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At least 19 recordsLinked to original sources

PubMed1975

Interactions between Azotobacter and "phosphobacteria" and their establishment in the rhizosphere as affected by soil fertility.

The effects on plant growth of "bacterial fertilizers" prepared from Azotobacter spp. and phosphate-solubilizing bacteria ("phosphobacteria") have been the subject of much controversy. Cases where no plant-growth stimulation occurred may often be accounted for by the failure to establish the bacterial inocula in the rhizosphere. Three factors that may influence inocula establishment, i.e. soil fertility, manuring, and interactions between Azotobacter and "phosphobacteria," were examined in pot experiments, designed for statistical analysis, in two neutral-alkaline soils, using lavender plants (Lavandula spica L.). During the experiments the numbers of Azotobacter and "phosphobacteria" were counted. Dry weights of roots and shoots were recorded after 16 weeks of growth. At the end of the experiments there were always more Azotobacter and "phosphobacteria" in the rhizospheres when plants were inoculated with both groups of organisms together than when they were inoculated singly. Addition of 2% farmyard manure to the richer soil enhanced this effect. Plant growth was greatest when seedlings were inoculated with both Azotobacter and the "phosphobacteria".

Azotobacter↗

PubMed1978

Transformation of Azotobacter vinelandii strains unable to fix nitrogen with Rhizobium spp. DNA.

The phenotypes of Azotobacter vinelandii ATCC 12837 strains defective in nitrogen fixation (Nif-) were characterized by intrageneric transformation with known Nif- strains of A. vinelandii OP. These former mutant strains were used as recipients for intergeneric transformation by deoxyribonucleic acid (DNA) prepared from Rhizobium spp. to determine if the rhizobia would transform the Azotobacter Nif- phenotypes to Nif+. The frequency of Nif+ transformants using Rhizobium DNA was always less than the frequency using Azotobacter wild-type DNA but was greater than the spontaneous reversion frequency. The Azotobacter Nif+ recombinants also were stable. DNA from all of the Rhizobium spp. transformed to Nif+ Azotobacter mutants defective in the nitrogenase component I (molybdoferredoxin); however, some recombinants had a lower nitrogenase activity and a delayed nitrogenase depression time. Mutants defective in the pleiotrophic transcriptional control of both nitrogenase components were transformed to Nif+ by the asymbiotic nitrogen fixing Rhizobium sp. 32H1 and 41A1, but not the symbiotic nitrogen-fixing species. The significance of these results and the possible future applications of this system are discussed.

Azotobacter↗

PubMed1979

Effect of Azotobacter inoculation on plant growth and soil nitrogen.

The validity of seed bacterization with Azotobacter chroococcum in soils of variable densities of naturally present azotobacters was studied. Inoculation of barley grains had no effect on counts of total microflora, neither in rhizosphere nor in root-free soil, but significantly increased Azotobacter population, especially in the rhizosphere. The rate of colonization in the root region was much higher when soil initially harboured low Azotobacter densities. Bacterization improved plant growth and increased soil nitrogen through nitrogen fixation. Nitrogen balance in soils showed higher gains in the inoculated treatments over the uninoculated analogues of 30--98 ppm.

Azotobacter↗

PubMed1979

Ecological studies on Azotobacter in Egyptian soils.

The present survey includes 156 representative soil samples. Results obtained confirm the richness of Egyptian soils, particularly the Nile Valley soils, in Azotobacter (60% of the samples contained greater than 10(3) colonies/g soil). Colony counts were lower than MPN estimations. Glucose is recommended for use in plating medium. Among the environmental factors affecting Azotobacter densities in soils of Egypt are: organic carbon content, total soluble salt content, pH and type of the soil, depth, cultivation, and standing crop. Pot experiments performed indicated that high incubation temperature (30, 37 degrees C) markedly enhanced development of Azotobacter as well as the gains of total nitrogen, particularly when soils are amended with 1% maize straw and incubated for 12 months. A. chrococcum was the most prevalent speciee; A. vinelandii was encountered as well. The analysis of some samples, representing soils of near Middle Eastern as well as North African countries, indicated the common occurrence of Azotobacter in these soils. Beijerinckia could not be detected in any of Egyptian or non-Egyptian samples examined.

