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PubMed1999

Biodegradation of 2-methyl, 2-ethyl, and 2-hydroxypyridine by an Arthrobacter sp. isolated from subsurface sediment.

A bacterium capable of degrading 2-methylpyridine was isolated by enrichment techniques from subsurface sediments collected from an aquifer located at an industrial site that had been contaminated with pyridine and pyridine derivatives. The isolate, identified as an Arthrobacter sp., was capable of utilizing 2-methylpyridine, 2-ethylpyridine, and 2-hydroxypyridine as primary C, N, and energy sources. The isolate was also able to utilize 2-, 3-, and 4-hydroxybenzoate, gentisic acid, protocatechuic acid and catechol, suggesting that it possesses a number of enzymatic pathways for the degradation of aromatic compounds. Degradation of 2-methylpyridine, 2-ethylpyridine, and 2-hydroxypyridine was accompanied by growth of the isolate and release of ammonium into the medium. Degradation of 2-methylpyridine was accompanied by overproduction of riboflavin. A soluble blue pigment was produced by the isolate during the degradation of 2-hydroxypyridine, and may be related to the diazadiphenoquinones reportedly produced by other Arthrobacter spp. when grown on 2-hydroxypyridine. When provided with 2-methylpyridine, 2-ethylpyridine, and 2-hydroxypyridine simultaneously, 2-hydroxypyridine was rapidly and preferentially degraded; however there was no apparent biodegradation of either 2-methylpyridine or 2-ethylpyridine until after a seven day lag. The data suggest that there are differences between the pathway for 2-hydroxypyridine degradation and the pathways(s) for 2-methylpyridine and 2-ethylpyridine.

Arthrobacter↗
PubMedDate not supplied

A strain of Arthrobacter that tolerates high concentrations of nitrate.

A gram-positive strain identified as Arthrobacter globiformis CECT 4500, tolerant to up to 1 M nitrate, was isolated from the grounds of a munitions factory. Under strict aerobic conditions, this bacterium used a wide variety of C-sources to obtain the energy required for growth, which took place when the nitrate concentration in the medium was below 150 mM. Cells of this bacterium growing in the absence of nitrate were seen as individual cells or forming pairs, whereas cells grown in the presence of nitrate formed short filaments. With ethylene glycol as the C-source, optimal conditions for the full nitrate removal by Arthrobacter were established under laboratory conditions with wastewaters from the synthesis of dinitroethylene glycol.

Arthrobacter↗
PubMed2003

Influence of Al on growth, cell size and content of intracellular water of Arthrobacter sp. PI/1-95.

A distinct inhibition of the growth of a typical soil-born bacterium, Arthrobacter sp. PI/1-95, by aluminium was established. The content of intracellular water and (consequently) the cell size of the bacterium significantly increased when cells came into contact with aluminium. Both parameters were also increased when applying HCl, but Al caused the greater change, so that a distinct discrimination between the effects of aluminium on the one hand and a sole pH-effect on the other hand was possible. The presented results point to an osmo-regulative disorder connected with a malfunction of cell membrane and cell wall, which seems to be a probable mechanism for an Al-toxicity in connection with Arthrobacter sp. PI/1-95.

Aluminum↗
PubMed2000

Degradation of o-methoxybenzoate by a two-member consortium made up of a gram-positive Arthrobacter strain and a gram-negative Pantotea strain.

Aromatic carboxylic acids substituted with methoxylated groups are among the most abundant products in "alpechin", the wastes resulting from pressing olives to obtain olive oil. Degradation of o-methoxybenzoate by an stable consortium made of a gram positive bacterium, Arthrobacter oxydans, and gram negative one, Pantotea agglomerans, was shown to mineralize this compound efficiently. The concerted action of both microorganisms was needed for the two first steps in the process, namely, the conversion of o-methoxybenzoate into salycilate, and the hydroxylation of the latter to gentisate. Gentisate was further degraded by the Arthrobacter strain.

Anisoles↗
PubMed2004

The purification and characterisation of 4-chlorobenzoate:CoA ligase and 4-chlorobenzoyl CoA dehalogenase from Arthrobacter sp. strain TM-1.

