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PubMed1997

Biological potential of extraterrestrial materials. 2. Microbial and plant responses to nutrients in the Murchison carbonaceous meteorite.

Meteoritic materials are investigated as potential early planetary nutrients. Aqueous extracts of the Murchison C2 carbonaceous meteorite are utilized as a sole carbon source by microorganisms, as demonstrated by the genetically modified Pseudomonas fluorescence equipped with the lux gene. Nutrient effects are observed also with the soil microorganisms Nocardia asteroides and Arthrobacter pascens that reach populations up to 5 x 10(7) CFU/ml in meteorite extracts, similar to populations in terrestrial soil extracts. Plant tissue cultures of Asparagus officinalis and Solanum tuberosum (potato) exhibit enhanced pigmentation and some enhanced growth when meteorite extracts are added to partial nutrient media, but inhibited growth when added to full nutrient solution. The meteorite extracts lead to large increases in S, Ca, Mg, and Fe plant tissue contents as shown by X-ray fluorescence, while P, K, and Cl contents show mixed effects. In both microbiological and plant tissue experiments, the nutrient and inhibitory effects appear to be best balanced for growth at about 1:20 (extracted solid : H2O) ratios. The results suggest that solutions in cavities in meteorites can provide efficient concentrated biogenic and early nutrient environments, including high phosphate levels, which may be the limiting nutrient. The results also suggest that carbonaceous asteroid resources can sustain soil microbial activity and provide essential macronutrients for future space-based ecosystems.

Arthrobacter↗

PubMed2001

Modular structure, local flexibility and cold-activity of a novel chitobiase from a psychrophilic Antarctic bacterium.

The gene archb encoding for the cell-bound chitobiase from the Antarctic Gram-positive bacterium Arthrobacter sp. TAD20 was cloned and expressed in Escherichia coli in a soluble form. The mature chitobiase ArChb possesses four functionally independent domains: a catalytic domain stabilized by Ca(2+), a galactose-binding domain and an immunoglobulin-like domain followed by a cell-wall anchorage signal, typical of cell-surface proteins from Gram-positive bacteria. Binding of saccharides was analyzed by differential scanning calorimetry, allowing to distinguish unequivocally the catalytic domain from the galactose-binding domain and to study binding specificities. The results suggest that ArChb could play a role in bacterium attachment to natural hosts. Kinetic parameters of ArChb demonstrate perfect adaptation to catalysis at low temperatures, as shown by a low activation energy associated with unusually low K(m) and high k(cat) values. Thermodependence of these parameters indicates that discrete amino acid substitutions in the catalytic center have optimized the thermodynamic properties of weak interactions involved in substrate binding at low temperatures. Microcalorimetry also reveals that heat-lability, a general trait of psychrophilic enzymes, only affects the active site domain of ArChb.

Acetylglucosaminidase↗

PubMed1998

Corynebacterium striatum chloramphenicol resistance transposon Tn5564: genetic organization and transposition in Corynebacterium glutamicum.

The clinical isolate Corynebacterium striatum M82B (formerly Corynebacterium xerosis M82B) carries the 50-kb R-plasmid pTP10 conferring resistance to the antibiotics chloramphenicol, erythromycin, kanamycin, and tetracycline. DNA sequence analysis of the chloramphenicol resistance region revealed the presence of the 4155-bp transposable element Tn5564. The ends of Tn5564 are identical 22-bp inverted repeats flanked by a 6-bp target site duplication. The central region of Tn5564 encodes the chloramphenicol resistance gene cmx, specifying a transmembrane chloramphenicol efflux protein, and an open reading frame homologous to transposases of insertion sequences identified in Arthrobacter nicotinovorans and Bordetella pertussis. Furthermore, the 1715-bp insertion sequence IS1513 encoding a putative transposase of the IS30 family is an integral part of Tn5564 and is located upstream of cmx. For transposon mutagenesis, Tn5564 was transferred to Corynebacterium glutamicum on a mobilizable Escherichia coli plasmid using RP4-mediated intergeneric conjugation. Transposition of Tn5564 in C. glutamicum occurred with a frequency of 3.3 x 10(-8) and resulted in an insertion into target sites containing the central palindromic tetranucleotide CTAG. A Tn5564-induced mutant strain of C. glutamicum was found to carry the transposon in the ftsZ gene region.