Azotobacter↗

PubMedDate not supplied

Growth of Azotobacter vinelandii in dialysed soil medium: studies upon the life cycle.

Azotobacter vinelandii ATCC 12837 cultured in dialysed soil medium with addition of 0.5% glucose showed four distinct morphological cell types: large cells, precyst forms, mature cysts and filterable corpuscles (0.3 micron in diameter). These results indicate that Azotobacter is a bacterium with a complex life cycle under certain culture conditions. Intracellular levels of RNA and poly-beta-hydroxybutyric acid were significantly affected when cells grown in dialysed soil were compared with those obtained after growth on defined medium (N-free). Further studies showed that the chemical composition of filterable corpuscles obtained from dialysed soil medium were different from the composition of normal Azotobacter cells produced in both culture media (dialysed soil and defined media). We suggest that filterable corpuscles represent a stage in the life cycle of Azotobacter in their natural environment.

Azotobacter↗

PubMed1990

Azotobacter vinelandii flavodoxin: purification and properties of the recombinant, dephospho form expressed in Escherichia coli.

The nifF gene coding for the flavodoxin from the nitrogen-fixing bacterium Azotobacter vinelandii (strain OP) was cloned into the plasmid vector pUC7 [Bennett, L. T., Jacobsen, M. R., & Dean, D. R. (1988) J. Biol. Chem. 263 1364-1369] and the resulting plasmid transformed and expressed in Escherichia coli strain DH5. Recombinant Azotobacter flavodoxin is expressed at levels 5-6-fold higher in E. coli than in comparable yields of Azotobacter cultures grown under nitrogen-fixing conditions. Even higher levels were observed with flavodoxin expressed in E. coli under control of a tac promoter. Electron spin resonance spectroscopy on whole cells and in cell-free extracts showed the flavodoxin to be largely in the semiquinone form. The flavodoxin purified from E. coli exhibited the same molecular weight, isoelectric point, flavin mononucleotide (FMN) content, N-terminal sequence, and carboxyl-terminal amino acids as for the wild-type Azotobacter protein. The recombinant flavodoxin differed from native flavodoxin in that it exhibited an increased antigenicity to flavodoxin antibody and did not contain a covalently bound phosphate. Small differences are also observed in circular dichroism spectral properties in the visible and ultraviolet spectral regions. The recombinant, dephospho flavodoxin exhibits an oxidized/semiquinone potential (pH 8.0) of -224 mV and a semiquinone/hydroquinone couple (pH 8.0) of -458 mV. This latter couple is 50-60 mV higher than that exhibited by the native flavodoxin. Resolution of recombinant dephospho flavodoxin resulted in an apoflavodoxin that was much less stable than that prepared from the native protein.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗

PubMed1990

The identification, characterization, sequencing and mutagenesis of the genes (hupSL) encoding the small and large subunits of the H2-uptake hydrogenase of Azotobacter chroococcum.

The structural genes (hupSL) of the membrane-bound NiFe-containing H2-uptake hydrogenase (Hup) of Azotobacter chroococcum were identified by oligonucleotide screening and sequenced. The small subunit gene (hupS) encodes a signal sequence of 34 amino acids followed by a 310-amino-acid, 34156D protein containing 12 cysteine residues. The large subunit gene (hupL) overlaps hupS by one base and codes for a predicted 601-amino-acid, 66433D protein. There are two regions of strong homology with other Ni hydrogenases: a Cys-Thr-Cys-Cys-Ser motif near the N-terminus of HupS and an Asp-Pro-Cys-Leu-Ala-Cys motif near the carboxy-terminus of HupL. Strong overall homology exists between Azotobacter, Bradyrhizobium japonicum and Rhodobacter capsulatus Hup proteins but less exists between the Azotobacter proteins and hydrogenases from Desulfovibrio strains. Mutagenesis of either hupS or hupL genes of A. chroococcum yielded Hup- phenotypes but some of these mutants retained a partial H2-evolving activity. Hybridization experiments at different stages of gene segregation confirmed the multicopy nature of the Azotobacter genome.

Amino Acid Sequence↗

PubMed1976

Regulation of respiration and nitrogen fixation in different types of Azotobacter vinelandii.

