- Volume 137, Issue 7, 1991
Volume 137, Issue 7, 1991
- Review Article
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- Biochemistry
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Kinetic properties of ribulose bisphosphate carboxylase/oxygenase from Thiobacillus thyasiris, the putative symbiont of Thyasira flexuosa (Montagu), a bivalve mussel
More LessSome kinetic properties of ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase from Thiobacillus thyasiris, a marine, facultatively heterotrophic, sulphur-oxidizing bacterium and putative symbiont of Thyasira flexuosa (Montagu), a bivalve mussel, have been determined. The kinetic parameters for the CO2/Mg2+-activated enzyme were: K m(RuBP) 24·3 μm, K m(CO2) 125·5 μm, Km(O2) 900 μm and K m(Mg2+) 1·53 mm. The low CO2 affinity suggests that T. thyasiris may possess a CO2-concentrating mechanism. RuBP oxygenase activity was inhibited by increasing CO2 concentration. Divalent metal ions were essential for RuBP carboxylase activity; activity of the Mg2+-free enzyme could be restored by the addition of Mg2+, Mn2+ or Ca2+. The pH optimum was 7·8. The temperature optimum for RuBP carboxylase activity was 55 °C, although the enzyme rapidly lost activity at this temperature. An Arrhenius plot was biphasic, with a break at 40 °C. The activation energies were 55·5 × 103 J mol−1 and 32·9 × 103 J mol−1 over the temperature ranges 10–40 °C and 40–55 °C, respectively. Q 10 was 2·12 for any 10 °C increment between 10·40 °C, and 1·47 between 40·55 °C. RuBP carboxylase activity was stable at 35 °C, the optimum growth temperature of T. thyasiris and at 7·5 °C, the temperature of the habitat of Thyasira flexuosa, but the activity was 40% and 3·5%, respectively, of the potential activity at 55 °C. RuBP carboxylase activity was stimulated by NaCl concentrations of up to 0·3 m, with a maximum (33 %), occurring between 0·1 and 0·2 m-NaCl. At higher concentrations of NaG (>0·3 m) RuBP carboxylase activity was inhibited
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Glycerol utilization in Fusarium oxysporum var. lini: regulation of transport and metabolism
More LessGlycrol was transported in the fungus Fusarium oxysporum var. lini by a facilitated diffusion transport system with a half-saturation constant, K s, of 0·5 mm and a maximum velocity, V max, of 0·9 mmol (g dry wt)−1 h−1 at pH 5 and 25 °C. 1,2-Propanediol was a competitive inhibitor of glycerol transport, but the cells did not actively accumulate 1,2-propanediol. The transport system was partially constitutive. In cells grown in the presence of glucose, glycerol was not transported, indicating that the synthesis of the system was under glucose repression. Glycerol kinase and NADP+-dependent glycerol dehydrogenase activities were present under all physiological conditions tested. A flavin-dependent glycerol phosphate dehydrogenase was induced only when glycerol was the sole energy source in the medium. This enzyme, together with the transport system, constitute the regulated steps in the glycerol metabolic pathway.
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Immunological relationships between glucosyltransferases synthesizing insoluble glucan from Streptococcus cricetus, Streptococcus sobrinus and Streptococcus downei
More LessSummary: The M r values and isoelectric points of glucosyltransferases synthesizing insoluble glucan (GTF-Is) were determined, and the immunological relationships between them studied. The GTF-I enzymes were from Streptococcus cricetus (mutans group serotype a), Streptococcus sobrinus (mutans group serotypes d and g) and Streptococcus downei (mutans group serotype h). By double immunodiffusion tests, the GTF-I enzymes from the three species possessed a common antigenic determinant; in addition, the GTF-I enzymes of serotypes d, g and h shared a further determinant. The S. sobrinus serotypes d and g GTF-I enzymes were immunologically identical. The GTF-I enzymes of S. sobrinus serotypes d and g, and of S. downei, had an M, of 161000 and isoelectric points of 4·8-4·9, while S. cricetus GTF-I had a lower M r (150000) and a higher isoelectric point (5·2). This suggests that the S. cricetus GTF-I enzyme may lack a sequence of amino acids which include the determinant shared by S. sobrinus and S. downei GTF-I enzymes. Antibodies specific to the determinant shared by all four serotypes inhibited the homologous and heterologous enzymes by 94-100%.
