- Volume 114, Issue 1, 1979
Volume 114, Issue 1, 1979
- Biochemistry
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Autotrophic Metabolism of Formate by Thiobacillus Strain A2
More LessSummary: Thiobacillus A2 grew on formate as its sole source of carbon and energy. Growth was autotrophic: formate and carbon dioxide were equivalent as carbon sources during growth on formate. Carbon dioxide was fixed by the Calvin cycle in formate- or thiosulphate-grown bacteria which contained comparable high specific activities of ribulosebisphosphate carboxylase. Formate incorporated by bacteria growing heterotrophically or on thio- sulphate showed more restricted metabolism, particularly providing carbon for purines. Bacteria growing on formate or thiosulphate assimilated acetate but showed disproportionately high incorporation into glutamate, proline, arginine, leucine, pyrimidines and lipid. Growth kinetics on formate were studied using extended cultures held at constant formate concentrations at pH 7·8. Yield was a function of substrate concentration and growth rate, which were linearly related in the range 4 to 40 mm-formate. Formate was an inhibitory substrate at higher concentrations. A computer analysis of the inhibited growth kinetics indicated K s and K i values of 26·5 and 187 mm-formate, respectively, and a true μ max of 0·299 h−1.
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Virulence Factors in Bacillus thuringiensis: Purification and Properties of a Protein Inhibitor of Immunity in Insects
More LessSummary: We have previously shown that Bacillus thuringiensis subsp. alesti, serotype 3, produces two extracellular inhibitors of the immune system of Saturniid pupae (designated inhibitors A and B; Edlund et al., 1976 ). Starting from the culture supernatant of a new mutant of B. thuringiensis with a decreased extracellular proteolytic activity, we have now purified immune inhibitor A (InA). The procedure described consists of three steps: ultrafiltration, precipitation with ammonium sulphate and chromatography on hydroxylapatite. Purified InA gave a single band on polyacrylamide gel electrophoresis using either a gel concentration of 7·5 % (w/v) and reducing and denaturing conditions or a gradient gel and native conditions. In both cases the apparent molecular weight was 78000. A certain amount of proteolytic activity was always co-purified with InA but the two activities could be dissociated by heat or EDTA treatment. Antiserum against purified InA gave only one sharp precipitation band on immunodiffusion against InA with or without EDTA. InA inhibited the in vitro killing of Escherichia coli by immune haemolymph but did not affect the killing of Bacillus subtilis. InA was toxic for Drosophila when injected into the abdomen of adult male flies.
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Localization of Chitin Synthase Activity in Subcellular Fractions of Schizophyllum commune Protoplasts
More LessSummary: Plasma membranes of Schizophyllum commune were stabilized against fragmentation by coating protoplasts with concanavalin A (Con A). A uniform distribution of Con A over the membrane was demonstrated cytochemically. After lysis of the protoplasts in the presence of an inhibitor of proteolysis, plasma membranes were purified and, together with other subcellular fractions, assayed for chitin synthase activity. About 50 % of the chitin synthase activity was associated with the plasma membranes and largely occurred in an active form. About 30 % of the chitin synthase, in an inactive form, was recovered in fractions sedimenting at 40000 to 300000 g The product of the plasma membrane-bound enzyme was shown to be α chitin occurring as microfibrils (about 6 nm wide). The chitin synthase could not be detached from the plasma membranes by incubation with substrate and activator at 0 °C and gradient centrifugation showed that the synthesized chitin remained associated with the plasma membranes.
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Evidence for Covalent Linkages between Chitin and β-Glucan in a Fungal Wall
More LessSummary: Covalent linkages between chitin and β-glucan in the wall of schizophyllum commune were indicated by the markedly changed solubility characteristics of the glucan when chitin was specifically removed either (i) by enzymic digestion with purified chitinase or (ii) by first deacetylating the chitin with alkali followed by depolymerization of the deacetylated chitin with nitrous acid. After depolymerization of the chitin, two types of β-glucans could be isolated: one was water-soluble and highly branched, the other was alkali-soluble with branches only one glucose unit long. Lysine (50 %) and citrulline (20 %) were the major amino acids in the R-glucan/chitin complex. By digesting 90 % of the β-glucan in the R-glucan/chitin complex with (1 → 3)-β-glucanase, a residue was obtained which, on hydrolysis with chitinase, yielded N-acetylglucosamine and a compound containing (N-acetyl) β-glucosamine, lysine and/or citrulline. A model is proposed for the R-glucan/chitin complex in which amino acids, especially lysine and citrulline, are involved in the linkages between glucan and chitin.
