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Expression from the nifB promoter of Azotobacter vinelandii can be activated by NifA, VnfA, or AnfA transcriptional activators.

In Azotobacter vinelandii, nifB is required for the activity of all three nitrogenases. Expression of a nifB-lacZ fusion was examined to determine which regulatory gene products are important for nifB expression and how its transcription is regulated in response to metals. In all conditions, expression in A. vinelandii was eliminated by an rpoN mutation, confirming the absolute requirement for sigma N. In the wild type, nifB-lacZ expression was approximately twofold higher in cells grown with Mo than without. Expression was negligible in a nifA mutant grown with Mo but was much higher in Mo-free medium, suggesting that in these conditions, another sigma N-dependent activator was responsible for nifB expression, possibly VnfA, AnfA, or NtrC. Although expression of the nifB-lacZ fusion in A. vinelandii vnfA, anfA, and ntrC mutants was little different from that in the wild type, nifB transcription could be activated by NifA, VnfA, or a truncated form of AnfA in Escherichia coli. The two potential NifA binding sites centered at -87 and -129 bp upstream of the transcription start site each overlapped a VnfA recognition sequence, motifs also found in Azotobacter chroococcum in two exactly conserved regions. Deletion analysis showed that both regions are important for nifB expression. Activation of the full-length promoter by AnfA was impaired by overexpressing the DNA-binding domain of NifA, suggesting that binding of NifA and AnfA can be competitive.

Azotobacter vinelandii↗

Purification and characterization of 2,4,6-trichlorophenol-4-monooxygenase, a dehalogenating enzyme from Azotobacter sp. strain GP1.

The enzyme which catalyzes the dehalogenation of 2,4,6-trichlorophenol (TCP) was purified to apparent homogeneity from an extract of TCP-induced cells of Azotobacter sp. strain GP1. The initial step of TCP degradation in this bacterium is inducible by TCP; no activity was found in succinate-grown cells or in phenol-induced cells. NADH, flavin adenine dinucleotide, and O2 are required as cofactors. As reaction products, 2,6-dichlorohydroquinone and Cl- ions were identified. Studies of the stoichiometry revealed the consumption of 2 mol of NADH plus 1 mol of O2 per mol of TCP and the formation of 1 mol of Cl- ions. No evidence for membrane association or for a multicomponent system was obtained. Molecular masses of 240 kDa for the native enzyme and 60 kDa for the subunit were determined, indicating a homotetrameric structure. Cross-linking studies with dimethylsuberimidate were consistent with this finding. TCP was the best substrate for 2,4,6-trichlorophenol-4-monooxygenase (TCP-4-monooxygenase). The majority of other chlorophenols converted by the enzyme bear a chloro substituent in the 4-position. 2,6-Dichlorophenol, also accepted as a substrate, was hydroxylated in the 4-position to 2,6-dichlorohydroquinone in a nondehalogenating reaction. NADH and O2 were consumed by the pure enzyme also in the absence of TCP with simultaneous production of H2O2. The NH2-terminal amino acid sequence of TCP-4-monooxygenase from Azotobacter sp. strain GP1 revealed complete identity with the nucleotide-derived sequence from the analogous enzyme from Pseudomonas pickettii and a high degree of homology with two nondehalogenating monooxygenases. The similarity in enzyme properties and the possible evolutionary relatedness of dehalogenating and nondehalogenating monooxygenases are discussed.

Amino Acid Sequence↗

Cloning and expression of the algL gene, encoding the Azotobacter chroococcum alginate lyase: purification and characterization of the enzyme.

The alginate lyase-encoding gene (algL) of Azotobacter chroococcum was localized to a 3.1-kb EcoRI DNA fragment that revealed an open reading frame of 1,116 bp. This open reading frame encodes a protein of 42.98 kDa, in agreement with the value previously reported by us for this protein. The deduced protein has a potential N-terminal signal peptide that is consistent with its proposed periplasmic location. The analysis of the deduced amino acid sequence indicated that the gene sequence has a high homology (90% identity) to the Azotobacter vinelandii gene sequence, which has very recently been deposited in the GenBank database, and that it has 64% identity to the Pseudomonas aeruginosa gene sequence but that it has rather low homology (15 to 22% identity) to the gene sequences encoding alginate lyase in other bacteria. The A. chroococcum AlgL protein was overproduced in Escherichia coli and purified to electrophoretic homogeneity in a two-step chromatography procedure on hydroxyapatite and phenyl-Sepharose. The kinetic and molecular parameters of the recombinant alginate lyase are similar to those found for the native enzyme.

