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PubMed1964

USE OF ARTHROBACTER TERREGENS FOR BIOASSAY OF MYCOBACTIN.

Reich, Claude V. (Johns Hopkins-Leonard Wood Memorial Leprosy Research Laboratory, Johns Hopkins University, Baltimore, Md.), and John H. Hanks. Use of Arthrobacter terregens for bioassay of mycobactin. J. Bacteriol. 87:1317-1320. 1964.-Arthrobacter terregens was used to assay mycobactin, a growth factor for Mycobacterium paratuberculosis. Within 7 days, A. terregens gave a linear photometric growth response to mycobactin in the range of 0.05 to 0.2 mug/ml. Preparations found to be active (or inactive) by this assay produced corresponding effects on the growth of M. paratuberculosis after 6 weeks to 4 months. Mycobactin was produced routinely from pellicles of M. phlei on a peptone-glycerol-beef heart infusion medium, and was extracted from both cells and medium by organic solvents. The mycobactin content per cell rose rapidly after the third day and attained a maximum at 4 to 6 days. The decline to less than one-half this value by the tenth day was associated with excretion into the medium. Production on synthetic media occurred after increasing the usual levels of asparagine. The demonstrated effects of crude mycobactin on the donor strain were (i) to catalyze the onset of growth and (ii) to reverse the effect of conditions which cause the formation of abnormal cells.

Animals↗
PubMed2004

Effect of temperature and pH on the toxicity of aluminium towards two new, soil born species of Arthrobacter sp.

Two coryneform bacteria Arthrobacter sp. PI/1-95 (Arth1) and Arthrobacter sp. PI/3-95 (Arth3) were isolated from forest soil characterized and investigated with respect to their reaction towards aluminium (Al). Sigmoid functions were used to describe dose-response relationships between Al concentration and microbial growth and to calculate EC-values. EC(100) -- indicating a complete inhibition of microbial growth -- varied between 185 microM Al for Arth1 and 11 mM Al for Arth3. A pure pH effect seems probable in connection with the sensitive Arth1 but not with the tolerant species Arth3. Temperature was shown to distinctly increase the toxic effects of Al towards Arth3 whereas only a moderate modification in Al-toxicity was observed with Arth1.

Aluminum↗
PubMed1989

Nitrogen metabolism in the facultative methylotroph Arthrobacter P1 grown with various amines or ammonia as nitrogen sources.

The metabolism of trimethylamine (TMA) and dimethylamine (DMA) in Arthrobacter P1 involved the enzymes TMA monooxygenase and trimethylamine-N-oxide (TMA-NO) demethylase, and DMA monooxygenase, respectively. The methylamine and formaldehyde produced were further metabolized via a primary amine oxidase and the ribulose monophosphate (RuMP) cycle. The amine oxidase showed activity with various aliphatic primary amines and benzylamine. The organism was able to use methylamine, ethylamine and propylamine as carbon- and nitrogen sources for growth. Butylamine and benzylamine only functioned as nitrogen sources. Growth on glucose with ethylamine, propylamine, butylamine and benzylamine resulted in accumulation of the respective aldehydes. In case of ethylamine and propylamine this was due to repression by glucose of the synthesis of the aldehyde dehydrogenase(s) required for their further metabolism. Growth on glucose/methylamine did not result in repression of the RuMP cycle enzyme hexulose-6-phosphate synthase (HPS). High levels of this enzyme were present in the cells and as a result formaldehyde did not accumulate. Ammonia assimilation in Arthrobacter P1 involved NADP-dependent glutamate dehydrogenase (GDH), NAD-dependent alanine dehydrogenase (ADH) and glutamine synthetase (GS) as key enzymes. In batch cultures both GDH and GS displayed highest levels during growth on acetate with methylamine as the nitrogen source. A further increase in the levels of GS, but not GDH, was observed under ammonia-limited growth conditions in continuous cultures with acetate or glucose as carbon sources.

Amines↗
PubMed1984

Isolation and partial characterization of plasmid DNA from Arthrobacter oxidans.