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Effects of d-Glutamate on Enzymes of Ammonia Assimilation in Bacillus megaterium NCIB 7581
More LessSummary: Enzymes possibly concerned in the assimilation of ammonia were assayed in Bacillus megaterium NCIB 7581 after growth with ammonium sulphate as sole source of nitrogen. Alanine dehydrogenase and aspartase were not detected, but both NADPH-dependent glutamate dehydrogenase and glutamate synthase (NADH- or NADPH-dependent) were found. Glutamine synthetase was also present, though differing methods of assay gave different values for its activity.
Glutamate dehydrogenase was competitively inhibited by d-glutamate, whereas glutamate synthase was insensitive to d-glutamate or d-glutamine (singly or together). d-Glutamate was a substrate for glutamine synthetase, and the use of l-glutamate by this enzyme was partly inhibited by a 10-fold molar excess of d-glutamate. l-Glutamine strongly inhibited glutamine synthetase, but d-glutamine had no effect
A d-glutamate-resistant substrain (grown with ammonium sulphate as nitrogen source) contained 10 times more glutamate dehydrogenase activity than did the wild-type under the same conditions, and the enzyme showed altered affinity for 2-oxoglutarate and for Dglutamate.Activities of glutamate synthase and glutamine synthetase in the substrain were similar to those in the wild-type.
Glutamate dehydrogenase was absent from organisms grown with nitrate as sole nitrogen source, yet growth under these conditions was still inhibited by d-glutamate.
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The Electron Transport System of an Extremely Thermophilic Bacterium
More LessSummary: Active, membrane-bound NADH and succinate oxidase activities with a temperature optimum of 75 °C were demonstrated in an extremely thermophilic bacterium. These were relatively stable in cell-free extracts and respiratory particles at 75 °C, but at 90 °C the half-lives of these oxidase systems were about 15 min in respiratory particles and 80 min in cell-free extracts. The stability of the NADH oxidase in respiratory particles at 90 °C was enhanced by 2 m-(NH4)2SO4, 50% (v/v) glycerol and by NADH. A number of other substrates were oxidized by the electron transport system. Respiratory particles contained cytochromes a-613, a-602, b-559, cytochrome o and at least one c-type cytochrome, c-555. The soluble fraction contained at least two c-type cytochromes, at least one of which was CO-reactive. The sensitivity of NADH and succinate oxidases to a range of inhibitors was determined.
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A Basis for Agrocin 84 Sensitivity in Agrobacterium radiobacter
More LessSummary: Agrocin 84 inhibits a virulent strain of Agrobacterium radiobacter containing a nopaline Ti plasmid, but not the same strain lacking the Ti plasmid; this specificity was investigated. Sensitivity to agrocin 84 was correlated with its active uptake by a high-affinity transport system with a K m of 5·88 × 10−8 m. Unmetabolized agrocin 84 was transported inside the sensitive strain and was associated with the soluble fraction of ruptured bacteria and not with the outer walls or cytoplasmic membrane. Agrocin 84 bound to a protein fraction isolated from the periplasmic space of the sensitive strain; there was no equivalent binding activity in the insensitive strain. It is proposed that sensitivity to agrocin 84 is due to the presence of one or more plasmid-coded binding proteins which are associated with transport of agrocin 84 into sensitive strains.
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- Ecology
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A Microscopical Investigation of the Bacterial Degradation of Wood Pulp in a Simulated Marine Environment
More LessSummary: Bleached wood pulp, derived from a mixture of Gymnosperm species, was degraded by bacteria in a laboratory model of a marine sediment. Zones of cellulolysis observed in the secondary cell walls of the pulp appeared to be due to bacterial activity. Although the bacteria were not in direct contact with the substrate, a fibrillar material associated with the bacterial cell envelope was observed by electron microscopy. Bacteria observed in the lumena of pulp cells appeared to be inactive in substrate degradation.
