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PubMed1992

Reclassification of two strains of Arthrobacter oxydans and proposal of Arthrobacter nicotinovorans sp. nov.

Arthrobacter oxydans DSM 419 and DSM 420 have chemical and microbiological properties that are consistent with assignment to the genus Arthrobacter. Both organisms have the lysine-alanine-threonine-alanine peptidoglycan type. DNA-DNA pairing studies indicated that A. oxydans DSM 419 should be reclassified as Arthrobacter ureafaciens and that A. oxydans DSM 420T forms the nucleus of a distinct genomic species. We propose that A. oxydans DSM 420 should be reclassified as Arthrobacter nicotinovorans sp. nov. The type strain is strain DSM 420.

Amino Acid Sequence↗

PubMed1978

Isolation and characterization of Arthrobacter bacteriophages and their application to phage typing of soil arthrobacters.

Seventeen bacteriophages, active against 19 Arthrobacter soil isolates, were isolated from concentrated samples of river water and sewage. Attempts to isolate Arthrobacter bacteriophages from filtrates of broth cultures of the soil isolates or from ultraviolet light-irradiated cultures were unsuccessful. Bacteriophages were not detected in either concentrated or unconcentrated soil extracts. Electron microscopic studies of 11 phages showed morphologies characteristic of Bradley's groups B (exhibited by 9 phages) and C (exhibited by 2 phages). Moles percent guanine plus cytosine, calculated from the deoxyribonucleic acid density of three phages, ranged from 60.2 to 65.3. The phages were characterized by their plague and virion morphology, host range, and serological specificity.

Arthrobacter↗

PubMed1975

A nutritional and taxonomic survey of Arthrobacter soil isolates.

One hundred and sixty Arthrobacter soil isolates, four groups of 40 from each of four soil types, and 17 Arthrobacter named strains were characterized on the basis of 203 different nutritional tests performed on each culture. One hundred and twenty-one compounds were examined as sole sources of carbon, 44 compounds as sole sources of nitrogen, 22 carbohydrates for the production of acid, and 16 tests were done for tolerance to various dyes. The four groups of soil arthrobacters differed markedly in acid production from carbohydrates, and in utilization of aliphatic amino acids and aromatic hydrocarbons as sole sources of carbon. The named strains did not exhibit as much nutritional diversity as any of the four groups of soil isolates. The results of the nutritional tests were subjected to a computerized taxonomic analysis. Eighty-four of the isolates were contained in nine separate clusters with 87 to 94% similarity; 39 isolates were contained in five mixed but recognizable clusters with 84 to 86% similarity; 60 isolates were randomly mixed with no recognizable clusters and similarity of 72 to 83%. All clusters were composed of nearly equal numbers of isolates from each of the four soils; the named strains were not found associated with any of the clusters of soil isolates. The results indicated that the diversity of the genus Arthrobacter is not represented by the named species already described, and the possibility of using a series of standardized tests to categorize soil arthrobacters into readily identifiable nutritional groups is discussed.

Acids↗

PubMed1977

Effects of temperature on the macromolecular composition and find structure of psychrophilic Arthrobacter species.

A facultatively psychrophilic bacterium, Arthrobacter SI 55, grows at 20 degrees C, but growth, as measured by increase of viable cell count, is inhibited at 32 degrees C. Corresponding temperatures for an obligate psychrophile, Arthrobacter glacialis SI 137, are 10 degrees C and 19-20 degrees C. At the higher temperatures for each organism increases of cell mass, as measured by turbidity and of DNA, RNA, and protein, were not inhibited. At the upper temperatures, fewer septa were formed in Arthrobacter SI 55, and cells appeared as distorted filaments with irregular brancehs. Arthrobacter glacilis grew as single cells at the lower temperature, but as clumps of coccoid cells with well marked septa at the higher temperature. It appears that in Arthrobacter SI 55 septum formation may be inhibited at the higher temperature. In contrast, in A. glacialis septation occurs but the cells do not separate.

