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PubMed1962

Synthesis of cellulose from pyruvate by succinate-grown cells of Acetobacter xylinum.

Benziman, Moshe (The Hebrew University of Jerusalem, Jerusalem, Israel) and H. Burger-Rachamimov. Synthesis of cellulose from pyruvate by succinate-grown cells of Acetobacter xylinum. J. Bacteriol. 84:625-630. 1962.-Pyruvate was converted into cellulose by succinate-grown cells of Acetobacter xylinum. With pyruvate-1-, 2-, or 3-C(14) as substrate, the upper half of the cellulose monomer mirrored the lower half, both as to total content and distribution of C(14). In each case, about 75% of the total radioactivity of the cellulose monomer was found in two carbon atoms (carbon pairs 3:4, 2:5, and 1:6, derived from pyruvate-1-, 2-, and 3-C(14), respectively). The carbonyl carbon of pyruvate contributed 2 equivalents to the cellulose monomer, compared with 1.4 and 2.8 equivalents contributed by the pyruvate carboxyl and methyl carbons, respectively. Cellulose formed in the presence of pyruvate and C(14)O(2) was nonradioactive. The results suggest that the carbon chain of the cellulose monomer is formed in these cells via a condensation involving two molecules of a three-carbon compound. Reactions involving pyruvate which could account for the observed distribution of C(14) in cellulose are discussed.

Acetobacter↗
PubMed1963

PATTERNS OF OXIDATIVE ASSIMILATION IN STRAINS OF ACETOBACTER AND AZOTOBACTER.

Tomlinson, Geraldine A. (The University of British Columbia, Vancouver, B.C., Canada), and J. J. R. Campbell. Patterns of oxidative assimilation in strains of Acetobacter and Azotobacter. J. Bacteriol. 86:1165-1172. 1963.-Oxidative assimilation of glucose-U-C(14) was studied with washed-cell suspensions of Acetobacter aceti, A. xylinum, Azotobacter vinelandii, and A. agilis. The suggestion that oxidative assimilation is largely the incorporation of endogenously produced ammonia is tenable. A. aceti did not exhibit oxidative assimilation and it did not incorporate ammonia in the presence of glucose, alpha-ketoglutarate, or pyruvate. A. xylinum, A. vinelandii, and A. agilis incorporated C(14) into the nitrogenous fractions of the cell. The level of assimilation into A. xylinum was low due to the accumulation of extracellular cellulose, and the level of assimilation into the Azotobacter was low presumably because of the requirement of energy for nitrogen fixation. The Azotobacter were characterized by the presence of a high level of radioactivity in the cold trichloroacetic acid-soluble pool. None of the organisms accumulated compounds in the supernatant fluid that might be considered pacemakers in glucose oxidation, and this could be a contributing factor in the low level of assimilation.

Acetobacter↗
PubMed1964

METABOLISM OF DICARBOXYLIC ACIDS IN ACETOBACTER XYLINUM.

Benziman, Moshe (The Hebrew University of Jerusalem, Jerusalem, Israel), and A. Abeliovitz. Metabolism of dicarboxylic acids in Acetobacter xylinum. J. Bacteriol. 87:270-277. 1964.-During the oxidation of fumarate or l-malate by whole cells or extracts of Acetobacter xylinum grown on succinate, a keto acid accumulated in the medium in considerable amounts. This acid was identified as oxaloacetic acid (OAA). No accumulation of OAA was observed when succinate served as substrate. These phenomena could be explained by the kinetics of malate, succinate, and OAA oxidation. OAA did not inhibit malate oxidation, even when present at high concentrations. When cells were incubated with OAA or fumarate in the presence of C(14)O(2), only the beta-carboxyl of residual OAA was found to be labeled. Evidence was obtained indicating that nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP) are not directly involved in malate oxidation by cell-free extracts. The results suggest that malate oxidation in A. xylinum is irreversible, and is catalyzed by an enzyme which is not NAD- or NADP-linked.

