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PubMed2002

Isolation and characterization of the glnD gene of Gluconacetobacter diazotrophicus, encoding a putative uridylyltransferase/uridylyl-removing enzyme.

The glnD gene of Gluconacetobacter diazotrophicus was isolated by complementation of the Azotobacter vinelandii glnD (nfrX) mutant strain MV17 using a pLAFR3 cosmid library. The 5 kb chromosomal DNA region encoding the glnD gene on cosmid pAD401 was identified by introduction of deletions as well as subcloning of restriction fragments followed by subsequent DNA sequencing. Three open reading frames were identified with the deduced amino acid sequence of ORF1 showing significant homologies to known GlnD proteins of other proteobacteria such as Sinorhizobium meliloti, Rhizobium tropici, Escherichia coli and Azotobacter vinelandii.A mutagenesis of the chromosomal glnD gene was carried out by insertion of an interposon carrying the kanamycin resistance gene of Tn5. Mutants carrying the cassette inserted into a central region of glnD could not be isolated, while an interposon mutation at the 3' end of glnD was successful. The resulting strain showed a prolonged generation time in complex growth medium and was unable to utilize ammonium as sole nitrogen source. This phenotype appears to be pleiotropic, since the addition of single amino acids to the minimal medium was not sufficient to allow growth. Furthermore, the glnD mutant was able to express nitrogenase under diazotrophic as well as repressing growth conditions.

Acetobacteraceae↗
PubMedDate not supplied

Gluconacetobacter diazotrophicus, a sugar cane endosymbiont, produces a bacteriocin against Xanthomonas albilineans, a sugar cane pathogen.

Gluconacetobacter diazotrophicus in liquid culture secretes proteins into the medium. Both medium containing Gluconacetobacter protein and a solution of this protein after acetone precipitation appeared to inhibit the growth of Xanthomonas albilineans in solid culture. This apparent inhibition of bacterial growth has, in fact, been revealed to be lysis of bacterial cells, as demonstrated by transmission electron microscopy. Fractionation of the Gluconacetobacter protein mixture in size-exclusion chromatography reveals a main fraction with lysozyme-like activity which produces lysis of both living bacteria and isolated cell walls.

Acetobacteraceae↗
PubMed1998

Detection of ethanol in a two-component glucose/ethanol mixture using a nonselective microbial sensor and a glucose enzyme electrode.

Chemometric theory was applied to a microbial sensor for determinations of ethanol in the presence of glucose. Microbial sensors, consisting of Gluconobacter oxydans cells immobilized on Clark-type amperometric oxygen electrodes, exhibited good sensitivity but low selectivity toward ethanol and glucose. An Eksan-G commercial glucose analyzer was used as a second sensor for multivariate calibration and analyses. Microbial sensors exhibited nearly complete additivity for total glucose plus ethanol concentrations from 0.0 to 0.6 mM. Within this linear range, chemometric analyses provided estimates of ethanol concentration with measurement errors of less than 8%. Multivariate calibration thus is a promising approach to enhance the usefulness of microbial sensors.

Acetobacteraceae↗
PubMed1998

Effects of high oxygen concentrations on microbial biosensor signals. Hyperoxygenation by means of perfluorodecalin.

Amperometric biosensors register oxygen depletion in response to analyte catabolism, and thus are limited by the availability of dissolved oxygen. Microbial sensors containing immobilized cells of Gluconobacter oxydans were hyperoxygenated to 400% of control levels and the effects on sensor responses to glucose were determined. Oxygenated perfluorodecalin (a completely fluorinated organic substance) was as effective in hyperoxygenation as direct sparging with O2, increasing sensor base medium oxygen concentrations from 9.3 to 37 mg/l. Hyperoxygenation enhanced maximal biosensor response amplitudes, particularly at high cell loading densities. Maximal response rates were also improved, although less dramatically. Results suggest that hyperoxygenation may be a new general approach for modulating biosensor responses.

Acetobacteraceae↗
PubMed1999

Polypyrrole-entrapped quinohemoprotein alcohol dehydrogenase. Evidence for direct electron transfer via conducting-polymer chains.