Arthrobacter↗

PubMedDate not supplied

[Plasmids for biodegradation of 2,6-dimethylpyridine, 2,4-dimethylpyridine, and pyridine in strains of Arthrobacter].

Arthrobacter crysallopoietes strain KM-4 degrading 2,6-dimethylpyridine and strain KM-4a degrading both 2,6-dimethylpyridine and pyridine, Arthrobacter sp. KM-4b degrading 2,4-dimethylpyridine were isolated from soil. Arthrobacter crystallopoietes KM-4 and Arthrobacter sp. KM-4b contain 100 Md plasmids pBS320 and pBS323. Arthrobacter crystallopietes KM-4a harbours a 100 Md and 80 Md plasmids. Plasmid curing and conjugation transfer results confirm that these plasmids are involved in degradation of 2,6-dimethylpyridine, 2,4-dimethylpyridine and pyridine. A mutant with lost ability to degrade 2,6-dimethylpyridine was isolated during the growth of strain KM-4 rifR at 42 degrees C. Electrophoretic analysis of the plasmid from temperature sensitive mutant revealed the deletion the size of 26 Md from pBS320 plasmid.

Arthrobacter↗

PubMed1979

DNA-DNA homology studies among strains of Arthrobacter and Brevibacterium.

Sixteen named strains of Arthrobacter and two strains of Brevibacterium were investigated by nucleic acid hybridisation. The Arthrobacter strains show homology values ranging between 11 and 55% to the type strain A. globiformis DSM 20124 (ATCC 8010), indicating only a low to moderate relationship. Two strains of A. globiformis, DSM 20124 and DSM 20125, exhibit only poor relationship to one another (30%). Among all the Arthrobacter strains the homology data range between 10 to 70% demonstrating separate status of almost all species. Only A. polychromogenes DSM 20136 was found to be a subspecies of A. oxydans DSM 20119. The type strain of A. citreus, DSM 20133 shows a remarkable lack of homology to four other strains of A. citreus, deposited as ATCC 15170, ATCC 17775, ATCC 21040 and ATCC 21348 (11--13%) which themselves can be separated into two groups according to the homology data (24--31%). Each of the two strains of Brevibacterium share high genetic relatedness with one of these A. citreus groups (71 and 73%, respectively). According to the DNA-DNA homology data, most of the species of Arthrobacter can actually be ranged taxonomically as species.

Arthrobacter↗

PubMed1977

Enzymes of the yeast lytic system produced by Arthrobacter GJM-1 bacterium and their role in the lysis of yeast cell walls.

Yeast lytic system produced by Arthrobacter GJM-1 bacterium during growth on baker's yeast cell walls contains a complete set of enzymes which can hydrolyze all structural components of cell walls of Saccharomyces cerevisiae. Chromatographic fractionation of the lytic system showed the presence of two types of endo-beta-1,3-glucanase. Rapid lysis of isolated cell walls of yeast was induced only by endo-beta-1,3-glucanase exhibiting high affinity to insoluble beta-1,3-glucans and releasing laminaripentaose as the main product of hydrolysis of beta-1,3-glucans. This enzyme was able to lyse intact cells of S. cerevisiae only in the presence of an additional factor present in the Arthrobacter GJM-1 lytic system, which was identified as an alkaline protease. This enzyme possesses the lowest molecular weight among other identified enzyme components present in the lytic system. Its role in the solubilization of yeast cell walls from the outer surface by endo-beta-1,3-glucanase could be substituted by preincubation of cells with Pronase or by allowing the glucanase to act on cells in the presence of thiol reagents. The mechanism of lysis of intact cells and isolated cell walls by the enzymes of Arthrobacter GJM-1 is discussed in the light of the present conception of yeast cell wall structure.

Arthrobacter↗

PubMed1992

Levels of trehalose and glycogen in Arthrobacter globiformis under conditions of nutrient starvation and osmotic stress.

