoesterase, phosphodiesterase and single-stranded exonuclease activities. maximal activity of the enzyme requires all four deoxyribonucleotides and activated calf thymus dna. an absolute requirement for divalent cation cofactor was satisfied by mg2+ or to a lesser extent by mn2+. monovalent catio ... | 1976 | 8432 |
| purification and characterization of a repressible alkaline phosphatase from thermus aquaticus. | a repressible alkaline phosphatase has been isolated from the extreme bacterial thermophile, thermus aquaticus. the enzyme can be derepressed more than 1,000-fold by starving the cells for phosphate. in derepressed cells, nearly 6% of the total protein in a cell-free enzyme preparation is alkaline phosphatase. the enzyme was purified to homogeneity as judged by disc acrylamide electrophoresis and sodium dodecyl sulfate electrophoresis. by sucrose gradient centrifugation it was established that t ... | 1976 | 5454 |
| purification and some properties of dna-dependent rna polymerase from an extreme thermophile, thermus thermophilus hb8. | | 1975 | 2588 |
| improved growth of thermus aquaticus on cellular lysates. | studies on the thermophilic bacterium thermus aquaticus have demonstrated the ability of this organism to exist on its own cell lysates. the use of 0.1% tryptone, and 0.1% yeast extract and a mineral salts lysate medium increased growth 9-to 44-fold over the above medium without cell lysates. it has also been established in this study that, due to the high growth temperature of t. aquaticus, its metabolic activities are greatly accelerated resulting in early cell destruction. therefore, bacteria ... | 1978 | 756954 |
| biochemical studies on an extreme thermophile thermus thermophilus: thermal stabilities of cell constituents and a bacteriophage. | | 1976 | 780125 |
| [infrared spectra of extreme and obligate thermophilic bacteria of the genus thermus]. | a recording double-beam spectrophotometer ur-10 was used to obtain ir spectra of the extreme thermophilic non-sporeforming bacterium thermus flavus, the obligate thermophilic non-sporeforming bacterium thermus ruber, the thermotolerant bacterium pseudomonas thermophilus, the sporeforming bacterium bacillus stearothermophilus, and the mesophilic bacteria pseudomonas aeruginosa, ps. denitrificans, flavobacterium breve, flavobact. arborescens. no significant differences have been found in the ir sp ... | 1975 | 814383 |
| nucleotide sequence of thermus aquaticus ribosomal 5 s ribonucleic acid. sequence homologies in thermophilic organisms. | the nucleotide sequence of ribosomal 5 s rna from thermus aquaticus grown at 75 degrees is p(a)-a-u-c-c-c-c-g-c-c-c-u-u-a-g-c-g-g-c-g-u-g-g-a-a-c-a-c-c-c-g-u-u-c-c-c-a-u-u-c-c-g-a-a-c-a-c-g-g-a-a-g-u-g-a-a-a-c-g-c-g-c-c-a-g-c-g-c-c-g-a-u-g-g-u-c-a-c-u-g-g-g-a-c-c-g-c-a-g-g-g-u-c-c-u-g-g-a-g-a-g-u-a-g-g-u-g-c-u-g-g-u-g-c-g-g-g-g-a-(u). the major molecular species is 120 nucleotides long; some molecules are one or two nucleotides shorter with one less nucleotide at either or both termini. when com ... | 1977 | 863927 |
| [influence of carbon sources on the development of thermus ruber at different temperatures]. | the obligate thermophilic bacterium thermus ruber was found to grow better at 55-65 degrees c on media containing organic acids rather than sugars as a sole source of carbon. in these conditions, the morphology of the cells changes: they are rod-shaped whereas, during growth on lactose which is the best carbon source as compared to other sugars, the cells have the shape of rods in the first hours of growth but later acquire the shape of long threads. malate and pyruvate are the best carbon sourc ... | 1977 | 870802 |
| an efficient synthesis of polyguanylic acid by a thermophilic polynucleotide phosphorylase. | polyguanylic acid (poly(g)) was synthesized from gdp in a yield of 60-75% by thermus thermophilus polynucleotide phosphorylase (polyribonucleotide: orthophosphate nucleotidyltransferase, ec 2.7.7.8) at 70 degrees c, ph 8.5 in the presence of mg2+. the yield was dependent on the ratio of gdp to mg2+, but was independent of the concentrations of enzyme or substrate. the maximal rate of gdp polymerization was obtained when the ratio of gdp to mg2+ was 3:1. however, by prolonged incubation, the high ... | 1977 | 884104 |
| thermophilic polynucleotide phosphorylase from thermus thermophilus. purification and properties of an altered form of enzyme which lacks phosphorolytic activity to polynycleotide. | a thermophilic polynucleotide phosphorylase lacking polynucleotide phosphoryltic activity was purified from thermus thermophilus hb-8 strain. the enzyme is an altered form of the native polynucleotide phosphorylase, probably attacked by the proteinase(s) of this extreme thermophile during the purification process. this modified enzyme lacks phosphorolytic activity to poly(a) while retaining weak activity to phosphorolyse tetranucleotides or hexanucleotides. the purified enzyme was shown to be ho ... | 1977 | 891551 |