It is reported for the first time that direct electron-transfer processes between a polypyrrole (PPY) entrapped quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33 (QH-ADH) and a platinum electrode take place via the conducting-polymer network. The cooperative action of the enzyme-integrated prosthetic groups--pyrroloquinoline-quinone and hemes--is assumed to allow this electron-transfer pathway from the enzyme's active site to the conducting-polymer backbone. A hypothetical model of the electron transfer is proposed which is supported by the influence of various parameters, such as, e.g., ionic strength and nature of the buffer salts. This unusual electron-transfer pathway leads to an accentuated increase of the K M app value (102 mM) and hence to a significantly increased linear detection range of an ethanol sensor based on this enzyme.

Acetobacteraceae↗
PubMed2000

Magnetic circular dichroism properties of reaction center complexes isolated from the zinc-bacteriochlorophyll a-containing purple bacterium Acidiphilium rubrum.

Reaction center (RC) complexes isolated from a Zn-bacteriochlorophyll (BChl) a-containing purple bacterium, Acidiphilium rubrum, were characterized by absorption, circular dichroism, and magnetic circular dichroism (MCD) spectroscopy. The oxidized-minus-reduced difference spectra indicated that, in this RC, the Zn-BChl a is the primary electron donor. The molecular structure of the donor was examined by measuring the ratio of the MCD intensity of the Faraday B-term (B) to the dipole strength (D). In the Q(y) region, B/D for the donor was about half those of bacteriopheophytin a and the accessory Zn-BChl a, indicating that the primary electron donor is a dimer. The magnitude of bleach of the Q(x) band was half that observed in Rhodobacter sphaeroides, suggesting the cation is localized on a single Zn-Bchl a. The absorption intensity of the higher-energy Q(y) exciton band was approximately 28% of that of the lower-energy band, and the exciton splitting was approximately 570 cm(-1), smaller than that in Rb. sphaeroides. These results indicate that, in A. rubrum, the primary electron donor is a Zn-BChl a dimer but that the interaction between the two molecules is rather weak. On the basis of these results, an adaptive strategy for changes in BChl a species is discussed from an evolutionary perspective.

Acetobacteraceae↗
PubMedDate not supplied

Acetate-specific stress response in acetate-resistant bacteria: an analysis of protein patterns.

Many metabolic byproducts have toxic effects on bacteria, and acetic acid is an excellent model for such molecules. The negative effects of acetate, which include decreased growth rates and specific productivities, appear for Escherichia coli at acetate concentrations lower than 5 g/L. Acetic acid bacteria, however, are naturally resistant to the detrimental effects of acetate in their surroundings; they remain active at acetate levels well over 40 g/L. This study investigated the response to acetate challenges by the naturally acetate-resistant bacteria Acetobacter aceti and Gluconobacter suboxydans to learn more about possible mechanisms of tolerance to otherwise toxic low molecular weight metabolites. Growth studies showed that the resistant bacteria grow more slowly in the presence of acetate but are not slowed nearly so much as is E. coli. In addition, two-dimensional gel electrophoresis (2DE) was applied to study the relative protein patterns of acetate-resistant bacteria during growth in the presence and absence of acetate. In each organism, growth in acetate-containing medium led to elevated levels of many stress response proteins. 2DE analysis of heat-shocked cultures was used to determine which were nonspecific. Elimination of those proteins that were also amplified following heat shock left only eight proteins, here designated acetate-specific stress proteins (Asps), which are overexpressed specifically in response to acetate. Three of these, AspA, AspB, and AspC, appear to be analogous in the two bacterial strains studied, based on their apparent pIs and molecular weights.

Acetates↗
PubMed2002

Influence of heterotrophic microbial growth on biological oxidation of pyrite.

The rate and extent of pyrite oxidation by the iron-oxidizing bacteria Acidithiobacillus ferrooxidans was limited by the growth of the heterotrophic microbe Acidiphilium acidophilum. In batch systems containing a mixture of both organisms, the maximum zero-order rate of ferric iron accumulation was about 1.4 mg of Fe3+ L(-1) d(-1) as compared to 9.4 mg of Fe3+ L(-1) d(-1) for pure cultures of A. ferrooxidans under the same conditions. Pyrite oxidation was limited in cases where both cultures of organisms were initially present as well as situations where the heterotrophic organisms were added to established, pyrite-oxidizing systems containing A. ferrooxidans. Results also indicated that organic carbon remaining in solution following heterotrophic bacterial growth reduced the rate of abiotic pyrite oxidation by the ferric ion. Furthermore, a cell-free solution of the residual organic carbon resulted in a lag of A. ferrooxidans growth in soluble ferrous medium. The residual organic carbon solution that accumulated during the growth of Aph. acidophilum had a diverse molecular weight distribution, indicating that different compounds could be responsible for the inhibition of chemical pyrite oxidation and the A. ferrooxidans growth lag observed. Titration of dissolved copper ions with residual dissolved organic carbon originating from Aph. acidophilum cultures indicated that a metal complexation mechanism could be responsible for the lower rates of pyrite oxidation observed. These data suggest that encouraging the growth of heterotrophic microorganisms under acid mine drainage conditions may be a feasible strategy for decreasing both the rate and the extent of sulfide mineral oxidation.