Amino Acid Sequence↗

Polyol dehydrogenases of Azotobacter agilis.

Marcus, Leon (University of California, Davis), and Allen G. Marr. Polyol dehydrogenases of Azotobacter agilis. J. Bacteriol. 82:224-232. 1961.-Two soluble diphosphopyridine-linked polyol dehydrogenases are formed by Azotobacter agilis (A. vinelandii). The first, d-mannitol dehydrogenase is induced by d-mannitol and all of the pentitols except l-arabitol. Ribitol is an excellent inducer of mannitol dehydrogenase although it is not metabolized, nor does the enzyme act upon it. This allows study of the gratuitous induction of mannitol dehydrogenase. Of the polyols tested, mannitol dehydrogenase oxidizes d-mannitol, d-arabitol, d-rhamnitol, and perseitol, demonstrating its requirement for substrates bearing the d-manno configuration. The corresponding 2-ketoses, d-fructose, d-xylulose, and presumably d-rhamnulose, and perseulose are reduced. The second enzyme, l-iditol dehydrogenase is induced only by polyols containing the d-xylo configuration, i.e., sorbitol and xylitol. l-Iditol dehydrogenase oxidizes d-xylo polyols seven times faster than it does d-ribo polyols. Substrates oxidized include l-iditol, sorbitol, xylitol, and ribitol. The corresponding 2-ketoses, l-sorbose, d-fructose, d-xylulose, and d-ribulose, are reduced. The two polyol dehydrogenases have been separated and purified by chromatography on a modified cellulose ion exchanger.

Azotobacter↗

Growth of Azotobacter in deuterium oxide.

Johnstone, D. B. (University of Vermont, Burlington). Growth of Azotobacter in deuterium oxide. J. Bacteriol. 83:867-870. 1962.-To the small list of bacteria that are reported to have been cultured in fully deuterated media can be added Azotobacter agilis and A. vinelandii. Moreover, these bacteria, although growing in a deuterium oxide medium with deuterated carbon sources, will fix atmospheric nitrogen. Lag periods occur prior to growth, and wide morphological variation is apparent during adaptation to a deuterated environment. A convenient method is presented for measuring, by infrared spectroscopy, the amount of water that accumulates in a D(2)O medium; during incubation this amounts to about 1% per day. Prevention of this accumulation of water indicates that growth, after a lag period, probably is not supported by accumulated hydrogen.

Adaptation, Physiological↗

Central body of the Azotobacter cyst.

Parker, Laura T. (Louisiana State University, Baton Rouge), and M. D. Socolofsky. Central body of the Azotobacter cyst. J. Bacteriol. 91:297-303. 1966.-Sodium citrate was found to effect extensive rupture of cyst coats of Azotobacter vinelandii. By filtering a citrate-ruptured cyst suspension through a Millipore microfiber glass prefilter, a preparation of viable central bodies was obtained that contained less than 1% residual cysts and vegetative cells. Electron micrographs showed the central bodies to have a cell wall and cell membrane. Free central bodies germinated into typical vegetative cells. Central bodies exhibited approximately the same resistance to ultraviolet radiation, sonic treatment, and elevated temperatures as did vegetative cells; cysts were much more resistant. Manometric experiments indicated that central bodies and cysts have almost the same oxidative capabilities. Results of resistance studies indicated that the central body is a contracted vegetative cell encased in a protective coat. The cyst coat appears to account for the resistance of the cyst.

Azotobacter↗

Cyst formation and poly-beta-hydroxybutyric acid accumulation in Azotobacter.

Stevenson, L. H. (Louisiana State University, Baton Rouge), and M. D. Socolofsky. Cyst formation and poly-beta-hydroxybutyric acid accumulation in Azotobacter. J. Bacteriol. 91:304-310. 1966.-The relationship between cyst formation and the accumulation of poly-beta-hydroxybutyric acid (PHB) in Azotobacter vinelandii (A. agilis) was investigated. After various periods of growth, the cells were harvested, and the amount of PHB and the extent of encystment were determined. The polymer content of the cells increased sharply and reached a maximum on the 2nd day of growth followed by a gradual decline as the culture aged. At maximal accumulation, the PHB content was 35% of the dry weight, and the PHB-nitrogen ratio was 11:1. Those substrates promoting the highest polymer content (glucose, butanol) also promoted 95 to 100% encystment. Manipulation of the carbon and nitrogen supply in the medium indicated that both the maximal PHB content and the extent of cyst formation could be controlled. A direct correlation was noted between the amount of polymer accumulated and the percentage of cysts formed, indicating a possible role of PHB as a carbon or energy source, or both, for the encystment process.