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Purification and characterization of the free form of the lactococcal extracellular proteinase and its autoproteolytic cleavage products
More LessSummary: In addition to the cell wall proteinase, Lactococcus lactis subsp. cremoris produced significant amounts of a free extracellular proteinase. The free proteinase activity was highest in the late exponential and early stationary phase of growth, whereas the cell wall activity was highest in the last half of the exponential phase. Both proteinase forms had a pH optimum between 4·6 and 5·8, and they behaved similarly upon anion exchange and hydrophobic interaction chromatography, chromatofocusing and gel filtration, indicating that they were related. Purification to homogeneity, as judged by SDS-PAGE, resulted in a 50000-80000-fold increase in the specific activity of the free proteinase. It contained two major protein species (termed pro150 and pro115) with proteinase activity. As judged by SDS-PAGE, the M r values of pro150 and pro115 were 150000 and 115000, respectively, and by chromatofocusing the isoelectric points were 4·3 and 4·1, respectively. Upon gel filtration, pro150 and pro115 had M r values of 300000 and 125000, respectively, indicating that pro150 was a dimer and pro115 a monomer. Pro115 was an autodegradation product of pro150. Other distinct autodegradation products had M r values of 90000 (p90), 53000 (p53), 37000 (p37) and 30000 (p30). These had little if any proteinase activity. Pro115, p90 and p53 had a common N-terminal sequence with that reported for the cell wall proteinase. Judging from its N-terminal sequence and M r, p30 was derived from the C-terminal half of p53. Cleavage of pro150 to pro115 generated p37.
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Purification and some characteristics of a calcium-binding protein from Bacillus cereus spores
More LessSummary: A novel calcium-binding protein has been purified from the dormant spores of Bacillus cereus T. Purity of this protein was verified by SDS-PAGE and reversed-phase HPLC. Its calcium-binding ability was verified by a competitive calcium-binding assay using Chelex-100 resin and 45Ca autoradiography. The protein is heat-stable and is retained by hydrophobic matrices (phenyl-Sepharose) in a calcium-dependent manner. SDS-PAGE and amino acid composition indicate the molecular mass of the protein to be 24 kDa.
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Phosphatidyltransferase activity in Bacillus megaterium
More LessSummary: Phosphatidyl transfer between phosphatidylethanolamine, phosphatidylglycerol or phosphatidylserine as donors and primary hydroxyl acceptors including ethanolamine, glycerol, serine and Triton X-100 has been shown to be catalysed by membrane particles derived from Bacillus megaterium strains ATCC 13632 and ATCC 14581. The rate of cardiolipin synthesis from phosphatidylglycerol in the presence of ethanolamine was an order of magnitude greater than that of phosphatidylethanolamine formation. Cardiolipin synthesis from phosphatidylethanolamine in the presence of glycerol was also observed, and was 1·5-fold greater than the formation of phosphatidylglycerol. Similar heat lability, effects of pH and of Triton X-100 for phosphatidyl transfer and cardiolipin synthesis indicate that both reactions were catalysed by cardiolipin synthase.
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Purification and some properties of carboxynorspermidine synthase participating in a novel biosynthetic pathway for norspermidine in Vibrio alginolyticus
More LessSummary: Carboxynorspermidine synthase, mediates the nicotinamide-nucleotide-linked reduction of the Schiff base H2N(CH2)3N = CHCH2CH(NH2)COOH. This is formed from l-aspartic β-semialdehyde (ASA) and 1,3-diaminopropane (DAP) and is reduced to carboxynorspermidine [H2N(CH2)3NH(CH2)2CH(NH2)COO H], an intermediate in the novel pathway for norspermidine (NSPD) biosynthesis. The enzyme was purified to apparent homogeneity from Vibrio alginolyticus and characterized. The overall purification was about 1800-fold over the crude extract, with a yield of 33%. The enzyme displayed an apparent M r of 93500 ± 1000 by gel filtration and 45100 ± 500 by SDS-PAGE, indicating that the native form is probably composed of two subunits of similar size. The specific activity of the purified enzyme was 31·0 μmol carboxynorspermidine produced min–1 (mg protein)–1. The enzyme was activated by dithiothreitol, and inhibited by SH-reactive compounds. The pH and temperature optima were 7·25–7·5 and 37 °C, respectively. The K m value for the Schiff base was 4·68 mm, measured by varying the ASA concentration while keeping the DAP concentration constant. Putrescine was slightly active as a substrate, forming carboxyspermidine (at about 7% of the rate of DAP), but ethylenediamine, cadaverine and d-ASA were inert. The K m value for NADPH was 1·51 mm. NADH was a much poorer cofactor than NADPH. When V. alginolyticus was grown in the presence of 5 mm-NSPD, the specific activity of this enzyme was reduced by ~ 70%. NSPD also repressed two other enzymes responsible for its biosynthesis, 2,4-diaminobutyrate decarboxylase and carboxynorspermidine decarboxylase.