Acetates↗
PubMed1964

VALINE-ISOLEUCINE METABOLISM IN ACETOBACTER SUBOXYDANS AND THE INHIBITION OF GROWTH BY VALINE.

Kerwar, Suresh S. (Oregon State University, Corvallis), Vernon, H. Cheldelin, and L. W. Parks. Valine-isoleucine metabolism in Acetobacter suboxydans and the inhibition of growth by valine. J. Bacteriol. 88:179-186. 1964.-Extracts of Acetobacter suboxydans can synthesize valine and isoleucine via acetolactate and acetohydroxybutyrate, respectively. The amounts of these amino acids synthesized from different intermediates were determined. The pathways appear to be identical to those described for yeast, Neurospora, and Escherichia coli. When exogenous valine was added to a synthetic growth medium inoculated with A. suboxydans, no growth of the culture was observed. The inhibitory effect of valine was reversed by the addition of isoleucine. The site and mechanism of valine inhibition were investigated. Threonine deaminase was inhibited by valine and isoleucine but not by leucine. Repression of the deaminase by isoleucine but not by valine was indicated. The data reported in this paper suggest that valine prevented growth of the organism through false feedback inhibition of threonine deaminase, thereby limiting isoleucine biosynthesis.

Acetobacter↗
PubMed1964

FLAVINE ADENINE DINUCLEOTIDE-LINKED MALIC DEHYDROGENASE FROM ACETOBACTER XYLINUM.

Benziman, Moshe (The Hebrew University of Jerusalem, Jerusalem, Israel), and Y. Galanter. Flavine adenine dinucleotide-linked malic dehydrogenase from Acetobacter xylinum. J. Bacteriol. 88:1010-1018. 1964.-The properties of the pyridine nucleotide-nonlinked malic dehydrogenase of Acetobacter xylinum were investigated in the supernatant fluid obtained by high-speed centrifugation of sonic extracts. Ferricyanide, phenazine methosulfate, and to a lesser extent dichlorophenolindophenol were active as oxidants for malate oxidation. After acid ammonium sulfate precipitation, the enzyme lost its malate-oxidizing activity. The enzyme was reactivated by low concentrations of flavine adenine dinucleotide (FAD) but not by flavine mononucleotide (FMN) or riboflavine. Atabrine inhibited the enzyme, and the inhibition was relieved by FAD but not by FMN or riboflavine. Malate-oxidizing activity was inhibited by hematin. The inhibition was prevented by imidazole or globin. o-Phenanthroline, 8-hydroxy quinoline, alpha,alpha'-dipyridyl, and p-chloromercuribenzoate inhibited malate oxidation. Amytal markedly inhibited oxidation of malate in the presence of oxygen, phenazine methosulfate, or dichlorophenolindophenol, but not in the presence of ferricyanide. The results suggest that the malic dehydrogenase of A. xylinum is a FAD enzyme, which contains an ironbinding site essential for its activity. Nonheme iron and sulfhydro groups are possibly involved in enzyme activity. The malic dehydrogenase is functionally linked to the cytochrome chain.

Acetobacter↗
PubMed1964

OXALOACETATE DECARBOXYLATION AND OXALOACETATE-CARBON DIOXIDE EXCHANGE IN ACETOBACTER XYLINUM.