Azotobacter↗

Endogenous metabolism of Azotobacter agilis.

Sobek, J. M. (University of Southwestern Louisiana, Lafayette), J. F. Charba, and W. N. Foust. Endogenous metabolism of Azotobacter agilis. J. Bacteriol. 92:687-695. 1966-Ribonucleic acid, deoxyribonucleic acid, cellular carbohydrate, and the cold trichloroacetic acid and acidic alcohol fractions of the cell do not appear to function as endogenous reserves for Azotobacter agilis. The immediate endogenous reserve of cells grown on glucose, acetate, or succinate was poly-beta-hydroxybutyric acid (PHB). Viability of the cells during starvation was dependent upon the initial levels of PHB and the growth substrate. Cells with high initial PHB levels survived longer than cells with lower levels. Cells from succinate-grown cultures had lower PHB levels than cells from glucose-grown cultures, but were capable of maintaining their viability longer. Cellular protein may also serve as a secondary endogenous reserve substrate for this organism.

Acetates↗

L-malate oxidation by the electron transport fraction of Azotobacter vinelandii.

The membrane-bound l-malate oxidoreductase of Azotobacter vinelandii strain O was found to be a flavoprotein-dependent enzyme associated with the electron transport system (R(3)) of this organism. The particulate R(3) fraction, which possessed the l-malate oxidoreductase, carried out the cyanide-sensitive oxidation of l-malate, d-lactate, reduced nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate, succinate, cytochrome c, tetramethyl-p-phenylenediamine, and p-phenylenediamine, with molecular O(2) as the terminal electron acceptor. d-Malate was not oxidized, but l-malate was oxidized to oxalacetate. Phenazine methosulfate (PMS), vitamin K(3), K(3)Fe(CN)(6), nitro blue tetrazolium, and dichloroindophenol all served as good terminal electron acceptors for the l-malate oxidoreductase. Cytochrome c was a poor electron acceptor. Extensive studies on the l-malate oxidase and PMS and K(3) reductases revealed that all were stimulated specifically by flavine adenine dinucleotide and nonspecifically by di- or trivalent cations, i.e., Ca(++), Ba(++), Mn(++), Mg(++), Fe(+++), Ni(++), and Al(+++). All these activities were markedly sensitive to ethylenediaminetetraacetate (EDTA). The V(max) values for the l-malate oxidase, PMS, and vitamin K(3) reductases were, respectively, 3.4, 15.1, and 45.5 mumoles of substrate oxidized per min per mg of protein at 37 C. Spectral studies revealed that the Azotobacter R(3) flavoprotein and cytochromes (a(2), a(1), b(1), c(4), and c(5)) were reduced by l-malate. l-Malate oxidase activity was sensitive to various inhibitors of the electron transport system, namely, p-chloromercuriphenylsulfonic acid, chlorpromazine, 2-n-heptyl-4-hydroxyquinoline-N-oxide, antimycin A, and KCN. Minor inhibitory effects were noted with the inhibitors 4,4,4-trifluoro-1-(2-thienyl)-1,3-butanedione, rotenone, and Amytal.

Antimycin A↗

The response of Azotobacter chroococcum to oxygen: superoxide-mediated effects.

Nitrogenase in Azotobacter chroococcum whole cells was inhibited by enzymically generated superoxide anion (O2-), hydrogen peroxide, and ethyl hydrogen peroxide. The degree of inhibition produced by O2- was related to the quantity of oxygen supplied to the organisms in continuous cultures. O2- also inhibited oxygen uptake by whole cells. These O2- mediated inhibitions were prevented by bovine superoxide dismutase. The quantities of superoxide dismutase (SOD), and catalase associated with cells grown under varying oxygen concentrations were determined. The role of hydrogen peroxide, and of the hydroxyl radical (.OH) in nitrogenase inhibition was examined. The response of Azotobacter chroococum to oxygen was evaluated with respect to the observed effects of O2- on the organism, and some explanation is given to account for nitrogenase sensitivity to oxygen.

Azotobacter↗

Azotobacter chroococcum does not contain sodA or its gene product Mn-superoxide dismutase.