4-Chlorobenzoate:CoA ligase, the first enzyme in the pathway for 4-chlorobenzoate dissimilation, has been partially purified from Arthrobacter sp. strain TM-1, by sequential ammonium sulphate precipitation and chromatography on DEAE-Sepharose and Sephacryl S-200. The enzyme, a homodimer of subunit molecular mass approximately 56 kD, is dependent on Mg2+-ATP and coenzyme A, and produces 4-chlorobenzoyl CoA and AMP. Besides Mg2+, Mn2+, Co2+, Fe2+ and Zn2+ are also stimulatory, but not Ca2+. Maximal activity is exhibited at pH 7.0 and 25 degrees C. The ligase demonstrates broad specificity towards other halobenzoates, with 4-chlorobenzoate as best substrate. The apparent Michaelis constants (Km) of the enzyme for 4-chlorobenzoate, CoA and ATP were determined as 3.5, 30 and 238 microM respectively. 4-Chlorobenzoyl CoA dehalogenase, the second enzyme, has been purified to homogeneity by sequential column chromatography on hydroxyapatite, DEAE-Sepharose and Sephacryl S-200. It is a homotetramer of 33 kD subunits with an isoelectric point of 6.4. At pH 7.5 and 30 degrees C, Km and kcat for 4-CBCoA are 9 microM and 1 s(-1) respectively. The optimum pH is 7.5, and maximal enzymic activity occurs at 45 degrees C. The properties of this enzyme are compared with those of the 4-chlorobenzoyl CoA dehalogenases from Arthrobacter sp. strain 4-CB1 and Pseudomonas sp. strain CBS-3, which differ variously in their N-terminal amino acid sequences, optimal pH values, pI values and/or temperatures of maximal activity.

Arthrobacter↗
PubMed1991

D-Xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728. Gene cloning, sequence and expression.

Arthrobacter strain N.R.R.L. B3728 superproduces a D-xylose isomerase that is also a useful industrial D-glucose isomerase. The gene (xylA) that encodes it has been cloned by complementing a xylA mutant of the ancestral strain, with the use of a shuttle vector. The 5' region shows strong sequence similarity to Escherichia coli consensus promoters and ribosome-binding sequences and allows high levels of expression in E. coli. The coding sequence shows similarity to those for other D-xylose isomerases and is followed by 22 nucleotide residues with stop codons in each reading frame, a good 'consensus' ribosome-binding site and an open reading frame showing similarity to those of known D-xylulokinases (xylB). Studies on the expression of the cloned gene in Arthrobacter and in E. coli suggest that the two genes are part of a xyl operon regulated by a repressor that is defective in strain B3728. Codon usage in these two genes, and in another open reading frame (nxi) that was adventitiously isolated during early cloning attempts, shows some characteristic omissions and a strong G + C preference in redundant positions.

Aldose-Ketose Isomerases↗
PubMed2001

Organization of the genes involved in dimethylglycine and sarcosine degradation in Arthrobacter spp.: implications for glycine betaine catabolism.

The nucleotide sequences of two cloned DNA fragments containing the structural genes of heterotetrameric sarcosine oxidase (soxBDAG) and dimethylglycine dehydrogenase (dmg) from Arthrobater spp. 1-IN and Arthrobacter globiformis, respectively, have been determined. Open reading frames were identified in the soxBDAG operon corresponding to the four subunits of heterotetrameric sarcosine oxidase by comparison with the N-terminal amino-acid sequences and the subunit relative molecular masses of the purified enzyme. Alignment of the deduced sarcosine oxidase amino-acid sequence with amino-acid sequences of functionally related proteins indicated that the arthrobacterial enzyme is highly homologous to sarcosine oxidase from Corynebacterium P-1. Deletion and expression analysis, and alignment of the deduced amino-acid sequence of the dmg gene, showed that dmg encodes a novel dimethylglycine oxidase, which is related to eukaryotic dimethylglycine dehydrogenase, and contains nucleotide-binding, flavinylation and folate-binding motifs. The recombinant dimethylglycine oxidase was purified to homogeneity and characterized. The DNA located upstream and downstream of both the soxBDAG and dmg genes is predicted to encode enzymes involved in the tetrahydrofolate-dependent assimilation of methyl groups. Based on the sequence analysis reported herein, pathways are proposed for glycine betaine catabolism in Arthrobacter species, which involve the identified folate-dependent enzymes.

Amino Acid Sequence↗
PubMed1998

A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization.

The gene encoding low specificity D-threonine aldolase, catalyzing the interconversion of D-threonine/D-allo-threonine and glycine plus acetaldehyde, was cloned from the chromosomal DNA of Arthrobacter sp. strain DK-38. The gene contains an open reading frame consisting of 1,140 nucleotides corresponding to 379 amino acid residues. The enzyme was overproduced in recombinant Escherichia coli cells and purified to homogeneity by ammonium sulfate fractionation and three-column chromatography steps. The recombinant aldolase was identified as a pyridoxal enzyme with the capacity of binding 1 mol of pyridoxal 5'-phosphate per mol of subunit, and Lys59 of the enzyme was determined to be the cofactor binding site by chemical modification with NaBH4. In addition, Mn2+ ion was demonstrated to be an activator of the enzyme, although the purified enzyme contained no detectable metal ions. Equilibrium dialysis and atomic absorption studies revealed that the recombinant enzyme could bind 1 mol of Mn2+ ion per mol of subunit. Remarkably, the predicted amino acid sequence of the enzyme showed no significant similarity to those of the currently known pyridoxal 5'-phosphate-dependent enzymes, indicating that low specificity D-threonine aldolase is a new pyridoxal enzyme with a unique primary structure. Taken together, low specificity D-threonine aldolase from Arthrobacter sp. strain DK-38, with a unique primary structure, is a novel metal-activated pyridoxal enzyme.