A method for the extraction of the high molecular weight plasmid AO 1 from the gram-positive soil bacterium Arthrobacter oxidans is presented. Following digestion of this DNA with the restriction endonucleases AccI, Bam HI, Eco RI and Hind III, an average molecular mass of 157.8 kb was estimated. This value is in good agreement with the 160 kb size determined previously by electron microscopy (Brandsch et al. 1982). Using the same method, no plasmid DNA was found in strains of the genus Arthrobacter which do not degrade nicotine, e.g., A. albidus, A. globiformis and A. auricans.

Arthrobacter↗
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↗
PubMed2005

Utilization of homoserine lactone as a sole source of carbon and energy by soil Arthrobacter and Burkholderia species.

Homoserine lactone (HSL) is a ubiquitous product of metabolism. It is generated by all known biota during the editing of certain mischarged aminoacyl-tRNA reactions, and is also released as a product of quorum signal degradation by bacterial species expressing acyl-HSL acylases. Little is known about its environmental fate over long or short periods of time. The mammalian enzyme paraoxonase, which has no known homologs in bacteria, has been reported to degrade HSL via a lactonase mechanism. Certain strains of Variovorax and Arthrobacter utilize HSL as a sole source of nitrogen, but not as a sole source of carbon or energy. In this study, the enrichment and isolation of four strains of soil bacteria capable of utilizing HSL as a carbon and energy source are described. Phylogenetic analysis of these isolates indicates that three are distinct members of the genus Arthrobacter, whereas the fourth clusters within the non-clinical Burkholderia. The optimal pH for growth of the isolates ranged from 6.0 to 6.5, at which their HSL-dependent doubling times ranged from 1.4 to 4 h. The biodegradation of HSL by these 4 isolates far outpaced its chemical decay. HSL degradation by soil bacteria has implications for the consortial mineralization of acyl-homoserine lactones by bacteria associated with quorum sensing populations.

4-Butyrolactone↗
PubMed2004

Hyper-production of an isomalto-dextranase of an Arthrobacter sp. by a proteases-deficient Bacillus subtilis: sequencing, properties, and crystallization of the recombinant enzyme.

Arthrobacter globiformis T6 is unique in that it produces an enzyme yielding only isomaltose from dextran. In the present study, the organism was re-identified and its classification as a new species of the genus Arthrobacter, A. dextranlyticum, was proposed. The high G+C gene (66.8 mol%) for the isomalto-dextranase was sequenced. The deduced amino acid sequence, with a calculated molecular mass of 65,993 Da (603 amino acids), was confirmed by nanoscale capillary liquid chromatography coupled to tandem mass spectrometry, which covered 71.1% of the amino acid residues of the entire sequence. The enzyme was grouped into glycoside hydrolase family 27, and the C-terminal domain has homology to carbohydrate-binding module family 6. Hyper-exoproduction of the recombinant enzyme was achieved at a level corresponding to approximately 4.6 g l(-1) of culture broth when proteases-deficient Bacillus subtilis cells were used as the host. The purified enzyme (65.5 kDa) had an optimal pH and temperature for activity of 3.5 and 60 degrees C, respectively. It was crystallized using the sitting-drop vapor-diffusion method at 293 K.

Amino Acid Sequence↗
PubMed1999

Manipulation of the DNA coding for the desulphurizing activity in a new isolate of Arthrobacter sp.

A new bacterial strain able to cleave C-S bonds from organosulphur heterocyclic compounds through the 4-S pathway and tentatively classified as Arthrobacter sp. was recently isolated. In the present short article we describe the cloning and the characterization of the DNA encoding the enzymes responsible for desulphurization in this microorganism, referred to as Arthrobacter sp. DS7. The desulphurization operon was found to be located in a large plasmid that also bears the genes conferring cadmium and arsenic resistance. By shortening this plasmid, a new cloning vector was prepared and used to obtain a recombinant derivative strain that desulphurizes dibenzothiophene despite of the presence of inorganic sulphur in the growth medium.

Arthrobacter↗
PubMed2004

Effect of chromium(VI) action on Arthrobacter oxydans.