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- Development And Structure
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Wheat germ agglutinin binding proteins in the cellular slime moulds Dictyostelium and Polysphondylium
More LessSummary: Analysis of the wheat germ agglutinin (WGA) binding proteins in the cellular slime moulds Dictyostelium mucoroides, D. rosarium, D. purpureum, Polysphondylium violaceum and P. pallidum revealed many cell-type specific proteins in each species examined. Furthermore, three species D. mucoroides, D. rosarium and P. violaceum, were found to have a wst34-like protein in their stalk cells. Wst34, which was originally identified in D. discoideum, is a stalk-specific WGA-binding protein having a molecular mass of 34 kDa and pI values of between 5·5 and 6·5.
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- Ecology
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DNA polymorphisms in new isolates of ‘Deinococcus radiopugnans’
More LessNineteen new Deinococcus isolates from soil, 18 of which were from samples immediately adjacent to a lake in Nottingham, UK, were characterized by conventional criteria, and found to be identical to each other and to conform most closely to the species D. radiopugnans. However, we detected three different restriction enzyme activities in three different isolates. Because of this suggestion of heterogeneity, we examined the isolates for restriction fragment length polymorphisms (RFLPs). RFLP analysis of the 19 original isolates, using three different probes, distinguished 17 divergent groups. This extraordinary diversity cannot be attributed to geographical differences, nor to the method of isolation, which employed UV-radiation selection.
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Description of two anaerobic fungal strains from the bovine rumen and influence of diet on the fungal population in vivo
More LessSummary: Neocallimastix sp. NC71 and Piromyces sp. PC12 isolated from the calf rumen grew optimally at 39 °C and pH 6·5–6·7, utilized a wide range of mono-, oligo- and polysaccharides and exhibited CMCase, Avicelase, cellobiase, amylase and xylanase activities. The end-products of wheat straw fermentation by both strains were acetate, formate, ethanol and lactate. The number of Neocallimastix sp. zoospores in the rumen of cows in the first 3h after feeding with hay-silage-concentrate diets varied from 7 × 103 to 5·4 × 105 ml−1; the number of uniflagellate zoospores varied from 104 to 105 ml−1. Fungal zoosporogenesis and colonization of plant substrates in the rumen were induced by feed intake and were favoured by increased levels of crude fibre in the diet.
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- Genetics And Molecular Biology
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Sequence and structural organization of a nifA-like gene and part of a nifB-like gene of Herbaspirillum seropedicae strain Z78
More LessSummary: The deduced amino acid sequence derived from the sequence of a fragment of DNA from the free-living diazotroph Herbaspirillum seropedicae was aligned to the homologous protein sequences encoded by the nifA genes from Atorhizobium caulinodans, Rhizobium leguminosarum, Rhizobium meliloti and Klebsiella pneumoniae. High similarity was found in the central domain and in the C-terminal region. The H. seropedicae putative NifA sequence was also found to contain an interdomain linker similar to that conserved among rhizobial NifA proteins, but not K. pneumoniae or Azotobacter vinelandii. Analysis of the regulatory sequences found 5′ from nifA indicated that the expression of this gene in H. seropedicae is likely to be controlled by NifA, NtrC and RpoN, as judged by the presence of specific NifA- and NtrC-binding sites and characteristic −24/−12 promoters. Possible additional regulatory features included an ‘anaerobox’ and a site for integration host factor. The N-terminus of another open reading frame was found 3′ from nifA and tentatively identified as nifB by amino acid sequence comparison. The putative nifB promoter sequence suggests that expression of H. seropedicae nifB may be activated by NifA and dependent on RpoN.