| [complex spherical bodies of thermus ruber]. | thermus ruber produces complex spherical bodies during its growth on liquid organic media. these bodies are similar to those formed by t. aquaticus. giant spheres of t. ruber can reach 30 mc in diameter. they may originate by two pathways: (1) from cell aggregates or (2) by local separation of the outer layer of the cell wall which accompanies bending of a cell or a bundle of cells (threads) in the form of a hook, a loop or a vibrio. in both cases, the spheres grow as a result of cell multiplica ... | 1977 | 895560 |
| [coccoid cells and spheroplasts in cultures of the genus thermus]. | the formation of capable of self-reproduction coccoid cells, and of spheroplasts, was studied in the cultures of thermus ruber and pigmentless thermus sp. by light and electron microscopy. the primary origination of cocci might be due to non-uniform or multiple cell division. spheroplasts can be produced either from coccoid or from rod-like cells as a result of autolysis of the glycopeptide layer of the cell wall. the spheroplasts of the cultures belonging to the thermus genus are characterized ... | 1977 | 909468 |
| a simple, general procedure for purifying restriction endonucleases. | a simple, general method for purifying restriction endonucleases is described. the method employs precipitation of nucleic acids from crude extracts with polyethyleneimine followed by affinity chromatography on columns of heparin covalently linked to agarose. most of the sixteen enzymes tested could be purified to a degree sufficient for dna sequencing work by this method sometimes supplemented by at most one step of ion exchange chromatography. | 1977 | 909783 |
| crystallisation of dna-dependent rna polymerase from thermus thermophilus hb 8. | | 1976 | 934322 |
| purification and properties of malate dehydrogenase from thermus aquaticus. | | 1976 | 939271 |
| purification and catalytic properties of "thermostable" fumarase from bacillus stearothermophilus nu-10 and thermus x-1. | fumarase (l-malate hydro-lysase e.c.4.2.1.2) was purified from the thermophilic bacteria bacillus stearothermophilus nu-10 (optimum growth temperature 62-63 degrees c) and thermus x-1 (optimum growth temperature 70 degrees c). the furmarase from thermus x-1 is slightly more thermostable and has an "optimum" catalytic reaction temperature of 83 degrees c as compared to 81 degrees c for the b. stearothermophilus enzyme. increased thermostability of these fumarases permitted an examination of the p ... | 1976 | 939272 |
| purification and properties of the rna polymerase of an extremely thermophilic bacterium: thermus aquaticus t2. | the rna polymerase of the extremely thermophilic bacterium thermus aquaticus t 2 has been purified to homogeneity. the apparent molecular weights of the subunits of the enzyme are : 165 000, 130000, 92 000 and 44 000. the in vitro temperature optimum of enzyme activity is around 65 degrees c. the enzyme has a preference towards the homologous template and is strongly inhibited by kci. rifampicin inhibits the enzyme only to 50% even at very high concentrations. heparin inhibits it completely, but ... | 1976 | 949494 |
| protein synthesis in a cell-free system from an extreme thermophile. effects of preincubation in the cold on polyuridylic acid-dependent polyphenylalanine synthesis at high temperature. | 1. it was found that preincubation of the reaction mixture in the cold enhanced polyuridylic acid-directed polyphenylalanine synthesis by a cell-free extract of thermus thermophilus hb8 at high temperature. 2. the effect of preincubation was most marked at 10-25 degrees in the presence of 20 mm mg2+. preincubation at 65 degrees failed to stimulate the incorporation. 3. the presence of phenylalanyl-trna, polyuridylic acid, and ribosomes was essential for preincubation in the cold to be effective. ... | 1976 | 956153 |
| heat-induced stability of trna from an extreme thermophile, thermus thermophilus. | | 1976 | 985514 |
| [research on enzymes of mycoplasma: enolase of mycoplasma hominis]. | a screening of enzymes on cell-free extracts of various species of mycoplasmas revealed the presence of enolase (ec 4.2.1.11) in significative amount in m. pneumoniae and m. fermentans, in lower amounts in m. hominis, a. laidlawii and in trace only in u. urealyticum. the value of activity of the various mycoplasmas could be correlated with their metabolism. from 40 g of cell paste of m. hominis, 2.5 mg of enolase purified over 70 folds, was obtained with successive steps of salt fractionation an ... | 1976 | 1023880 |