Amino Acid Sequence↗

PubMed1997

Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum.

Homoprotocatechuate (hpca, 3,4-dihydroxyphenylacetate) is a central intermediate for the bacterial degradation of aromatic compounds. Homoprotocatechuate 2,3-dioxygenase (HPCD) catalyzes the key ring cleavage step in the metabolism of hpca by the Gram (+) bacterium Brevibacterium fuscum to yield alpha-hydroxy-delta-carboxymethyl cis-muconic semialdehyde. A genomic DNA library of B. fuscum was constructed in Escherichia coli using a cosmid vector and screened by spraying the cells with hpca. One clone was found to contain the gene for HPCD based on its ability to convert hpca into the yellow-colored product. This cosmid clone was further subcloned and the gene for HPCD was localized and sequenced. The open reading frame codes for a protein with 365 amino acids and M(r) = 41,699, in accord with the characteristics of the previously purified wild-type enzyme. The gene for HPCD was overexpressed in E. coli to approximately 30% of the total soluble protein, and purification of the recombinant enzyme to apparent homogeneity was achieved by a two-step procedure. Iron was the only abundant metal found in the purified recombinant enzyme, and the specific activity per iron was comparable to that observed for the wild-type enzyme. The deduced amino acid sequence of HPCD has a very high level of homology (78.6% identity in the 337-aa overlap) to the manganese-dependent homoprotocatechuate 2,3-dioxygenase (MndD) from Arthrobacter globiformis CM-2. The basis for the difference in metal selection by HPCD and MndD was investigated by mutagenesis of a 50-base-pair region of the HPCD gene containing three frame shifts relative to the MndD gene. The purified triple mutant of HPCD did not exhibit a significant change in the metal content; therefore, other factors must contribute to the selection of the active site metal.

3,4-Dihydroxyphenylacetic Acid↗

PubMed2001

Neuraminidase from a bacterial source enhances both HIV-1-mediated syncytium formation and the virus binding/entry process.

Neuraminidases, also termed sialidases, which catalyze the removal of sialic acid residues from various glycoconjugates, have been previously reported to modulate HIV-1 replication. Given that some of the known opportunistic microbes found in patients infected with HIV-1 harbor neuraminidase (NA) activity, we speculated that pathogen-derived NA might be envisaged as an important factor in the pathogenesis of this retroviral infection. In the present study, we have monitored the putative modulation of HIV-1-mediated syncytium formation and virus replication by highly purified bacterial-derived NA from Arthrobacter ureafaciens. Taking advantage of a luciferase-based syncytium quantitative assay, we demonstrate here that the level of HIV-1-mediated syncytium formation is enhanced in the presence of NA and that it necessitates interaction between gp120 and CD4/chemokine coreceptor. By using pseudotyped recombinant luciferase-encoding HIV-1 particles, we found that NA treatment of human CD4-positive target cells (i.e., T lymphoid, monocytoid, and peripheral blood mononuclear cells) significantly augmented single-round infection by T- and macrophage-tropic isolates of HIV-1. The observed increase in HIV-1 infection was linked with an enhancement in the initial steps of the virus replicative cycle as monitored by viral binding and entry assays. Interestingly, NA treatment also enhances infectivity of HIV-1 pseudotypes with envelope glycoprotein from the amphotropic murine leukemia virus or the vesicular stomatitis virus. Taken together, our results provide useful information regarding the possible contribution of microbial agents carrying NA activity to HIV-1 pathogenesis.

Arthrobacter↗

PubMed1994

Expression of a bacterial gene in transgenic plants confers resistance to the herbicide phenmedipham.