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Cloning, characterization and taxonomic significance of genes for the 5S ribosomal RNA of Leptonema illini strain 3055
More LessSummary: The genes encoding the 5S ribosomal RNA (rRNA) for Leptonema illini strain 3055 were isolated and sequenced. The 5S RNA molecule encoded was 117 nucleotides long. The genome of strain 3055 contained two genes for 5S rRNA that were located close together. The nucleotide sequences of the Leptonema illini genes exhibited less similarity to the rRNA gene of Leptospira interrogans strain Moulton and also to those of typical eubacterial genes than did the rRNA genes of other leptospires. However, the overall secondary structure of the 5S rRNA encoded exhibited a strong similarity to that of typical eubacterial 5S rRNA. Southern hybridization of the 5S rRNA gene probe with the genomic DNA of strain 965, which is currently classified as Leptospira biflexa, showed the latter to have close similarity to that of strain 3055. The physical map of strain 965 was quite similar to that of strain 3055 and was greatly different from that of any other strains of L. biflexa. In the organization of 5S rRNA genes, strain 965 is sufficiently different from other members of the genus Leptospira to be regarded as a member of the genus Leptonema.
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Molecular analysis of a Leptospira borgpetersenii gene encoding an endoflagellar subunit protein
More LessSummary: A flagellin gene, flaB, from Leptospira borgpetersenii (formerly L. interrogans) serovar hardjo was cloned and expressed in Escherichia coli. Expression of the 32 kDa FlaB protein was dependent upon the lacZ promoter from pUC18. Nucleotide sequence data showed an open reading frame encoding 283 amino acid residues, corresponding to a protein of molecular mass 31·3 kDa. The G + C content of the flaB gene was 54·7 mol%. Comparison of the deduced FlaB amino acid sequence with flagellins from other bacteria revealed a high level of identity with the Treponema pallidum FlaB proteins.
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Isolation and structural analysis of the laccase gene from the ligninegrading fungus Phlebia radiata
More LessSummary: We have isolated and characterized a gene coding for the laccase of the lignin-degrading fungus Phlebia radiata. The gene has nine introns and recognizable fungal promoter elements. Sequences homologous to the consensus eukaryotic heat-shock regulatory element can be found in the promoter. RNA hybridization results indicate that this gene is regulated at the transcriptional level. The derived laccase amino acid sequence shows homology to plant ascorbate oxidases, suggesting that the basic structure of the laccase is similar to the three-fold repeated β-barrel of the ascorbate oxidases. Potential copper ligands and a residue carrying the prosthetic group pyrroloquinoline quinone (PQQ) in the laccase protein can be identified by homology. The intron/exon structure of the laccase gene suggests that this protein could have evolved by exon shuffling.
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Induction and partial purification of bacteriophages from Desulfovibrio vulgaris (Hildenborough) and Desulfovibrio desulfuricans ATCC 13541
More LessSummary: Bacteriophages were induced from cultures of Desulfovibrio vulgaris NCIMB 8303 and Desulfovibrio desulfuricans ATCC 13541 by UV light. The optimum time of UV exposure was 1 min and the maximum yield of phage was obtained 9-10 h after UV treatment. The two phage preparations were compared by restriction enzyme analysis and Southern blot hybridization. The nucleic acid from both phages was cut by restriction endonucleases specific for double-stranded DNA. The phage DNAs from D. vulgaris and D. desulfuricans showed different restriction enzyme cleavage patterns. No homology was observed between a 25 kb probe from the D. vulgaris phage DNA and the phage DNA from D. desulfuricans. Protein profiles of the phages from both sources were also studied; the D. vulgaris phage contained two major bands corresponding to Mr values of 37000 and 56000 while the D. desulfuricans phage contained only one major band, of M r 38000.