The levels of the adenine nucleotides, pyridine nucleotides and the kinetical parameters of the enzymes of the Entner-Doudoroff pathway (glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase) were determined in Azotobacter vinelandii cells, grown under O2- or N2-limiting conditions. It was concluced that the levels of both the adenine nucleotides and pyridine nucleotides do not limit the rate of sucrose oxidation. Experiments with radioactive pyruvate and sucrose show that the rate of sucrose oxidation of Azotobacter cells is associated with an increase in the rate of sucrose uptake. The sites of oxidative phosphorylation and the composition of the respiratory membranes with respect to cytochromes c4 + c5, b and d differ in cells growth either O2- or N2-limited. It was possible to show that the respiration protection of the nitrogen-fixing system in Azotobacter is mainly independent of the oxidation capacity of the cells. The oxidation capacity intrinsically depends on the type of substrate and can be partly adapted. The maximum activity of the nitrogenase in Azotobacter depends on the type of substrate oxidized. Although the level of energy charge is somewhat dependent on the type of substrate used, no obvious relation can be derived between changes in energy charge and nitrogenase activity. An alternative proposal is given.

Azotobacter↗

PubMed1978

[Studies on the effects of atrazine and simazine on the N-binding bacteria Azotobacter and Beijerinckia in the ferralitic soils of Cuba].

In two Cuban locations (Santiago de las Vegas and Jovellanos) the effect was investigated of increasing atrazin and simazin applications (0, 4, 8, 16 kg/ha) to the number of Azotobacter and Beijerinckia colonies in weakly ferrallitic soils 7 and 15 days after their application during the rainy and dry seasons. The results were as follows: 1. The number of the Beijerinckia colonies is higher in all variants than that of Azotobacter. 2. Beijerinckia and Azotobacter are stimulated up to 7 days, partly also up to 15 days, after application of the triazins. Atrazin exhibits a stronger and more lasting effect than simazin, and Azotobacter are influenced more strongly than Beijerinckia. 3. This stimulation can be adduced with a high degree of probability to the inhibition of organisms which have an antagonistic effect on N-binding bacteria.

Atrazine↗

PubMed1975

The Azotobacter flora of some Czechoslovakian watercourses.

The occurrence of Azotobacter in some Szechoslovakian watercourses has been investigated. Several strains belonging to A. chroococcum and A. beijerinckii were isolated from 7 out of 18 samples. A. insignis has been isolated from the flowing water of Lake Machovo at Doksy. This is first report of this strictly aquatic Azotobacter species in Czechoslovakian watercourses. The taxonomy of the genus Azotobacter was discussed against the background of the existing knowledge resulting mainly from other taxonomic techniques than those based on the phenotypically expressed characters.

Azotobacter↗

PubMed1979

Associative symbiosis of Azotobacter chroococcum and higher plants.

The association between a selected strain of Azotobacter chroococcum and seven plants was investigated in water cultures under sterile conditions. Azotobacter population progressively increased in the nutrient solution and on the rhizoplane. Microbial propagation depends on the type of plant, being much higher in presence of wheat, followed by barley, maize, broad bean, and cotton, while in presence of fenugreek and lentil lower rates of multiplication were recorded. Inoculation increased the dry weight of plants by 5--12% and in length by 3--18% in addition to increased nitrogen content of plants and nutrient solution. Nitrogen balance showed no significant change in systems devoid of Azotobacter, but association between plants and the microorganism invariably showed positive results. The extent of N2-fixation depends on the type of plants; higher gains were recorded in presence of non-leguminous plants.

Azotobacter↗

PubMed1979

Studies on azotobacters prevailing in Egyptian soils.

Soil samples from different locations in Egypt, representing various types of soils, different degrees of fertility and under various standing crops, were used for isolating Azotobacter strains. Sixty Azotobacter isolates were obtained, and A. chroococcum was found to be the most predominant species (56 isolates), while A. vinclandii was sporadically found (4 isolates). Other species of the genus Azotobacter were not detected in the examined soil samples. Isolates were studied for their morphological, cultural, and physiological properties. Thirteen isolates, differing in morphological features, were selected for studying their pleomorphic character.

Azotobacter↗

PubMed1978

Kinetic studies on electron transfer and interaction between nitrogenase components from Azotobacter vinelandii.