Acetobacteraceae↗
PubMed2000

Changes in major components of tea fungus metabolites during prolonged fermentation.

Changes in major components and microbes in tea fungus broth (or kombucha; teakwass) prepared from nine different sources during a prolonged fermentation of up to 60 days were investigated. Cell concentrations of both yeasts and acetic acid bacteria in broth were generally higher than those in the cellulosic pellicles. The residual sucrose concentration decreased linearly with time, although the rate fell after the first month. Metabolic fates of glucose and fructose produced as a result of the hydrolysis of sucrose were different. Glucose was not produced in parallel with fructose (0.085 g 100 ml(-1) d(-1)) but was produced with a lower initial rate (0.041 g 100 ml(-1) d(-1)). Both titratable acidity and gluconic acid increased steadily with time for all samples, although gluconic acid was not generated for 6 days until the fermentation had begun. Acetic acid increased slowly to a maximum value of 1.1 g 100 ml(-1) after 30 days; thereafter, it decreased gradually. Gluconic acid contributed to the titratable acidity and thus, the taste of tea fungus broth, during the final stage of fermentation. It is concluded that the desired quality or composition of kombucha can be obtained through the proper control of fermentation time.

Acetic Acid↗
PubMed2002

Reduction of ferric iron by acidophilic heterotrophic bacteria: evidence for constitutive and inducible enzyme systems in Acidiphilium spp.

AIMS: To compare the abilities of two obligately acidophilic heterotrophic bacteria, Acidiphilium acidophilum and Acidiphilium SJH, to reduce ferric iron to ferrous when grown under different culture conditions. METHODS AND RESULTS: Bacteria were grown in batch culture, under different aeration status, and in the presence of either ferrous or ferric iron. The specific rates of ferric iron reduction by fermenter-grown Acidiphilium SJH were unaffected by dissolved oxygen (DO) concentrations, while iron reduction by A. acidophilum was highly dependent on DO concentrations in the growth media. The ionic form of iron present (ferrous or ferric) had a minimal effect on the abilities of harvested cells to reduce ferric iron. Whole cell protein profiles of Acidiphilium SJH were very similar, regardless of the DO status of the growth medium, while additional proteins were present in A. acidophilum grown microaerobically compared with aerobically-grown cells. CONCLUSIONS: The dissimilatory reduction of ferric iron is constitutive in Acidiphilium SJH while it is inducible in A. acidophilum. SIGNIFICANCE AND IMPACT OF THE STUDY: Ferric iron reduction by Acidiphilium spp. may occur in oxygen-containing as well as anoxic acidic environments. This will detract from the effectiveness of bioremediation systems where removal of iron from polluted waters is mediated via oxidation and precipitation of the metal.

Acetobacteraceae↗
PubMed1998

Molecular cloning and mutational analysis of the ddsA gene encoding decaprenyl diphosphate synthase from Gluconobacter suboxydans.

Decaprenyl diphosphate (decaprenyl-PP) synthase catalyzes the consecutive condensation of isopentenyl diphosphate with allylic diphosphates to produce decaprenyl-PP, which is used for the side chain of ubiquinone (Q)-10. We have cloned the synthase gene, designated ddsA, from Gluconobacter suboxydans and expressed it in Escherichia coli. Sequence analysis revealed the presence of an ORF of 948 bp capable of encoding a 33,898-Da polypeptide that displays high similarity (30-50%) to other prenyl diphosphate synthases. Expression of the ddsA gene complemented the lethality resulting from a defect in the octaprenyl diphosphate synthase gene of E. coli and produced Q-10, indicating that Q-10 can substitute for the function of Q-8. The His-tagged DdsA protein was purified to characterize its enzymatic properties. This enzyme required detergent (0.05% Triton X-100) and 10 mM Mg2+, for full activity. The Michaelis constants for geranyl diphosphate, all-E-farnesyl diphosphate and all-E-geranylgeranyl diphosphate were 7.00, 0.50 and 0.32 microM, respectively. Nine single-amino-acid substitutions were introduced upstream of conserved region II or VI. Most of the mutants showed a considerable decrease in catalytic activity or shortening of the ultimate chain length. However, the A70G mutant produced a longer-chain-length product than wild-type decaprenyl-PP synthase, and the A70Y mutant completely abolished the decaprenyl-PP synthase function, indicating that Ala70 is important for enzyme activity and the determination of the chain-length properties of DdsA.