Arthrobacter species is of interest because of its high potential for bioremediation. Bacteria can detoxify chromium, by either reduction or accumulation inside the bacteria and/or absorption of chromium(VI) (CrVI) on their surface, and efflux pump. The possible pathway of Cr(VI) reduction by Arthrobacter oxydans isolated from Columbia basalt rocks at a US DOE highly contaminated site (USA) has been considered in the present study. FTIR absorption spectroscopy showed that these bacteria reduce Cr(VI). In the present study the threshold Cr(VI) nontoxic concentration (35 microg/mL) for A. oxydans growing in liquid medium was estimated. Complete uptake of this concentration was achieved in about 10 days after chromium addition into the medium. At this concentration an increase in the protein isolated from the cell wall of A. oxydans was observed. This increased protein predominated independently of the growth phase at which Cr(VI) was added. Thermal analysis was used to identify any influence of Cr(VI) on the DNP complex of A. oxydans. According to the data obtained it can be supposed that Cr(VI) reduction predominantly occurs on the bacterial surface and that cell wall represents a permeable barrier for these bacteria at the non-toxic chromium action.

Arthrobacter↗
PubMed2005

Isolation and characterization of a fructosyl-amine oxidase from an Arthrobacter sp.

An Arthrobacter sp. was isolated that, when induced by fructosyl-valine, expressed a fructosyl-amine oxidase (FAOD) that was specific for alpha-glycated amino acids. The N-terminal amino acid sequence of the purified oxidase was determined and used to design oligonucleotides to amplify the gene by inverse PCR. Expression of the gene in Escherichia coli produced 0.23 units FAOD per mg protein, over 30-fold greater than native expression levels, with properties almost indistinguishable from the native enzyme. The presence of FAOD was confirmed in other Arthrobacter ssp.

Amino Acid Oxidoreductases↗
PubMed2005

Depolymerisation and biodegradation of a synthetic tanning agent by activated sludges, the bacteria Arthrobacter globiformis and Comamonas testosteroni, and the fungus Cunninghamella polymorpha.

Degradation of a synthetic tanning agent CNSF (a condensation product of 2-naphthalenesulfonic acid (2-NSA) and formaldehyde) by four activated sludges, two previously characterised bacterial strains, Arthrobacter sp. 2AC and Comamonas sp. 4BC, and the fungus Cunninghamella polymorpha, was studied in batch culture at 25 degrees C by determining the changes in the concentrations of CNSF and its component monomers and oligomers (n2-n11). The loss of individual oligomers was correlated with the length of the NSA-CH2 chain. Approximately 25% of the total CNSF was degraded (i.e. mineralised) by the microbes contained in the four activated sludges and by the two bacterial isolates but with different lag phases and at different overall rates. The decline in CNSF concentration was due almost entirely to the biodegradation of the monomers (34.3% of CNSF) and, in particular, 2-NSA (27% of CNSF). There was no change in the n2-n11 components. The growth of C. polymorpha, on the other hand, arose from extracellular depolymerisation of CNSF oligomers and the biodegradation of the lower molecular mass products. Between 38% and 42% of total CNSF was degraded by C. polymorpha at 25 degrees C. The order of oligomer degradation was inversely related to degree of polymerisation. Eighty percent and 90% of the n4 and n5 and 100% oligomers n6-n11 were degraded after 120 h. At a higher temperature (37 degrees C) oligomers n4-n11 were degraded completely after 120 h. A combination of biodegradation (75%) and sorption to fungal biomass (25%) accounted for the measured loss of all oligomers from the solution phase. The CNSF degradation rates and the volume of fungal biomass produced (and therefore the extent of biosorption) were dependent on the presence of a second carbon source (both optimum at glucose 5 g/l). This is the first report that identifies and distinguishes between depolymerisation, sorption and biodegradation processes in the removal of CNSF and its component oligomers. The use of combinations of the depolymerising fungus C. polymorpha, and the monomer-degrading bacteria, Arthrobacter sp. 2AC and Comamonas sp. 4BC, have potential for wastewater treatment.

Adsorption↗
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↗
PubMed1993

Overproduction of riboflavin by an Arthrobacter sp. mutant resistant to 5-fluorouracil.

Antagonistic action between 5-fluorouracil (5-FU) and riboflavin (RF) was investigated. The growth of Arthrobacter sp. was inhibited by 5-FU at 5 x 10(-5) M, and the inhibition was reversed by RF at 5 x 10(-5) M. 5-FU-resistant mutants of Arthrobacter sp. were isolated and excreted RF in relatively high yields, but the wild-type strain excreted no RF. One of the mutants, strain No. 28-35, produced 223.2 micrograms ml-1 of RF in culture medium at 4 days.