Cells of Arthrobacter globiformis grown in carbohydrate-rich media were found to contain large quantities of low-Mr carbohydrates (800 micrograms/mg protein) and only small amounts of amino acids, in addition to high amounts of glycogen (2 mg/mg protein). At increasing osmotic values of the medium, low-Mr carbohydrate levels increased to 1300 micrograms/mg protein. Low-Mr pools were extracted from the cells with hot 75% ethanol, and subjected to thin layer, gel and gas-liquid chromatography. They turned out to consist mainly of alpha,alpha-trehalose. Levels of trehalose in Arthrobacter cells have the tendency to remain constant, both during nutrient exhaustion (resulting in glycogen consumption), and on addition of excess of carbon source to the medium (resulting in an increased glycogen content of the cells). The stress-tolerant properties of Arthrobacter (resistance to nutrient starvation, desiccation and high salt concentration) are discussed with respect to the high glycogen and trehalose contents of the cells.

Actinomycetales↗

PubMed1976

Growth and pigment production by Arthrobacter pyridinolis n. sp.

A new bacterium capable of growing on 2-hydroxypyridine as sole source of carbon and nitrogen was isolated from soil. During its growth on solid medium, approximately 50% of this substrate was converted to a brilliant blue crystalline pigment which was deposited extracellularly in the colony mass. The pigment was identical to that produced by Arthrobacter crystallopoietes during its growth on 2-hydroxypyridine. The new isolate exhibited the typical cycle of morphogenesis characteristic of the genus Arthrobacter. The organism is different from all other reported species of Arthrobacter. It is proposed that the organism be named Arthorbacter pyridinolis n. sp.

Arthrobacter↗

PubMed1976

Colonization of soil by Arthrobacter and Pseudomonas under varying conditions of water and nutrient availability as studied by plate counts and transmission electron microscopy.

Arthrobacter globiformis and a Pseudomonas soil isolate were incubated separately and in combination in soil that had been presterilized by autoclaving. Growth and other responses of the cells in situ in this soil were monitored by plate counts and transmission electron microscopy examinations of cell sections. During the soil incubations, some of the samples were first allowed to dry and then were remoistened with water or with a dilute or a concentrated nutrient solution. Based on plate counts and ultrastructural analysis. Arthrobacter seemed to be in a non-multiplying coccoid-rod resting state and to be virtually immune to soil drying. Addition of a dilute nutrient solution helped maintain cell ultrastructure and prevent a low level of lysing that occurred in the absence of nutrient addition. Addition of a concentrated nutrient solution brought on cell multiplication as both coccoid-rods and long rods, but the ultimate form with further incubation was the coccoid-rod. The Pseudomonas strain suffered death and ultrastructural deterioration as water became less available. It responded by cell multiplication to an equal extent when either water or dilute nutrients were added, but possibly was able to give a growth response to nutritive amendment when a concentrated nutrient addition was made. The Arthrobacter was not affected by the presence of Pseudomonas in dual culture. The Pseudomonas, however, possibly suffered a nutritive deficiency under these conditions.

Arthrobacter↗

PubMed1992

Immunological demonstration of a unique 3,4-dihydroxyphenylacetate 2,3-dioxygenase in soil Arthrobacter strains.

Many bacteria biosynthesize 3,4-dihydroxyphenylacetate 2,3-dioxygenases for growth on aromatic acids, but gram-negative organisms have been most extensively studied. A gram-positive strain containing 2,3-dioxygenase activity was identified as Arthrobacter strain Mn-1. The 2,3-dioxygenase from strain Mn-1 was purified to homogeneity by fast protein liquid chromatography with a Mono Q anion-exchange column. Rabbit polyclonal antidioxygenase antibodies were prepared. Ouchterlony double-diffusion and Western blotting (immunoblotting) protocols were used to probe the distribution of the Mn-1 dioxygenase antigen in soil bacteria. Fourteen 2,3-dioxygenase-containing Bacillus and Pseudomonas strains did not contain immunologically cross-reactive proteins. Six of eight Arthrobacter strains contained 2,3-dioxygenase activity, and all of them produced cross-reactive proteins. The data presented here suggest that a unique type of dioxygenase is geographically widespread but is taxonomically confined to Arthrobacter soil bacteria.