Acetobacteraceae↗
PubMed2002

Microbial reduction of Fe(III) in the presence of oxygen under low pH conditions.

In acidic, coal mining lake sediments, facultatively anaerobic Acidiphilium species are probably involved in the reduction of Fe(III). Previous results indicate that these bacteria can co-respire O2 and Fe(III). In this study, we investigated the capacity of the sediment microbiota to reduce Fe(III) in the presence of O2 at pH 3. In sediment microcosms with 4% O2 in the headspace, the concentration of Fe(II) increased at a rate of 1.03 micromol (g wet sediment)-1 day-1 within the first 7 days of incubation which was similar to the rate obtained with controls incubated under anoxic conditions. However, in microcosms incubated under air, Fe(II) was consumed after a lag phase of 8 h with a rate of 2.66 micromol (g wet sediment)-1 day-1. Acidiphilium cryptum JF-5, isolated from this sediment, reduced soluble Fe(III) with either 4 or 21% O2 in the headspace, and concomitantly consumed O2. However, the rate of Fe(II) formation normalized for cell density decreased under oxic conditions. Schwertmannite, the predominant Fe(III)-mineral of this sediment, was also reduced by A. cryptum JF-5 under oxic conditions. The rate of Fe(II) formation by A. cryptum JF-5 decreased after transfer from preincubation under air in medium lacking Fe(III). Acidiphilium cryptum JF-5 did not form Fe(II) when preincubated under air and transferred to anoxic medium containing Fe(III) and chloramphenicol, an inhibitor of protein synthesis. These results indicate that: (i) the reduction of Fe(III) can occur at low O2 concentrations in acidic sediments; (ii) Fe(II) can be oxidized at O2 concentrations near saturation; and (iii) the enzyme(s) responsible for the reduction of Fe(III) in A. cryptum JF-5 are not constitutive.

Acetobacteraceae↗
PubMed2004

Asaia bogorensis peritonitis identified by 16S ribosomal RNA sequence analysis in a patient receiving peritoneal dialysis.

Here the authors report a case of refractory peritonitis leading to multiple hospitalizations and the loss of peritoneal dialysis access in a patient on automated peritoneal dialysis, caused by Asaia bogorensis, a bacterium not previously described as a human pathogen. This organism was identified by sequence analysis of the 16S ribosomal RNA gene. Unusual microbial agents may cause peritonitis, and molecular microbiological techniques are important tools for identifying these agents.

Acetobacteraceae↗
PubMed1996

Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans.

Alcohol dehydrogenase (ADH) of acetic acid bacteria functions as the primary dehydrogenase of the ethanol oxidase respiratory chain, where it donates electrons to ubiquinone. ADH is a membrane-bound quinohemoprotein-cytochrome c complex which consists of subunits I (78 kDa), II (48 kDa), and III (14 kDa) and contains several hemes c as well as pyrroloquinoline quinone as prosthetic groups. To understand the role of the heme c moieties in the intramolecular electron transport and the ubiquinone reduction, the ADH complex of Gluconobacter suboxydans was separated into a subunit I/III complex and subunit II, then reconstituted into the complex. The subunit I/III complex, probably subunit I, contained 1 mol each of pyrroloquinoline quinone and heme c and exhibited significant ferricyanide reductase, but no Q1 reductase activities. Subunit II was a triheme cytochrome c and had no enzyme activity, but it enabled the subunit I/III complex to reproduce the Q1 and ferricyanide reductase activities. Hybrid ADH consisting of the subunit I/III complex of G. suboxydans ADH and subunit II of Acetobacter aceti ADH was constructed and it had showed a significant Q1 reductase activity, indicating that subunit II has a ubiquinone-binding site. Inactive ADH from G. suboxydans exhibiting only 10% of the Q1 and ferricyanide reductase activities of the active enzyme has been isolated separately from active ADH (Matsushita, K., Yakushi, T., Takaki, Y., Toyama, H., and Adachi, O (1995) J. Bacteriol. 177, 6552-6559). Using these active and inactive ADHs and also isolated subunit I/III complex, we performed kinetic studies which suggested that ADH contains four ferricyanide-reacting sites, one of which was detected in subunit I and the others in subunit II. One of the three ferricyanide-reacting sites in subunit II was defective in inactive ADH. The ferricyanide-reacting site remained inactive even after alkali treatment of inactive ADH and also after reconstituting the ADH complex from the subunits, in contrast to the restoration of Q1 reductase activity and the other ferricyanide reductase activities. Thus, the data suggested that the heme c in subunit I and two of the three heme c moieties in subunit II are involved in the intramolecular electron transport of ADH into ubiquinone, where one of the two heme c sites may work at, or close to, the ubiquinone-reacting site and another between that and the heme c site in subunit I. The remaining heme c moiety in subunit II may have a function other than the electron transfer from ethanol to ubiquinone in ADH.