Tobacco plants were genetically engineered to express a detoxifying pathway for the herbicide phenmedipham. A gene from Arthrobacter oxidans strain P52 that encodes an enzyme catalysing the hydrolytic cleavage of the carbamate compound phenmedipham has recently been cloned and sequenced. The coding sequence was fused with a cauliflower mosaic virus 35S promoter and introduced into tobacco plants by Agrobacterium-mediated gene transfer. Transgenic plants expressing high levels of phenmedipham hydrolase exhibited resistance when sprayed with the herbicide at up to ten times the usual field application rate.

Arthrobacter↗

PubMed1995

Transformation of Synechococcus with a gene for choline oxidase enhances tolerance to salt stress.

Choline oxidase, isolated from the soil bacterium Arthrobacter globiformis, converts choline to glycinebetaine (N-trimethylglycine) without a requirement for any cofactors. The gene for this enzyme, designated codA, was cloned and introduced into the cyanobacterium Synechococcus sp. PCC 7942. The codA gene was expressed under the control of a strong constitutive promoter, and the transformed cells accumulated glycinebetaine at intracellular levels of 60-80 mM. Consequently the cells acquired tolerance to salt stress, as evaluated in terms of growth, accumulation of chlorophyll and photosynthetic activity.

Adaptation, Physiological↗

PubMed1994

Evidence for the interference of aluminum with bacterial porphyrin biosynthesis.

Aluminum (0.74 mM) was found to retard bacterial growth, and enhance porphyrin formation and excretion in Arthrobacter aurescens RS-2. Coproporphyrin III was shown to be the main porphyrin excreted by aluminum-exposed A. aurescens RS-2 cultures and by RS-2 cultures grown under anoxic conditions. Synthesis and excretion of porphyrins in A. aurescens RS-2 increased in a dose-dependent manner when the bacteria were exposed to increasing aluminum concentrations. Incubation of A. aurescens RS-2 with delta-aminolevulinic acid (delta-ALA, 1.2 mM) brought about the intense formation and excretion of porphyrins by the cells, in the presence or absence of aluminum. delta-ALA slightly enhanced the toxicity of aluminum towards RS-2 bacteria. Furthermore, the intracellular concentration of heme was reduced by 63.9 +/- 8.67% in aluminum-exposed RS-2 bacteria when compared with control cultures. The results are discussed in light of the recent finding concerning aluminum toxicity and porphyrin biosynthesis in microorganisms.

Aluminum↗

PubMed1990

Sites of cadmium uptake in bacteria used for biosorption.

Electron microscopy and x-ray spectroscopy were used to determine location and type of cadmium biosorption on and in bacteria, some of which produced extracellular polymers. Examined Arthrobacter and Pseudomonas species appear to have detoxification systems that precipitate cadmium internally irrespective of whether or not they excrete polymers. Capsular Klebsiella aerogenes strains showed minimal intracellular uptake but over a 5-100 mg dm-3 Cd range produced the highest net metal removal levels due to significant extracellular adsorption.

Arthrobacter↗

PubMed1992

The structural genes encoding CO dehydrogenase subunits (cox L, M and S) in Pseudomonas carboxydovorans OM5 reside on plasmid pHCG3 and are, with the exception of Streptomyces thermoautotrophicus, conserved in carboxydotrophic bacteria.

Employing deoxyoligonucleotide probes and Southern hybridizations, we have examined in carboxydotrophic bacteria the localization on the genome of genes encoding the large, medium and small subunits of CO dehydrogenase (coxL, M and S, respectively). In Pseudomonas carboxydovorans OM5 coxL, M and S were identified on the plasmid pHCG3; they were absent on the chromosome. This was evident from positive hybridizations with plasmid DNA of the wild-type strain OM5 and the absence of hybridizations with chromosomal DNA from the plasmid cured mutant strain OM5-12. The genes coxL, M and S were found on plasmids in all other plasmid-containing carboxydotrophic bacteria e.g. Alcaligenes carboxydus, Azomonas B1, Pseudomonas carboxydoflava, Pseudomonas carboxydovorans OM2 and OM4. Cox L, M and S could be identified on the chromosome of the plasmid-free bacteria Arthrobacter 11/x, Bacillus schlegelii, Pseudomonas carboxydohydrogena, and Pseudomonas carboxydovorans OM3. These results essentially confirm and extend former reports that cox genes are rather conserved among carboxydotrophic bacteria of distinct taxonomic position. However, Streptomyces thermoautotrophicus is an noteworthy exception since none of the three cox genes could be detected. This refers to a new type of CO dehydrogenase and is in accord with results indicating that the S. thermoautotrophicus CO dehydrogenase has an unusual electron acceptor specificity and some other properties setting it apart from the 'classical' CO dehydrogenases.