Benziman, Moshe (The Hebrew University of Jerusalem, Jerusalem, Israel), and N. Heller. Oxaloacetate decarboxylation and oxaloacetate-carbon dioxide exchange in Acetobacter xylinum. J. Bacteriol. 88:1678-1687. 1964.-Extracts of Acetobacter xylinum, prepared by sonic treatment, were shown to catalyze the decarboxylation of oxaloacetate (OAA) to pyruvate and CO(2), and the exchange of C(14)-carbon dioxide into the beta-carboxyl of OAA. Fractionation of the extracts with ammonium sulfate resulted in a 10-fold increase of the specific activity of the enzyme system catalyzing the CO(2) exchange and OAA decarboxylation reactions. The purified preparation catalyzed the exchange of pyruvate-3-C(14) into OAA. Similar pH curves with a pH optimum of 5.6 were obtained for the CO(2) exchange and OAA decarboxylation reactions. Both reactions require the presence of Mn(2+) or Mg(2+) ions. OAA decarboxylation was more strongly inhibited than the exchange of CO(2) by dialysis or metal-chelating agents. Avidin did not inhibit either reaction. Adenosine triphosphate (ATP), adenosine diphosphate (ADP), guanosine triphosphate (GTP), guanosine diphosphate (GDP), pyrophosphate, or inorganic phosphate did not promote OAA decarboxylation and the CO(2)-exchange reaction catalyzed by the purified preparation. The purified preparation failed to catalyze the carboxylation of phosphoenolpyruvate in the presence of GDP, ADP, or inorganic phosphate, and that of pyruvate in the presence of ATP or GTP, even when supplemented with an OAA-trapping system. A scheme for OAA decarboxylation which could account for the observed exchange reactions and for the failure to obtain net fixation of CO(2) is proposed. The relation between the exchange reaction and the synthesis of cellulose from pyruvate by A. xylinum is discussed.

Acetates↗
PubMed1990

Mutagenesis of acetobacter methanolicus MB58 with the transposon Tn5.

Transposon mutagenesis was applied to the isolation of mutants of the facultatively methylotrophic Acetobacter methanolicus MB 58. The transposon Tn5 (pSU2011) was transferred from Escherichia coli SM 10 by means of conjugation to Acetobacter methanolicus MB 58. Four out of 1850 stable Km-resistant transconjugants were identified that were formaldehyde sensitive and failed to grow on methanol.

Acetobacter↗
PubMedDate not supplied

Genetic organization of Acetobacter for acetic acid fermentation.

Plasmid vectors for the acetic acid-producing strains of Acetobacter and Gluconobacter were constructed from their cryptic plasmids and the efficient transformation conditions were established. The systems allowed to reveal the genetic background of the strains used in the acetic acid fermentation. Genes encoding indispensable components in the acetic acid fermentation, such as alcohol dehydrogenase, aldehyde dehydrogenase and terminal oxidase, were cloned and characterized. Spontaneous mutations at high frequencies in the acetic acid bacteria to cause the deficiency in ethanol oxidation were analyzed. A new insertion sequence element, IS1380, was identified as a major factor of the genetic instability, which causes insertional inactivation of the gene encoding cytochrome c, an essential component of the functional alcohol dehydrogenase complex. Several genes including the citrate synthase gene of A. aceti were identified to confer acetic acid resistance, and the histidinolphosphate aminotransferase gene was cloned as a multicopy suppressor of an ethanol sensitive mutant. Improvement of the acetic acid productivity of an A. aceti strain was achieved through amplification of the aldehyde dehydrogenase gene with a multicopy vector. In addition, spheroplast fusion of the Acetobacter strains was developed and applied to improve their properties.

Acetates↗
PubMed2003

Characterisation of plasmids purified from Acetobacter pasteurianus 2374.

Four cryptic plasmids pAP1, pAP2, pAP3, and pAP4 with their replication regions AP were isolated from Gram-negative bacteria Acetobacter pasteurianus 2374 and characterised by sequence analyses. All plasmids were carrying the kanamycin resistance gene. Three of four plasmids pAP2, pAP3, and pAP4 encode an enzyme that confers ampicillin resistance to host cells. Moreover, the tetracycline resistance gene was identified only in pAP2 plasmid. All plasmids are capable to coexist with each other in Acetobacter cells. On the other hand, the coexistence of more than one plasmid is excluded in Escherichia coli. The nucleotide sequence of replication regions showed significant homology. The nucleotide and protein sequence analyses of resistance genes of all plasmids were compared with transposons Tn3, Tn10, and Tn903 which revealed significant differences in the primary structure, however no functional changes of gene were obtained.