Acetobacter↗
PubMed1999

Magnesium insertion by magnesium chelatase in the biosynthesis of zinc bacteriochlorophyll a in an aerobic acidophilic bacterium Acidiphilium rubrum.

To elucidate the mechanism for formation of zinc-containing bacteriochlorophyll a in the photosynthetic bacterium Acidiphilium rubrum, we isolated homologs of magnesium chelatase subunits (bchI, -D, and -H). A. rubrum bchI and -H were encoded by single genes located on the clusters bchP-orf168-bchI-bchD-orf320-crtI and bchF-N-B-H-L as in Rhodobacter capsulatus, respectively. The deduced sequences of A. rubrum bchI, -D, and -H had overall identities of 59. 8, 40.5, and 50.7% to those from Rba. capsulatus, respectively. When these genes were introduced into bchI, bchD, and bchH mutants of Rba. capsulatus for functional complementation, all mutants were complemented with concomitant synthesis of bacteriochlorophyll a. Analyses of bacteriochlorophyll intermediates showed that A. rubrum cells accumulate magnesium protoporphyrin IX monomethyl ester without detectable accumulation of zinc protoporphyrin IX or its monomethyl ester. These results indicate that a single set of magnesium chelatase homologs in A. rubrum catalyzes the insertion of only Mg(2+) into protoporphyrin IX to yield magnesium protoporphyrin IX monomethyl ester. Consequently, it is most likely that zinc-containing bacteriochlorophyll a is formed by a substitution of Zn(2+) for Mg(2+) at a step in the bacteriochlorophyll biosynthesis after formation of magnesium protoporphyrin IX monomethyl ester.

Acetobacteraceae↗
PubMed2004

Rhodovarius lipocyclicus gen. nov. sp. nov., a new genus of the alpha-1 subclass of the Proteobacteria.

A bacterial strain (CCUG 44693T) was recovered during an industrial hygiene control. Phylogenetic analyses using the 16S rRNA gene sequence of the isolate indicated that it represents a new lineage in the alpha-1 subclass of the Proteobacteria, with the highest sequence similarity of 93.3% to the type strain of Muricoccus roseus. In the polyamine pattern spermidine was the predominant compound. The polar lipid profile consisted of the major lipids phosphatidyl ethanolamine, phosphatidyl dimethylethanolamine, phosphatidyl glycerol, phosphatidyl cholin and an unknown amino lipid. The major respiratory quinone was a ubiquinone Q-10 and the major whole cell fatty acids were 19:0 cyclo omega8c and 18:1 omega7c. The isolate also contained 18:1 2-OH and other fatty acids typical for members of the alpha-1 subclass of the Proteobacteria in addition to 10:0 2-OH in low amounts, not detected in members of closely related genera. The strain grew heterotrophically and strictly aerobically and formed red-colored colonies on tryptone soy agar. Bacteriochlorophyll a could not be detected by direct spectrophotometric analyses of aerobically grown cells. On the basis of the phylogenetic analyses, chemotaxonomic and biochemical characteristics, we propose that strain CCUG 44693T (CIP 108310T) represents a new genus of the alpha-1 subclass of the Proteobacteria for which we propose the name Rhodovarius lipocyclicus gen. nov. sp. nov.

Acetobacteraceae↗