Arthrobacter↗
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↗
PubMed2006

Optimization of MALDI-TOF MS for strain level differentiation of Arthrobacter isolates.

Matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) has been shown to be a rapid and sensitive method for characterization of bacteria, but it has not yet become a routine microbiological procedure. Currently there are no standardized protocols that would allow development of large libraries of reproducible protein profiles from a broad range of microorganisms to use for identification purposes. Important variables that may affect spectrum quality are MALDI matrices, solvents, cell growth condition, and culture age. In the present study our aim was to: (1) to determine optimal sample preparation and MALDI conditions for discrimination at the strain level; (2) to determine if changes in growth cycle correlated with MALDI spectrum changes; and (3) to compare level of isolate discrimination based on their MALDI spectra versus their 16S rRNA gene sequence. Using 16 strains of the Gram positive bacterium Arthrobacter, optimal spectra were obtained using two-layer sample application of intact cells grown on solid surface overlaid with a matrix consisting of sinapinic acid (SA) or alpha-cyano-hydroxy-cinnaminic acid (CHCA) in 50:50 acetonitrile:water solvent with 2% trifluoroacetic acid. Spectrum changes paralleled the coccus-rod-coccus growth cycle indicative of Arthrobacter. Strain differences based on their MALDI profiles (using Pearson coefficient and UPGMA) corresponded with their 16S rRNA gene phylogeny but it had greater discrimination.

Arthrobacter↗
PubMed2000

Cloning and nucleotide sequence of a gene encoding a glycogen debranching enzyme in the trehalose operon from Arthrobacter sp. Q36.

A gene located just upstream of the treYZ operon was isolated from Arthrobacter sp. strain Q36. The gene, designated treX, encoded an 823-amino acid protein. The amino acid sequence of the protein had 50% identity with the TreX protein (isoamylase) from Sulfolobus acidocaldarius ATCC 33909 which has a treZXY operon on the genome. We suggest that Arthrobacter treX is an isoamylase gene, and that it is a component of a treXYZ operon.

Amino Acid Sequence↗
PubMed2003

Biotransformations of propenylbenzenes by an Arthrobacter sp. and its t-anethole blocked mutants.

Propenylbenzenes are often used as starting materials in the chemical synthesis of aroma compounds and fine chemicals. In the present study, we demonstrate the ability of an Arthrobacter sp. to transform various structures of propenylbenzenes derived from essential oils to flavor, fragrance, and fine chemicals. Arthrobacter strain TA13 and its t-anethole blocked mutants (incapable of growing on t-anethole) converted isoeugenol to vanillin and vanillic acid; and safrole to hydroxychavicol. High conversion efficiencies were achieved in the biotransformations of isosafrole to piperonylic acid, and eugenol to a mixture of ferulic acid and vanillic acid. In addition, anisic acid was produced in high yields from t-anethole, anisyl alcohol, or anisaldehyde. The accumulation of the corresponding aromatic acids from the tested propenylbenzenes is due to the lack of m-demethylase activity in strain TA13 that prevents further cleavage of the benzene ring. Interestingly, in the transformation of eugenol (a 2-propenylbenzene) the side chain was initially oxidized to the corresponding cinamic acid derivative (ferulic acid) while the 1-propenylbenzenes gave substituted benzoic acids, suggesting two different chain shortening mechanisms.

Allylbenzene Derivatives↗
PubMed1999

Effects of moisture and sorption on bioavailability of p-hydroxybenzoic acid to Arthrobacter sp. in soil.

Effects of bioavailability on degradation of 14C-p-hydroxybenzoate were examined using sterile soil inoculated with Arthrobacter sp. Physical accessibility of p-hydroxybenzoate was controlled by varying pore continuity with a range of moisture regimes (-33 to -420 kPa), whereas sorption was controlled via addition of an exchange resin. Arthrobacter sp. accessed 94% of p-hydroxybenzoate in soil at -33 kPa, owing to continuity of soil pores and sufficient cells to exploit available space. A deviation in degradation kinetics at -420 kPa soil was attributed to inaccessible p-hydroxybenzoate in solution. Addition of resin decreased extent of degradation, though the effect diminished as pore continuity decreased. Subtle differences in effects of these processes on degradation kinetics may facilitate their separate treatment in environmental fate models.

Absorption↗