Amino Acids↗

PubMed1976

[Degradation of 4-chlorobenzoic acid by an Arthrobacter species (author's transl)].

An Arthrobacter sp. growing on 4-Chlorobenzoic acid as its sole source of carbon excretes 4-hydroxygenzoic acid and protocatechuic acid into the culture medium. Protocatechuic acid is further attacked by "meta"-cleavage. During growth of the Arthrobacter sp. on benzoic acid cis-cis muconic acid can be isolated from the medium, suggesting the involvement of the "ortho"-cleavage pathway. The enzymes both for the "meta"- and the "ortho"-cleavage pathway are inducible.

Arthrobacter↗

PubMed1978

Purification and properties of Arthrobacter neuraminidase.

Neuraminidase (EC 3.2.1.18) from an Arthrobacter species was purified homogeneity by conventional procedures (yield approx. 1 mg/1) and was judged to be homogeneous by sodium dodecyl sulfate gel electrophoresis. Gel electrofocusing of neuraminidase revealed 1 major band (85-90%), pI 5.35 +/- 0.05, and 6 minor bands, whose pI ranged from 5.25 to 5.70, and each of which had catalytic activity. Arthrobacter neuraminidase is a monomeric glycoprotein of molecular weight 88 000, has an apparent Km of 7.8-10(-4) M for N-acetylneuraminlactose, is insensitive to inhibition by N-acetylneuraminic acid, and is about 2% carbohydrate by weight. The amino acid composition as well as the galactosamine and glucosamine content was determined. The enzyme can hydrolyze (alpha, 2-3), (alpha, 2-6), (alpha, 2-8) linkages. The active size of the enzyme appears to be inaccessible since no inhibition was observed by reagents known to modify sulfhydryl, lysyl, carboxyl, histidinyl, and argininyl residues. In contrast, N-bromosuccinimide at a 60-fold molar ratio to enzyme, gave complete inhibition. These results suggest that a tryptophan residue is essential for catalysis.

Amino Acids↗

PubMed1975

Peptidoglycan compositions of a new strain of Arthrobacter crystallopietes during sphere-rod morphogenesis.

Arthrobacter crystallopoieties ATCC 15481 was used to isolate a new strain. designated Arthrobacter crystallopoieties EPSR-16, which had a mass doubling time in brain heart infusion broth and in glucose/salts/yeast extract medium of 30 min compared to 2.40 h for the parent strain in similar media. The growth rates for the new strain and for the parent were close to 12 h in glucose/salts medium. The new strain formed well-separated cocci and diplococci in glucose/salts medium, and upon nutrient shift-up all the cells in the population gradually changed into well-separated rods of regular shape. In the spherical state the cell wall peptidoglycan of the new strain contained lysine and no diaminopimelic acid. A gradual loss in lysine and a gain in diaminopimelic acid occurred during morphogenesis. Diaminopimelic acid became predominant in the cell wall during balanced growth in the rod state.

Arthrobacter↗

PubMed1977

Distribution of neuraminidase in Arthrobacter and its purification by affinity chromatography.

Neuraminidase [sialidase, EC 3.2.1.18] was found to be widely distributed in bacteria belonging to Arthrobacter. Among these bacteria, Arthrobacter ureafaciens, A. oxydans, and A. aurescens produced relatively potent neuraminidase activities. For the production of this enzyme, not only colominic acid, a homopolymer of N-acetylneuraminic acid, but also N-acetylneuraminic acid, the reaction product of this enzyme, are effective as sources of carbon. An affinity adsorbent specific for neuraminidase was prepared by cross-linking colominic acid with soluble starch by means of epichlorohydrin. Neuraminidase from A. ureafaciens could be purified on this affinity column. The purified neuraminidase was shown to be free from protease, N-acetylneuraminic acid aldolase, phospholipase C, and glycosidases. Aminoff's assay procedure for sialic acid was modified to avoid the centrifugation step. The modified procedure gave a higher molecular extinction coefficient.

Arthrobacter↗

PubMed1976

Metabolism of L-rhamnose in Arthrobacter pyridinolis.