Alcaligenes↗

PubMed1987

Degradation 1,2-dimethylbenzene by Corynebacterium strain C125.

In an attempt to obtain bacteria growing on 1,2-dimethylbenzene as sole carbon and energy source two different strains were isolated. One was identified as an Arthrobacter strain, the other as a Corynebacterium strain. Corynebacterium strain C125 was further investigated. The organism was not capable to grow on 1,3- and 1,4-dimethylbenzene. cis-1,2-Dihydroxycyclohexa-3,5-diene oxidoreductase and 3,4-dimethylcatechol-2,3-dioxygenase activity was found in cell extracts. When 3,4-dimethylcatechol was added to cell extract of 1,2-dimethylbenzene-grown cells, first a compound with the spectral properties of 2-hydroxy-5-methyl-6-oxo-2,4-heptadienoate was formed and subsequently acetate was produced. It is proposed that dioxygenases are involved in the initial steps of 1,2-dimethylbenzene degradation, and ring opening proceeds via meta-cleavage.

Arthrobacter↗

PubMed1980

Microbial growth on 2-bromobutane.

A member of the genus Arthrobacter was isolated which grew at the expense of 2-bromobutane as sole source of carbon and energy. Evidence is presented which suggests that the initial conversion of 2-bromobutane to 2-butanol is a spontaneous chemical hydrolysis and not mediated by the organism. Further evidence from oxygen consumption experiments indicates that 2-bromobutane is oxidized through 2-butanol, methyl ethyl ketone, ethyl acetate to acetate and ethanol. Results of experiments with cells grown on pathway intermediates reveal that the enzymes necessary for the oxidation of 2-butanol, methyl ethyl ketone, ethyl acetate, ethanol and acetaldehyde are not coordinately, but individually induced by their respective substrates.

Arthrobacter↗

PubMed1988

Characterization of 15 selected coccal bacteria isolated from Antarctic rock and soil samples from the McMurdo-Dry Valleys (South-Victoria Land).

Approximately 1500 cultures of microorganisms were isolated from rocks and soils of the Ross Desert (McMurdo-Dry Valleys). From these, 15 coccoid strains were chosen for more detailed investigation. They were characterized by morphological, physiological and chemotaxonomical properties. All isolates were Gram-positive, catalase-positive and nonmotile. Six strains showed red pigmentation and could be identified as members of the genera Micrococcus (M. roseus, M. agilis) or Deinococcus. In spite of their coccoid morphology, the remaining nine strains had to be associated with coryneform bacteria (Arthrobacter, Brevibacterium), because of their cell wall composition and G+C ratios. Most of the strains were psychrotrophic, but one strain was even obligately psychrophilic, with a temperature maximum below 20 degrees C. Red cocci had in vitro pH optima above 9.0 although they generally originated from acid samples. Most isolates showed a preference for sugar alcohols and organic acids, compounds which are commonly known to be released by lichens, molds and algae, the other components of the cryptoendolithic ecosystem. These properties indicate that our strains are autochthonous members of the natural Antarctic microbial population.

Antarctic Regions↗

PubMed1978

[Peptidoglycan type and cell wall polysaccharide composition of Cellulomonas cartalyticum and some coryneform organisms (author's transl)].