Kinetic properties of electron transfer by nitrogenase of Azotobacter vinelandii are dependent on the concentration of the two components of nitrogenase. An excess of the MoFe protein inhibits electron transfer in a distinctive manner, and the inhibition is reversed by increasing levels of reductant. The saturation curve for Fe protein is hyperbolic, indicating that only one Fe protein molecule per MoFe protein is required for full activity in ATP hydrolysis and electron transfer. These results can be interpreted on the basis of a complex between the Fe protein and the MoFe protein that dissociates rapidly during turnover. Both 2:1 and 1:1 complexes (Fe-MoFe) are active. Dithionite appears to be a relatively poor reductant for nitrogenase from Azotobacter vinelandii, whereas azotobacter flavodoxin is much better. In the presence of the flavodoxin it is possible to increase the specific activity of the Fe protein more than 50% relative to its activity with dithionite alone as a reductant; specific activities greater than 3000 nmol of C2H4 formed min(-1) (mg of Fe protein)(-1) have been observed.

Adenosine Triphosphate↗

PubMed1990

Distribution of alginate gene sequences in the Pseudomonas rRNA homology group I-Azomonas-Azotobacter lineage of superfamily B procaryotes.

Chromosomal DNA from group I Pseudomonas species, Azotobacter vinelandii, Azomonas macrocytogens, Xanthomonas campestris, Serpens flexibilis, and three enteric bacteria was screened for sequences homologous to four Pseudomonas aeruginosa alginate (alg) genes (algA, pmm, algD, and algR1). All the group I Pseudomonas species tested (including alginate producers and nonproducers) contained sequences homologous to all the P. aeruginosa alg genes used as probes, with the exception of P. stutzeri, which lacked algD. Azotobacter vinelandii also contained sequences homologous to all the alg gene probes tested, while Azomonas macrocytogenes DNA showed homology to all but algD. X. campestris contained sequences homologous to pmm and algR1 but not to algA or algD. The helical bacterium S. flexibilis showed homology to the algR1 gene, suggesting that an environmentally responsive regulatory gene similar to algR1 exists in S. flexibilis. Escherichia coli showed homology to the algD and algR1 genes, while Salmonella typhimurium and Klebsiella pneumoniae failed to show homology with any of the P. aeruginosa alg genes. Since all the organisms tested are superfamily B procaryotes, these results suggest that within superfamily B, the alginate genes are distributed throughout the Pseudomonas group I-Azotobacter-Azomonas lineage, while only some alg genes have been retained in the Pseudomonas group V (Xanthomonas) and enteric lineages.

Alginates↗

PubMed1991

Degradation of 2,4,6-trichlorophenol by Azotobacter sp. strain GP1.

A bacterium which utilizes 2,4,6-trichlorophenol (TCP) as a sole source of carbon and energy was isolated from soil. The bacterium, designated strain GP1, was identified as an Azotobacter sp. TCP was the only chlorinated phenol which supported the growth of the bacterium. Resting cells transformed monochlorophenols, 2,6-dichlorophenol, and 2,3,6-trichlorophenol. Phenol and a number of phenolic compounds, including 4-methylphenol, all of the monohydroxybenzoates, and several dihydroxybenzoates, were very good carbon sources for Azotobacter sp. strain GP1. The organism utilized up to 800 mg of TCP per liter; the lag phase and time for degradation, however, were severely prolonged at TCP concentrations above 500 mg/liter. Repeated additions of 200 mg of TCP per liter led to accelerated degradation, with an optimum value of 100 mg of TCP per liter per h. TCP degradation was significantly faster in shaken than in nonshaken cultures. The optimum temperature for degradation was 25 to 30 degrees C. Induction studies, including treatment of the cells with chloramphenicol prior to TCP or phenol addition, revealed that TCP induced TCP degradation but not phenol degradation and that phenol induced only its own utilization. Per mol of TCP, 3 mol of Cl- was released. 2,6-Dichloro-p-benzoquinone was detected in the resting-cell medium of Azotobacter sp. strain GP1. By chemical mutagenesis, mutants blocked in either TCP degradation or phenol degradation were obtained. No mutant defective in the degradation of both phenols was found, indicating separate pathways for the dissimilation of the compounds. In some of the phenol-deficient mutants, pyrocatechol was found to accumulate, and in some of the TCP-deficient mutants, 2,6-dichlorohydroquinone was found to accumulate.