In Arthrobacter pyridinolis, a respiration-coupled transport system for L-rhamnose caused accumulation of free L-rhamnose, while a phosphoenolpyruvate: L-rhamnose phosphotransferase system caused accumulation of L-rhamnose I-phosphate (Levinson & Krulwich, 1974). The pathways for subsequent metabolism of L-rhamnose and L-rhamose I-phosphate have now been investigated. Arthrobacter pyridinolis contains an inducible L-rhamnose isomerase and L-rhamnulokinase, as well as a constitutive L-rhamnulose I-phosphate aldolase. Results with mutants which are unable to metabolize L-rhamnose suggest the presence of an L-rhamnose I-phosphate phosphatase, which forms free L-rhamnose by hydrolysis of L-rhamnose I-phosphate produced by the phosphotransferase system. Mutants which lack this enzyme exhibited severe inhibition of growth in the presence of L-rhamnose plus any of a variety of carbon sources. There is some evidence that this inhibition was due to accumulation of L-rhamnose I-phosphate at toxic concentrations within the bacteria. The metabolism of L-rhamnose transported by the phosphotransferase system therefore appears to occur by hydrolysis of L-rhamnose I-phosphate to free L-rhamnose by a phosphatase. Metabolism of the L-rhamnose thus produced, and of that accumulated by the respiration-coupled transport system, the proceeds by the sequence of reactions: L-rhamnose leads to L-rhamnulose leads to L=rhamnulose I-phosphate leads to dihydroxyacetone phosphate plus L-lactaldehyde.

Aldehyde-Lyases↗

PubMed1992

Myceloid cell formation in Arthrobacter globiformis during osmotic stress.

Arthrobacter globiformis was grown in a semi-defined liquid medium containing added solutes to determine the effects of osmotic stress on its reproduction and cell morphology. There was a progressive reduction in the specific growth rate during exponential phase as the concentration of NaCl was increased, although the final yields of the cultures during stationary phase were not affected. Clusters of branching myceloid cells rather than the typical bacillary forms predominated during exponential phase. These myceloids did not undergo complete septation and persisted into stationary phase. Similar responses were observed with potassium sulphate as the exogenous solute but less dramatic morphological effects were found with added polyethylene glycol or sucrose. The myceloids formed in response to osmotic stress could not be disrupted mechanically but were more sensitive than normal cells to lysozyme, particularly during stationary phase. Addition of osmoprotective compounds such as proline, glutamate, glycine betaine, or trehalose to the growth medium did not significantly relieve the effects of osmotic stress on growth rate or morphology. A. simplex also formed myceloid cells during osmotic stress but A. crystallopoietes did not. These results indicate that arthrobacters exhibit characteristic responses to osmotic stress and suggest these bacteria may contain novel osmoprotective compounds.

Arthrobacter↗

PubMed1992

Cloning and sequence analysis of genes for dehalogenation of 4-chlorobenzoate from Arthrobacter sp. strain SU.

Strains of Arthrobacter catalyze a hydrolytic dehalogenation of 4-chlorobenzoate (4-CBA) to p-hydroxybenzoate. The reaction requires ATP and coenzyme A (CoA), indicating activation of the substrate via a thioester, like that reported for Pseudomonas sp. strain CBS3 (J. D. Scholten, K.-H. Chang, P. C. Babbit, H. Charest, M. Sylvestre, and D. Dunaway-Mariano, Science 253:182-185, 1991). The dehalogenase genes of Arthrobacter sp. strain SU were cloned and expressed in Escherichia coli. Analyses of deletions indicate that dehalogenation depends on three open reading frames (ORFs) which are organized in an operon. There is extensive sequence homology to corresponding gene products in Pseudomonas sp. strain CBS3, suggesting that ORF1 and ORF2 encode a 4-CBA-CoA-ligase and a 4-CBA-CoA dehalogenase, respectively. ORF3 possibly represents a thioesterase, although no homology to the enzyme from Pseudomonas sp. strain CBS3 exists.

Amino Acid Sequence↗