Cellulomonas cartalyticum was found to contain a peptidoglycan type different from that of the other species of Cellulomonas. The diamino acid is lysin instead of ornithine and the interpeptide bridge consists of D-Asp-D-Ser. The same peptidoglycan type occurs in Corynebacterium manihot, Brevibacterium liticum and Arthrobacter luteus. These non cellulolytic organisms are most likely not closely related with Cellulomonas cartalyticum, as indicated by the very different G +C content of their DNA, although they formed a narrow cluster including C. cartalyticum when numeric taxonomical methods were applied.

Actinomycetales↗

PubMed1996

Characterization of novel mono-O-acetylated GM3s containing 9-O-acetyl sialic acid and 6-O-acetyl galactose in equine erythrocytes.

Novel mono-O-acetylated GM3s, one containing 9-O-acetyl N-glycolyl neuraminic acid and another containing 6'-O-acetyl galactose, were isolated as a mixture from equine erythrocytes, and the structures were characterized by one- and two-dimensional proton nuclear magnetic resonance (NMR) and fast atom bombardment-mass spectrometry (FAB-MS). The position of the O-acetyl residue was identified by the downfield shift of the methylene protons at C-9 of N-glycolyl neuraminic acid (9-O-Ac GM3) and C-6 of galactose (6'-O-Ac GM3) in the NMR spectrum, in comparison to the respective non-acetylated counterparts. To confirm the presence of 6'-O-Ac GM3, the O-acetylated GM3 mixture was desialylated with Arthrobacter neuraminidase, giving 6-O-acetyl galactosyl glucosylceramide, the structure of which was estimated by NMR and FAB-MS, together with non-acetylated lactosylceramide with a ratio of 1:1.

Acetylation↗

PubMed1995

Formation of polyhydroxylated isoflavones from the soybean seed isoflavones daidzein and glycitein by bacteria isolated from tempe.

Five tempe-derived bacterial strains identified as Micrococcus or Arthrobacter species were shown to transform the soybean isoflavones daidzein and glycitein to polyhydroxylated isoflavones by different hydroxylation reactions. All strains converted glycitein and daidzein to 6,7,4'-trihydroxyisoflavone (factor 2) and the latter substrate also to 7,8,4'-trihydroxyisoflavone. Three strains transformed daidzein to 7,8,3',4'-tetrahydroxyisoflavone and 6,7,3',4'-tetrahydroxyisoflavone. In addition, two strains formed 6,7,8,4'-tetrahydroxyisoflavone from daidzein. Conversion of glycitein by these two strains led to the formation of factor 2 and 6,7,3',4'-tetrahydroxyisoflavone. The structures of these transformation products were elucidated by spectroscopic techniques and chemical degradation.

Arthrobacter↗

PubMed1984

Factors limiting the microbial conversion of sterols to 17-ketosteroids in the presence of metal chelate inhibitors.

Bioconversion of sterols to 17-ketosteroids by an Arthrobacter species occurred in the presence of hydrophobic metal-chelating agents but the production of 17-ketosteroids (17-KS) was seriously limited by the rapid loss of the viability of cells in the presence of these inhibitors. Besides, the conversion was inhibited by 17-KS at concentrations of 500 ppm or more. The 17-KS formed consisted exclusively of 1,4-androstadiene-3,17-dione (ADD) and 4-androstene-3,17-dione (AD) and these were found in the extracellular medium predominantly in bound form or as molecular aggregates which may limit their accumulation. It was concluded that enhanced production of 17-KS could be achieved by protecting the viability of cells and by removing the steroid metabolites from the site of inhibition.

17-Ketosteroids↗

PubMed1987

Microbiological and chemical dehydrogenation of withaferin A.

Arthrobacter simplex dehydrogenated withaferin A to 4-dehydrowithaferin A but it was not able to dehydrogenate this substrate in position 27. 27-Dehydrowithaferin A was prepared chemically using pyridinium chlorochromate. Whereas 4-dehydrowithaferin A surpassed in its effect on leukemic (388 cells the original compound and all its derivates synthesized so far, 27-dehydrowithaferin A was biologically inactive.

Animals↗