Azotobacter↗

PubMed1975

Characterization studies on the membrane-bound adenosine triphosphatase (ATPase) of Azotobacter vinelandii.

The adenosinetriphosphatase (ATPase) (EC 3.6.1.3) activity in Azotobacter vinelandii concentrates in the membranous R3 fraction that is directly associated with Azotobacter electron transport function. Sonically disrupted Azotobacter cells were examined for distribution of ATPase activity and the highest specific activity (and activity units) was consistently found in the particulate R3 membranous fraction which sediments on ultracentrifugation at 144 000 X g for 2 h. When the sonication time interval was increased, the membrane-bound ATPase activity could neither be solubilized nor released into the supernatant fraction. Optimal ATPase activty occurred at pH 8.0; Mg2+ ion when added to the assay was stimulatory. Maximal activity always occurred when the Mg2+:ATP stoichiometry was 1:1 on a molar ratio at the 5 mM concentration level. Sodium and potassium ions had no stimulatory effect. The reaction kinetics were linear for the time intervals studied (0-60 min). The membrane-bound ATPase in the R3 fraction was stimulated 12-fold by treatment wiTH TRypsin, and fractionation studies showed that trypsin treatment did not solubilize ATPase activity off the membranous R3 electron transport fraction. The ATPase was not cold labile and the temperature during the preparation of the R3 fraction had no effect on activity; overnight refrigeration at 4 degrees C, however, resulted in a 25% loss of activity as compared with a 14% loss when the R3 fraction was stored overnight at 25 degrees C. A marked inactivation (although variable, usually about 60%) did occur by overnight freezing (-20 degrees C), and subsequent sonication failed to restore ATPase activity. This indicates that membrane reaggregation (by freezing) was not responsible for ATPase inactivation. The addition of azide, ouabain, 2,4-dinitrophenol, or oligomycin to the assay system resulted in neither inhibition nor stimulation of the ATPase activity. The property of trypsin activation and that ATPase activity is highest in the R3 electron transport fraction suggests that its probable functional role is in coupling of electron transport to oxidative phosphorylation.

Adenosine Triphosphatases↗

PubMed1975

Variation in the Azotobacter population from several habitats in the botanical garden in Poznań.

The abundance of Azotobacter was estimated in the rhizosphere of 13 plant species from four habitats in the Botanical Garden in Poznań. The results have shown that within the particular habitats the plant exerts a pronounced influence on the abundance of Azotobacter. The morphological differences between Azotobacter populations obtained from various habitats confirm the specific effect of the plant on this bacterium.

Azotobacter↗

PubMed1990

Cross-linking site in Azotobacter vinelandii complex.

The Fe-protein and the MoFe-protein of the Azotobacter vinelandii nitrogenase complex can be chemically cross-linked by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (Willing, A., Georgiadis, M.M., Rees, D. C., and Howard, J. B. (1989) J. Biol. Chem. 264, 8499-8503). In this reaction, one of the identical subunits of the Fe-protein dimer is linked by an isopeptide bond to each beta-subunit of the MoFe-protein tetramer. The reaction has been found to be highly specific with greater than 85% of amino acid residues Glu-112 (Fe-protein) and Lys-399 (MoFe-protein) cross-linked to each other. Although Glu-112 is located in a highly conserved amino acid sequence, it is found in only half of the known Fe-protein sequences. Likewise, Lys-399 is not a conserved residue in the MoFe-protein. Glu-112 appears to be part of an anionic cluster of nine carboxylic acids which is located between the proposed thiol ligands for the Fe:S center. In contrast, the basic residue cluster which includes Lys-399 has been found in only in the Azotobacter MoFe-protein. Thus, this crosslinking reaction either is unique to Azotobacter nitrogenase or must involve other residues in the MoFe-protein of other species. Because Lys-399 and Glu-112 form a specific cross-link, it is probable that they are part of the interaction site leading to productive complex formation. This information should be useful for the model building of the complex from the crystallographic structures of the individual components.

Amino Acid Sequence↗