Amino Acid Sequence↗
PubMed2006

Studies on biodegradation of nicotine by Arthrobacter sp. strain HF-2.

A nicotine-degrading bacterium, strain HF-2, was isolated from tobacco waste-contaminated soil and identified as a member of Arthrobacter sp. based on morphology, physiological tests, 16S rDNA sequence and phylogenetic characteristics. At thermal denaturation test indicated that the G + C mol% of strain HF-1 was 63.5. The relationship between the growth of the isolate and the nicotine degradation suggested that strain HF-2 could utilize nicotine as sole sources of carbon, nitrogen and energy. Blue pigment was observed during the nicotine degradation by strain HF-2. The isolate grew well at 20 to 33 degrees C, initial pH 6.5 to 8.0 and 0.5 to 2.0 g L-1 of nicotine concentration in the nicotine inorganic salt media. The maximum growth and nicotine degradation occurred at 30 degrees C, initial pH 7.0 and 0.7 g.L-1 of nicotine concentration in media under natural incubation condition. Strain HF-2 could degrade 100% of nicotine under the optimized incubation conditions for 43 h. The concentrations of nicotine were monitored by high performance liquid chromatography. This study demonstrates Arthrobacter sp. strain HF-2 had a great ability to degrade nicotine, and it may be available for the application to the bioremediation of environments contaminated by tobacco waste.

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↗
PubMed1987

Comparison of backbone structures of glucose isomerase from Streptomyces and Arthrobacter.

The C alpha backbones of the glucose isomerase molecules of Streptomyces rubiginosus and Arthrobacter have been determined by X-ray crystallography and compared. Each molecule is a tetramer of eight-stranded alpha/beta barrels, and the mode of association of the tetramers is identical in each case. The Arthrobacter electron density shows four additional amino acids at the carboxyl terminus. There is also an insertion of six amino acids at position 277, and two individual insertions at about positions 348 and 357 (numbering according to the Streptomyces structure). There is a close structural homology throughout the whole molecule, which is most accurate up to position 325. The r.m.s. displacement for 315 homologous C alpha positions up to this position is 0.92 A.

Aldose-Ketose Isomerases↗
PubMed2000

Arthrobacter chlorophenolicus sp. nov., a new species capable of degrading high concentrations of 4-chlorophenol.

A micro-organism was isolated from soil which could grow on high concentrations [up to 350 p.p.m. (2.7 mM)] of 4-chlorophenol (4-CP). The isolate, designated strain A6T, was obtained from a soil suspension that had been selectively enriched with gradually increasing concentrations of 4-CP. Strain A6T could also grow on several other para-substituted phenols. Characterization of strain A6T with respect to chemical, biochemical and morphological properties, 16S rDNA sequencing and DNA-DNA hybridization indicated that the isolate is a novel species within the genus Arthrobacter for which the name Arthrobacter chlorophenolicus sp. nov. is proposed. The type strain is DSM 12829T.

Arthrobacter↗
PubMed2001

Arthrobacter siderocapsulatus Dubinina and Zhdanov 1975AL is a later subjective synonym of Pseudomonas putida (Trevisan 1889) Migula 1895AL.

The taxonomic position of Arthrobacter siderocapsulatus Dubinina and Zhdanov 1975AL was investigated using 16S rDNA, fatty acid and phenotypic analyses. The type strain (NCIMB 11286T) showed 99.85% 16S rDNA similarity to the type strain of Pseudomonas putida. Phenotypic properties of the two strains were compared using API 20NE and BIOLOG kits. Identical reactions were recorded for all tests, except for assimilation of malonic acid. The two strains also showed almost identical cellular fatty acid profiles. On the basis of evidence presented in this and earlier studies, it is proposed that Arthrobacter siderocapsulatus is a later subjective synonym of Pseudomonas putida (Trevisan 1889) Migula 1895AL.

Arthrobacter↗
PubMed1988

A host-vector system for an Arthrobacter species.