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- Genetics And Molecular Biology
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Application of Agarose Gel Electrophoresis to the Characterization of Plasmid DNA in Drug-resistant Enterobacteria
More LessSummary: A simple gel electrophoresis method has been described for the detection of plasmid DNA in bacteria ( Meyers et al., 1976 ). We investigated further the problems encountered in using this method for the analysis of plasmids in wild enterobacterial strains. The migration of open circular and linear plasmid DNA was examined, since these forms sometimes caused difficulty in the interpretation of the plasmid content of uncharacterized strains. Electrophoresis at different agarose concentrations was employed to resolve clearly plasmid DNA from the chromosomal DNA fragments in the crude preparations. Dissociation of some plasmids occurs in Salmonella typhimurium, and this was detected by electrophoresis. The technique was applied to the study of drug-resistant strains of S. typhimurium phage type 208 from several Middle Eastern countries. The cultures carry a drug resistance plasmid of the FI me compatibility group, and at least two other plasmids which were detected and identified by gel electrophoresis. The studies supported and extended the genetic findings and provided information on the distribution of particular plasmids.
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Genetics of Actinorhodin Biosynthesis by Streptomyces coelicolor A3(2)
More LessSummary: A series of 76 mutants of Streptomyces coelicolor A3(2) specifically blocked in the synthesis of the binaphthoquinone antibiotic actinorhodin were classified into seven phenotypic classes on the basis of antibiotic activity, accumulation of pigmented precursors or shunt products of actinorhodin biosynthesis, and cosynthesis of actinorhodin in pairwise combinations of mutants. The polarity of cosynthetic reactions, and other phenotypic properties, allowed six of the mutant classes to be arranged in the most probable linear sequence of biosynthetic blocks. One member of each mutant class was mapped unambiguously to the chromosomal linkage map in the short segment between the hisD and guaA loci, suggesting that structural genes for actinorhodin biosynthesis may form an uninterrupted cluster of chromosomal genes.
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Molecular Basis of Altered Enzyme Specificities in a Family of Mutant Amidases from Pseudomonas aeruginosa
More LessSummary: A family of mutant amidases has been derived by experimental evolution of the aliphatic amidase of Pseudomonas aeruginosa strain PAC1. Mutation amiE16, in the structural gene for the enzyme, results in the production of the mutant B amidase by strain B6. This strain, unlike the wild-type, can utilize butyramide for growth. Strain B6 gave rise by a single mutational event to strain V9, utilizing valeramide, and strain PhB3, utilizing phenylacetamide. Strain V9 was not itself able to utilize phenylacetamide but gave rise by mutation to the phenylacetamide-utilizing mutant PhVI. Peptide 108 was isolated from chymotryptic digests of mutant amidases from strains B6, PhB3 and PhV1, but could not be detected in chymotryptic digests of the wild-type amidase. The sequence of peptide 108 was established as Met-Arg-His-Gly-Asp-Ile-Phe. Thermolytic digests of mutant amidases from strains B6, PhB3, PhV1 and V9 were compared with digests of the wild-type amidase. A peptide of the composition Met, Arg, His, Gly2, Asp3, Ile, Ser3, Thr, Val was found in the digest of the wild-type amidase and was replaced in the digests of the mutant amidases by a peptide of the composition Met, Arg, His, Gly2, Asp3, Ile, Ser2, Thr, Val, Phe. Mutation amiE16 is common to the four mutant enzymes and can be accounted for by the mutation Ser →Phe. The sequence of the chymotryptic peptide corresponds with the N-terminal sequence of the amidase protein, and can also be related to the thermolysin peptides. It is concluded that mutation amiE16 is a Ser the change at position 7 from the N-terminus and the effect of this on the enzyme conformation is discussed.
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- Medical Microbiology
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Differential Neutralization of Spontaneous and Centrifuge-assisted Chlamydial Infectivity
More LessSummary: Neutralization by specific antibody of a fast-killing variant strain of Chlamydia trachomatis, which showed high spontaneous infectivity for cell monolayers, was examined. It appeared that in spontaneous infection antibody-treated chlamydiae were neutralized by inhibition of attachment to cells. Centrifugation imposed a different effect: infection was inhibited at some step at or subsequent to attachment.