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Photosynthetic genes in Rhodobacter capsulatus can be regulated by oxygen during dark respiratory growth with dimethylsulphoxide
More LessSummary: In the purple non-sulphur bacterium Rhodobacter capsulatus, genes encoding structural polypeptides of the lightharvesting (LH) and reaction center (RC) complexes incorporated into an intracytoplasmic photosynthetic membrane are induced upon lowering the oxygen tension in the media of aerobically growing cultures. When cultures are grown microaerophilically in the dark, an intracytoplasmic photosynthetic membrane develops gratuitously if a terminal oxidant, such as dimethylsulphoxide (DMSO) is present in the medium. The purpose of the present study was to determine whether in these conditions, photosynthetic genes are completely derepressed or whether they are still inducible in response to a lowering of oxygen tension. Oxygen induction of mRNA for the puf and puc operons was compared in dark aerobic cultures (20% O2) shifted to low oxygen conditions (3% O2) allowing growth microaerophilically with or without DMSO as an accessory terminal oxidant. The extent of the induction was similar in both growth conditions, 6 to 12-fold for pufA mRNA and at least 400-fold for pucB mRNA which encode the light-harvesting I (LHIα) and light-harvesting II (LHIIβ) polypeptides, respectively. The puf and puc operons were also induced by low oxygen tension in a mutant strain blocked in an early step of bacteriochlorophyll (BChl) synthesis, suggesting that the presence of BChl may not be a prerequisite for the normal oxygen regulation of the genes encoding the structural polypeptides of the photosynthetic apparatus.
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Chlamydia trachomatis major outer membrane protein epitopes expressed as fusions with LamB in an attenuated aroA strain of Salmonella typhimurium; their application as potential immunogens
More LessSummary: The major outer-membrane protein (MOMP) of Chlamydia trachomatis is the focus of attention for chlamydial vaccine design, particularly those serovar- and subspecies-specific epitopes which provoke neutralizing immune responses. Selected surface-exposed B-cell epitopes of MOMP, incorporating B-subspecies specificities, were expressed as fusions with LamB, an inducible outer-membrane transport protein of Escherichia coli. These recombinant chlamydial-LamB proteins were correctly transported to the outer membrane of both E. coli and an aroA mutant of Salmonella typhimurium. The immunogenicity of the constructs was investigated in a mouse model of chlamydial salpingitis. After oral immunization, recombinant S. typhimurium were recovered from the livers of mice for up to two weeks, and a serum IgG response was induced both to the Salmonella and to the inserted chlamydial epitopes. By contrast, intravenous inoculation was ineffective. Although these LamB fusions proved only weakly immunogenic, this approach should be useful for investigating the ability of attenuated S. typhimurium vaccines incorporating chlamydial epitopes to stimulate protective mucosal immunity in the mouse model of chlamydial salpingitis.
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A Rhizobium leguminosarum gene required for symbiotic nitrogen fixation, melanin synthesis and normal growth on certain growth media
More LessThe gene nfrX in Azotobacter vinelandii activates transcription of other nif genes in that species. A cosmid containing cloned Rhizobium leguminosarum DNA that corrected the Nif- defect of an nfrX mutant of A. vinelandii was isolated. Following Tn5 transposon mutagenesis of the cosmid in Escherichia coli, mutant derivatives unable to correct the A. vinelandii nfrX mutants were obtained in two separate regions of DNA. In addition, mutations close to one of the nfrX regions conferred a complex phenotype when introduced into the Rhizobium genome by marker exchange. These mutants induced non-fixing nodules on peas, were slow-growing on media with succinate as C source or nitrate as N source and, when present in R. leguminosarum biovar phaseoli, they failed to make melanin, a pigment that is normally synthesized by R. l. bv. phaseoli. The mutated gene, termed melC, was fused to uidA (which encodes β-glucuronidase); it was found that transcription of melC-uidA was enhanced in microaerobic conditions and that it was expressed at high levels in infection threads in pea nodules.
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Nucleotide sequence and characteristics of endoglucanase gene engB from Clostridium cellulovorans
More LessSummary: An endoglucanase gene, engB, from Clostridium cellulovorans, previously cloned into pUC19, has been further characterized and its product investigated. The enzyme, EngB, encoded by the gene was secreted into the periplasmic space of Escherichia coli. The enzyme was active against carboxymethylcellulose, xylan and lichenan but not Avicel (crystalline cellulose). The sequenced gene showed an open reading frame of 1323 base pairs and coded for a protein with a molecular mass of 48·6 kDa. The mRNA contained a typical Gram-positive ribosome-binding site sequence GGAGG and a sequence coding for a putative signal peptide. There is high amino acid and base sequence homology between the N-terminal regions of EngB and another C. cellulovorans endoglucanase, EngD, but they differ significantly in their C-termini. Deletion analyses revealed that up to 32 amino acids of the N-terminus and 52 amino acids of the C-terminus were not required for catalytic activity. The conserved reiterated domains at the C-terminus of EngB were similar to those from endoglucanases from other cellulolytic bacteria. According to our deletion analyses, this region is not needed for catalytic activity.
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