| extremely thermophilic gram-negative bacteria from hot tap water. | two strains of heterotrophic, non-motile, gram-negative extreme thermophiles have been isolated from hot tap water. these strains (nh and di) have been characterized and compared with strains of genus thermus. few of the single organic compounds tested supported growth in the presence of ammonium salts, and, like thermus strains, growth on undefined media was restricted to dilute tryptone-yeast extract-mineral salt solutions. nutrients agar and similar common laboratory media did not support gro ... | 1975 | 1097586 |
| [ecology of the obligate thermophilic bacteria]. | the obligate thermophilic non-sporeforming bacterium thermus ruber, isolated from the thermal springs of kamchatka at temperatures of 60 to 90 degrees c (loginova et al.,1974), has a high lytic activity towards the living and dead cells of escherichia coli and micrococcus lysodeikticus. | 1975 | 1099409 |
| novel monofunctional substrates of polynucleotide phosphorylase. the "single-addition" of 2'(3')-o-dihydrocinnamoyl-nucleoside 5'-diphosphate to a primer oligonucleotide. | a method was developed for stepwise wynthesis of oligonucleotides of difined wequence using 2'(3')-o-dihydrocinnamoyl-nucleoside 5'-diphosphates as substrates for polynucleotide phosphorylase [ed 2.7.7.8]. polynucleotide phosphorylase from thermus thermophilus catalyzed the transfer of one 2'(3')-blocked adp to the 3'-terminus of the primer trinucleoside diphosphate, apapa. the product was 2'(3')-substituted triadenylyladenosine. the blocking group, dihydrocinnamoyl, could be removed complete ... | 1975 | 1126926 |
| [new species of obligate thermophilic, nonsporulating bacteria of the genus thermus]. | | 1975 | 1133245 |
| isolation and characterization of a bacteriophage infectious to an extreme thermophile, thermus thermophilus hb8. | a bacteriophage (phiys40) infectious to an extreme thermophile, thermus thermophilus hb8, was isolated and characterized. phiys40 grows over the temperature range of 56 to 78 c, and the optimum growth temperature is about 65 c. the phage had a latent period of 80 min and a burst size of about 80 at 65 c. the phage has a hexagonal head 0.125 mum in diameter, a tail 0.178 mum long and 0.027 mum wide, a base plate and tail fibers. the phage is thermostable in broth but rather unstable in a buffer c ... | 1975 | 1142476 |
| [growth and development of extreme-thermophilic bacteria at 70 degrees]. | nine cultures of non-sporeforming gram-negative extreme-thermophilic bacterium thermus flavus have been isolated from hot springs of kamchatka. their optimal growth temperature on a solid potato medium was 70 to 76 degrees c, and on a liquid medium (20 per cent potato broth containing 0.5 per cent peptone and 0.1 per cent yeast extract) 70 degrees c. the minimum time of generation of the bacterium, strain 71, growing on the liquid medium at 70 degrees c, was 52 minutes. other extreme-thermophili ... | 1975 | 1160629 |
| [structure of trna from an extreme thermophile, thermus thermophilus (author's transl)]. | | 1975 | 1170596 |
| [thermus ruber obligate thermophilic bacteria in the thermal springs of kamchatka]. | the new species of the obligate-thermophilic bacterium thermus ruber is widely distributed in hot springs of kamchatka with the temperature of water from 57 to 90 degrees c. the bacterium does not oxidize sulphur. it contains a red carotenoid pigment similar to neuro-sporaxanthine and retrodehydro-gamma-carotene. | 1975 | 1177778 |
| thermostable polynucleotide phosphorylases from bacillus stearothermophilus and thermus aquaticus. | polynucleotide phosphorylase from bacillus stearothermophilus has been purified to homogeneity. polyacrylamide gel electrophoresis run under denaturing conditions indicates that the enzyme is a tetramer with subunits of apparent molecular weight 51,000 daltons. a partial purification of polynucleotide phosphorylase from thermus aquaticus has also been effected. the two enzymes show similar catalytic properties, which differ little from those of mesophilic polynucleotide phosphorylases. the use o ... | 1976 | 1250699 |
| occurrence of phosphenolpyruvate carboxylase in the extremely thermophilic bacterium thermus aquaticus. | in the extreme thermophile thermus aquaticus, phosphoenolpyruvate carboxylase catalyzes carbon dioxide fixation on the c3 metabolite phosphoenolpyruvate, producing oxaloacetate. in a moderately thermophilic bacillus species this function is fulfilled by pyruvate carboyxlase. like several of its mesophilic counterparts, the thermus enzyme exhibits a requirement for acetyl coenzyme a. | 1976 | 1254553 |