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Wall-associated Protein Antigens of Streptococcus mutans
More LessSummary: When heat-killed whole organisms of Streptococcus mutans strain Ingbritt (serotype c) were injected into rabbits, antibodies to at least 12 antigens were detectable by crossed immuno-electrophoresis. In contrast, when rabbits were immunized with organisms which had been subjected to extraction with the detergent sodium dodecyl sulphate (SDS), antibodies to only two protein antigens were found. These two proteins (A and B), while existing in a form apparently closely associated with peptidoglycan, could also be recovered from homogenates of whole organisms after sonication and from culture filtrates. Antigenic material was excreted throughout growth. SDS-polyacrylamide gradient gel electrophoresis showed A to have a molecular weight of 29000, while B had a molecular weight of 190000. Antigen B was purified to apparent homogeneity as judged by SDS-polyacrylamide gel electrophoresis and isoelectric focusing. All of six strains of serotype c examined produced antigen B. Strains of serotypes e and f also produce antigenically identical proteins and strains of serotypes d and g produce proteins which cross-reacted with antigen B. Antigen B was specifically precipitated by rabbit antiserum to human heart tissue.
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Phenotypically Determined Resistance of Neisseria gonorrhoeae to Normal Human Serum: Environmental Factors in Subcutaneous Chambers in Guinea Pigs
More LessSummary: Some gonococci obtained from human urethral exudate or from subcutaneously implanted chambers in guinea pigs show a resistance to killing by human serum which is lost on subculture in vitro after a few generations. The environmental factors which may influence the phenotypic expression of resistance to serum killing were investigated in guinea pig chambers and in chamber fluid in vitro.
The redox potential in chambers before and after infection was lower than that of heart blood but conditions were not anaerobic; H2O2 increased the redox potential but did not decrease gonococcal serum resistance. The chambers were slightly alkaline before and after infection. When the concentration of glucose (depleted in infected chambers by the abundant polymorphonuclear cells) was restored to excess, the serum resistance of the gonococci was unaffected. Concentrations of free amino acids in chambers changed little during infection. Gonococci adapted to growth in chambers and subsequently rendered serum-sensitive by growing once on agar reverted to serum-resistance after 0·5 to 1 h incubation in chamber fluid in vitro at 37 0C but not at 25 °C or 4 °C. After 16 to 24 h growth at 37 °C, resistance was again lost. The reversion to serum resistance did not occur in a complex laboratory medium. Examination of the chamber fluid after growth of gonococci in vitro showed depletion of lactate, glutamine and proline.
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- Physiology And Growth
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Morphology and Growth of a Temperature-sensitive Mutant of Aspergillus nidulans which Forms Aseptate Mycelia at Non-permissive Temperatures
More LessA study was made of the morphology and growth of young mycelia of a temperature-sensitive mutant (sepA2) of Aspergillus nidulans. At 25 °C the mutant grew at the same rate as the parental strain, formed septa and branched normally. At 30 and 37 °C the mutant grew at about three-quarters of the rate of the parental strain and, unlike the parental strain, branched dichotomously. The mutant was aseptate at 37 °C, and at 30 °C produced fewer septa than the parental strain. No septal initials were detected in mutant mycelia grown at 37 °C. Aseptate mycelia of the mutant were grown at 37 °C and then transferred to 25 °C. After transfer to 25 °C, septa appeared parasynchronously throughout aseptate regions of the mycelium previously formed at 37 °C. The intercalary compartments formed in this manner had a mean length which was identical with those of intercalary compartments formed by the parental strain at 37 °C or the mutant at 25 °C. The lag between transfer of mutant mycelia from 37 to 25 °C and the first appearance of septa varied from 0·15 to 2·75 h; the maximum lag observed was similar to the organisms’s doubling time (2·37 h) at 25 °C.
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Regulation of Glucosyl- and Fructosyltransferase Synthesis by Continuous Cultures of Streptococcus mutans
More LessSummary: Streptococcus mutans strain Ingbritt, and its derivative B7 which had been passaged through monkeys, have been used to investigate how the synthesis of extracellular glucosyl- and fructosyltransferases is regulated. The most active enzyme from carbon-limited continuous cultures was a fructosyltransferase; enzymes catalysing the formation of water-insoluble glucans from sucrose were relatively inactive. Dextransucrase (EC 2.4.1.5), which catalyses soluble glucan synthesis, was most active in the supernatant fluid from cultures grown with excess glucose, fructose or sucrose, but full activity was detected only when the enzyme was incubated with both sucrose and dextran. Little dextransucrase activity was detected in carbon-limited cultures. It is concluded that glucosyl- and fructosyltransferases are constitutive enzymes in that they are synthesized at similar rates during growth with an excess of the substrate or of the products of the reactions which they catalyse. Although the Ingbritt strain was originally isolated from a carious lesion, it is now a poor source of glucosyltransferase activity. Glucosyltransferases were extremely active in cultures of a recent clinical isolate, strain 3209, and were apparently induced during growth with excess glucose.