An efficient host-vector system has been developed for an industrial strain of Arthrobacter sp. (NRRL B3728)used for glucose isomerase production. Protoplasts of Arthrobacter were generated by treating the cells with 0.5 mg lysozyme ml(-1) for 60 min in a solution containing 0.5 M-sucrose. Around 30% of the protoplasts regenerated on agar containing 0.5 M-sodium succinate as osmotic stabilizer. Three hybrid vectors, PBL2100, pCG1100 and pCG2100, were constructed by combining the Escherichia coli plasmid pBR322, a kanamycin- resistance gene from pNCAT4 and a cryptic plasmid from either Brevibacterium lactofermentum NCIB 9567 or Corynebacterium glutamicum NCIB 10026. These vectors transformed the protoplasts and expressed the kanamycin-resistance gene for screening. They contain a number of unique restrictions sites for cloning of foreign DNA. The transformation frequency of this system was 10(5)-10(6) transformants per micrograms of input plasmid and ws constant up to 5 micrograms of DNA. the probability of a plasmid transforming a plasmid transforming a protoplast was in the range 10(-5)-10(-6). The copy number of pBL2100 was around 5 per cell and those of pCG1100 and pCG2100 were around 33 per cell. Deletion mutants were generated from pCG2100. One of them, pCG2120, was able to transform protoplasts of strain NRRL B3728. Plasmids pBL2100 and pCG2100 were structurally stable in cells of NRRL B3728 but could not be maintained in non-selective medium. They segregated at a rate of 12.2 and 2.2% per generation respectively.

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↗
PubMed1995

Molecular cloning, expression in Streptomyces lividans, and analysis of a gene cluster from Arthrobacter simplex encoding 3-ketosteroid-delta 1-dehydrogenase, 3-ketosteroid-delta 5-isomerase and a hypothetical regulatory protein.

The Arthrobacter simplex gene coding for 3-ketosteroid-delta 1-dehydrogenase, a key enzyme in the degradation of the steroid nucleus, was cloned in Streptomyces lividans. Nucleotide sequence analysis revealed that the gene for 3-ketosteroid-delta 1-dehydrogenase (ksdD) is clustered with at least two more genes possibly involved in steroid metabolism. Upstream of ksdD, we found a gene, ksdR, encoding a hypothetical regulatory protein that shows homologies to KdgR, the negative regulator of pectin biodegradation in Erwinia, and GyIR, the activator for glycerol metabolism in Steptomyces. A helix-turn-helix DNA-binding domain can be predicted at similar positions near the N-terminal of KsdR, KdgR and GyIR. ksdl adjoining downstream to ksdD codes for a protein that has strong similarities to 3-ketosteroid-delta 5-isomerases. The highly conserved Tyr and Asp residues are present in the active-centre motif of the enzyme. The translated ksdD gene product was found to be similar to the 3-ketosteroid-delta 1-dehydrogenase of Pseudomonas testosteroni and to the fumarate reductase of Shewanella putrefaciens. A region highly conserved between the two steroid dehydrogenases can be aligned to the active-centre motif of the fumarate reductase. S. lividans strains carrying the ksdD gene overexpressed 3-ketosteroid-delta 1-dehydrogenase. The expression of 3-ketosteroid-delta 5-isomerase, however, was barely detectable in recombinant S. lividans strains carrying the ksdl gene, or in the parental Arthrobacter strain.

Amino Acid Sequence↗
PubMed1987

Metabolism of glyphosate in an Arthrobacter sp. GLP-1.

The metabolism of glyphosate [N-(phosphonomethyl)glycine] in a bacterium tentatively identified as an Arthrobacter sp., capable of growth on this herbicide as its sole phosphorus source, has been investigated using solid-state NMR techniques as well as radiotracer analysis. The pathway involves the conversion of glyphosate to glycine, a C1 unit and phosphate. The phosphonomethyl carbon is specifically incorporated into the amino acids serine, cysteine, methionine, and histidine, as well as into purine bases and thymine, indicating the involvement of tetrahydrofolate in single-carbon transfer reactions. Glycine derived from glyphosate is utilized in purine and protein biosynthesis. This pathway for glyphosate degradation in a gram-positive bacterium is similar to that previously reported for Pseudomonas sp. PG2982 [Jacob et al. (1985) J. Biol. Chem. 260, 5899-5905] and is distinct from that reported for soil metabolism of glyphosate where aminomethylphosphonic acid has been shown to be a major metabolite. Preliminary evidence is presented which indicates that the conversion of glyphosate to glycine and the C1 unit involves the intermediate formation of sarcosine. Thus, the primary event in glyphosate degradation by Arthrobacter sp. GLP-1 is the cleavage of its C-P bound. This report constitutes the first demonstration of the metabolism of glyphosate in a gram-positive bacterium.

Arthrobacter↗