| resonance raman studies of rieske-type proteins. | resonance raman (rr) spectra are reported for the [2fe-2s] rieske protein from thermus thermophilus (trp) and phthalate dioxygenase from pseudomonas cepacia (pdo) as a function of ph and excitation wavelength. depolarization ratio measurements are presented for the rr spectra of spinach ferredoxin (sfd), trp, and pdo at 74 k. by comparison with previously published rr spectra of sfd, we suggest reasonable assignments for the spectra of trp and pdo. the spectra of pdo exhibit virtually no ph depe ... | 1992 | 1280165 |
| cleavage efficiencies of model substrates for ribonuclease p from escherichia coli and thermus thermophilus. | we compared cleavage efficiencies of mono-molecular and bipartite model rnas as substrates for rnase p rnas (m1 rnas) and holoenzymes from e. coli and thermus thermophilus, an extreme thermophilic eubacterium. acceptor stem and t arm of pre-trna substrates are essential recognition elements for both enzymes. impairing coaxial stacking of acceptor and t stems and omitting the t loop led to reduced cleavage efficiencies. small model substrates were less efficiently cleaved by m1 rna and rnase p fr ... | 1992 | 1281315 |
| purification and characterization of trna(adenosine-1-)-methyltransferase from thermus thermophilus hb27. | a58, the conserved adenosine residue in the t psi c loop of trnas, is methylated to m1a 58 in an extreme thermophile, thermus thermophilus hb27. the enzyme catalyzing this methyltransfer reaction was purified from the thermophle. the substrate specificity of the enzyme was investigated by using trna fragments. the enzyme can transfer the methyl group to the 3'-half fragment of e. coli initiator trna, indicating that the main recognition site of the enzyme exists in the 3' half of trna including ... | 1992 | 1289795 |
| development of plasmid cloning vectors for thermus thermophilus hb8: expression of a heterologous, plasmid-borne kanamycin nucleotidyltransferase gene. | while several thermus genes have been cloned and t. thermophilus has been shown to be transformable, molecular genetic studies of these thermophiles have been hampered by the absence of selectable cloning vectors. we have constructed a selectable plasmid by random insertion of a heterologous gene encoding a thermostable kanamycin nucleotidyltransferase activity into a cryptic, multicopy plasmid from t. thermophilus hb8. this plasmid should serve as a suitable starting point for the development o ... | 1992 | 1311546 |
| reaction of cyanide with cytochrome ba3 from thermus thermophilus: spectroscopic characterization of the fe(ii)a3-cn.cu(ii)b-cn complex suggests four 14n atoms are coordinated to cub. | cytochrome ba3 from thermus thermophilus reacts slowly with excess hcn at ph 7.4 to create a form of the enzyme in which cua, cytochrome b, and cub remain oxidized, while cytochrome a3 is reduced by one electron, presumably with the formation of cyanogen. we have examined this form of the enzyme by uv-visible, resonance raman, epr, and electron nuclear double resonance spectroscopies in conjunction with permutations of 13c- and 15n-labeled cyanide. the results support a model in which one cn- bi ... | 1992 | 1314380 |
| expression, purification, and characterization of a recombinant ribonuclease h from thermus thermophilus hb8. | thermus thermophilus ribonuclease h was overexpressed and purified from escherichia coli. the determination of the complete amino acid sequence allowed modification of that predicted from the dna sequence, and the enzyme was shown to be composed of 166 amino acid residues with a molecular weight of 18,279. the isoelectric point of the enzyme was 10.5, and the specific absorption coefficient a0.1%(280) was 1.69. the enzymatic and physicochemical properties as well as the thermal and conformationa ... | 1992 | 1315754 |
| purification and characterization of dna polymerases from bacillus species. | dna polymerases from bacillus stearothermophilus, bacillus caldotenax, and bacillus caldovelox were purified by chromatography on deae-cellulose, phosphocellulose, and heparin-sepharose and obtained in high yield. the enzyme preparations are free of exo- and endonuclease activities. additional purification steps, e.g., hydrophobic interaction chromatography and chromatography on a mono q column or sucrose density gradient centrifugation, are needed to obtain the enzymes in the form of homogeneou ... | 1992 | 1320608 |