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The Growth of Pseudomonas putida on Chlorinated Aliphatic Acids and its Dehalogenase Activity
More LessSUMMARY: Two strains of Pseudomonas putida, S3 and P3, were shown to contain dehalogenase activity against monochloroacetate, dichloroacetate, 2-monochloropropionate and 2,2′-dichloro-propionate but differed markedly in their levels of enzyme activity. Strain S3 had activities of less than 1 μmol substrate converted (mg protein)−1 h−1 and was unable to grow on any of nine chlorinated compounds tested. Strain P3 had enzyme activities 10 to 40 times greater than those of strain S3 but was capable of growth only on 2-monochloropropionate and 2,2′-dichloropropionate. In strain P3, dehalogenase activity was induced by a number of chlorinated compounds other than those that acted as growth substrates. Strain P3 dehalogenase activity dehalogenated C-2 substituted compounds. The evidence of the dehalogenase activity profiles in chemostat cultures and from thermal denaturation experiments suggested that there was more than one dehalogenase enzyme in P. putida strain P3. In crude extract, the enzyme activity was optimal at pH 7·9 to 8·1 and apparent K m values were in the millimolar range for the four major substrates, monochloroacetate, dichloroacetate, 2-monochloropropionate and 2,2′-dichloropropionate.
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Inhibition by d-Glutamate as the Cause of Diphasic Growth of Bacillus megaterium NCIB 7581 with Glycerol plus dl-Glutamic Acid
More LessSUMMARY: Growth of Bacillus megaterium NC1B 7581 in a simple chemically defined medium was inhibited by d-glutamate above 0·01 mg ml−1; equimolar l-glutamate prevented this inhibition. When dl-glutamate (2 mg ml−1) was present in the medium (with glycerol as the main carbon source), organisms grew exponentially until all the l-isomer had disappeared; growth then stopped for about 24 h during which there was a transient appearance of d-glutamine in the medium. Throughout the first stationary phase the concentration of d-glutamate in the medium fell continuously and when it was less than 0·01 mg ml−1 there was a second phase of growth.
Exponential phase organisms growing without glutamate contained only 4 mm-glutamate in the free amino acid pool. During the first stationary phase with d l-glutamate added to the medium, the concentration of glutamate (all d-isomer) was 47 mm in the pool.
Of four other strains of B. megaterium tested, only one was sensitive to d-glutamate. From strain 7581 a d-glutamate-resistant substrain was easily developed. Among other amino acids added singly to the defined medium, only d- (and l-) serine was inhibitory to all five strains examined. Inhibition of B. megaterium 7581 by d-glutamate was prevented by single addition of several amino acids, each of which could act as a sole source of nitrogen for growth.
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Peptide Transport in Candida albicans
More LessSummary: The tripeptide l-methionyl-l-methionyl-l-[methyl -14C]methionine was taken up into Candida albicans by a saturable system with a pH optimum of 3·5, a temperature optimum of 37 °C and an apparent K m of 33· 10−5 M. Metabolic inhibitors such as sodium azide and dinitrophenol completely prevented uptake. Neither methionine nor dimethionine effectively competed with trimethionine uptake. (Leu)3, Gly-Met-Gly, acetyl-(Met)3, D-Met-l-Met-l-Met and Met-Met-Ile effectively competed with (Met)3 uptake, whereas (Lys)3, l-Met-l-Met-d-Met, d-Met-d-Met-d-Met, (Met)3 methyl ester and (Ala)3 did not. Trimethionine was rapidly hydrolysed by a peptidase after entry into the cell.
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Isolation and Characterization of Methane-utilizing Yeasts
More LessSummary: Five yeast strains capable of utilizing CH4 as the sole energy source for growth have been isolated using selective enrichments for methanotrophic micro-organisms. One of the pure cultures was selected for single-cell isolations and antibiotic screening to verify more rigorously the purity of the methanotrophic yeast cultures. Examination of the ultrastructure of this isolate confirmed its eukaryotic nature. The rates of CH4 oxidation by the isolates were determined by assaying whole cell suspensions for CH4-dependent oxygen consumption in an oxygen electrode and by measuring the conversion of 14CH4 to 14CO2 and incorporation of 14C into cellular material by whole cells. Characterization of the isolates suggests that four different species of yeast have been obtained that are capable of utilizing CH4
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