Azotobacter chroococcum and Azotobacter vinelandii grown in Burk medium with 1% mannitol (BM) or in BM supplemented with 2.2 mg/mL ammonium acetate (BM+N) were found to have only iron-containing and CuZn-containing superoxide dismutase. Furthermore, genomic DNA from A. chroococcum and A. vinelandii were subjected to polymerase chain reaction analysis using sodA- and sodB-specific primers and yielded only a sodB product. These results dispute the assertion by Buchanan and Lees (Can. J. Microbiol. 26: 441-447, 1980) that A. chroococcum contains Mn-superoxide dismutase.

Amino Acid Sequence↗

Alginate production by Azotobacter vinelandii.

Although all commercial alginates are today of algal origin, there is interest in the production of alginate-like polymers from bacteria. The species Azotobacter vinelandii seems to be the best candidate for the industrial production of alginate molecules characterized by a chemical composition, molecular mass and molecular mass distribution suited to a well defined application, especially required in the biotechnological, biomedical and pharmaceutical fields. The production of alginate by A. vinelandii has been to date widely investigated both in batch (mainly in the shaken flask scale) and in continuous cultures. This article summarizes current knowledge on the structure and properties of alginates and their applications and presents an overview of up-dated research on the physiology, genetics and kinetics of the production of alginate by Azotobacter vinelandii and its rheology, including the results of our recent studies.

Alginates↗

Transcription of Azotobacter phage deoxyribonucleic acid. Salt-dependent equilibrium between steps in initiation.

The transcription of Azotobacter phage A21 DNA by Escherichia coli or Azotobacter vinelandii RNA polymerase differs from that of some other DNAs in its inhibition by moderate concentrations of KCl. This characteristic results in an apparent low template activity for this DNA as compared with T4 DNA under standard assay conditions. From an analysis of the dependence of the various steps in initiation on KCl it is concluded that the effect is exerted on an equilibrium between an inactive polymerase-DNA complex and an active preintitiation complex. This salt-sensitive equilibrium favors the inactive complex at a lower KCl concentration than with other templates. It can be approached from other low or high salt concentrations at a measurably slow rate.

Azotobacter↗

[Growth of Azotobacter chroococcum strains on different substrates].

Azotobacter chroococcum 34, actively growing on alpha-ketoglutaric acid, and Azotobacter chroococcum B and KL, which almost do not assimilate this acid, can grow on the majority of substrates of the tricarboxylic acid cycle and on glucose, with and without nitrogen. The rate of assimilation of alpha-ketoglutaric acid is several times higher in the cells cultivated in the presence of this acid than in the cells grown on other substrates. This difference seems to involve the mechanism of transport of alpha-ketoglutaric acid into the cell.

Acetates↗

[Effect of rotting corn straw on the development of bacteria of the Azotobacter group].

The effects of the addition of ground maize straw, nitrogen compounds, ground lucern and water to soils incubated at 30 degrees C in Erlenmeyer flasks, on Azotobacter chroococcum growth have been studied. The results showed that the highest number of Azotobacter in soils treated with different percentage of ground maize straw without addition of nitrogen compounds and with water at 100% field capacity appeared as soon as the 5th day, reaching a maximun on the 20th day when the following numbers of bacteria were observed: control, 1,5 times 20(6); straw 1% 30 times 10(6), 2%, 33 times 10(6) and 4%, 77 times 10(6) per gram of air dried soil. This enables us to assume that the anaerobic decomposition of straw (cellulose and hemicellulose principally) in nature leads to the indirect utilization of its energy for a high asymbiotic microbiogical soil fixation of atmospheric nitrogen.

Azotobacter↗

[Use of bacteria of the genus Azotobacter for biodegradation of oil-contaminated soils].

The rate of self-purification of oil-contaminated soil increases after introduction of bacteria of the genus Azotobacter. The bacteria can assimilate oil hydrocarbons as the sole source of carbon and energy, both in the presence of fixed nitrogen and during nitrogen fixation. The species Azotobacter chroococcum activates growth of hydrocarbon-oxidizing bacteria present in Devoroil.

Azotobacter↗

Seed borne nature of Azotobacter chroococcum in chilli (Capsicum annum) and its role in seed germination and plant growth.

Investigations were carried out on seed borne nature of Azotobacter chroococcum in chilli and their role in plant growth at the Department of Agriculture Microbiology, University of Agricultural Sciences, Dharwad. Azotobacter chroococcum were isolated from both surface sterilized and unsterilized seeds of 14 varieties of chilli at different stages of fruit maturity. Inoculation with these strains increased the seed germination, root, shoot length and total dry matter content of chilli plants significantly in both sterilized and unsterilized soil., the results of which are presented.

Azotobacter↗