Acetobacter↗
PubMed2005

Analysis of replication region of the cryptic plasmid pAG20 from Acetobacter aceti 3620.

The DNA sequence of small cryptic plasmid pAG20 in Acetobacter aceti was determined at 3064 bp with 51.6% GC pairs. The plasmid encoded a 186 amino acid protein which is important for plasmid replication in Gram-negative bacteria except Escherichia coli. Two 21 bp large direct repeat sequence 1 and two 13 bp direct repeat sequence 2 were determined in the regulation region upstream from gene encoded Rep protein. Vector pAG24 with kanamycin gene and two deletion derivatives pAG25 and pAG26 without rep gene from plasmid pAG20 were constructed. Plasmid pAG24 was replicated in a broad host range like E. coli, Acetobacter pasteurianus, A. aceti, Comanomonas spp., Serratia marcescens, and Shigella spp.

Acetobacter↗
PubMed2004

Enhanced expression of aconitase raises acetic acid resistance in Acetobacter aceti.

Acetobacter spp. are used for industrial vinegar production because of their high ability to oxidize ethanol to acetic acid and high resistance to acetic acid. Two-dimensional gel electrophoretic analysis of a soluble fraction of Acetobacter aceti revealed the presence of several proteins whose production was enhanced, to various extents, in response to acetic acid in the medium. A protein with an apparent molecular mass of 100 kDa was significantly enhanced in amount by acetic acid and identified to be aconitase by NH2-terminal amino acid sequencing and subsequent gene cloning. Amplification of the aconitase gene by use of a multicopy plasmid in A. aceti enhanced the enzymatic activity and acetic acid resistance. These results showed that aconitase is concerned with acetic acid resistance. Enhancement of the aconitase activity turned out to be practically useful for acetic acid fermentation, because the A. aceti transformant harboring multiple copies of the aconitase gene produced a higher concentration of acetic acid with a reduced growth lag-time.

Acetic Acid↗
PubMed2005

Natural association of Gluconacetobacter diazotrophicus and diazotrophic Acetobacter peroxydans with wetland rice.

The family Acetobacteraceae currently includes three known nitrogen-fixing species, Gluconacetobacter diazotrophicus, G. johannae and G. azotocaptans. In the present study, acetic acid-producing nitrogen-fixing bacteria were isolated from four different wetland rice varieties cultivated in the state of Tamilnadu, India. Most of these isolates were identified as G. diazotrophicus on the basis of their phenotypic characteristics and PCR assays using specific primers for that species. Based on 16S rDNA partial sequence analysis and DNA: DNA reassociation experiments the remaining isolates were identified as Acetobacter peroxydans, another species of the Acetobacteraceae family, thus far never reported as diazotrophic. The presence of nifH genes in A. peroxydans was confirmed by PCR amplification with nifH specific primers. Scope for the findings: This is the first report of the occurrence and association of N2-fixing Gluconacetobacter diazotrophicus and Acetobacter peroxydans with wetland rice varieties. This is the first report of diazotrophic nature of A. peroxydans.

Acetobacter↗
PubMed2001

Structure of Acetobacter cellulose composites in the hydrated state.

The structure of composites produced by the bacterium Acetobacter xylinus have been studied in their natural, hydrated, state. Small-angle X-ray diffraction and environmental scanning electron microscopy has shown that the ribbons have a width of 500 A and contain smaller semi-crystalline cellulose microfibrils with an essentially rectangular cross-section of approximately 10 x 160 A(2). Incubation of Acetobacter in xyloglucan or pectin results in no changes in the size of either the microfibrils or the ribbons. Changes in the cellulose crystals are seen upon dehydration of the material, resulting in either a reduction in crystal size or an increase in crystal disorder.

Acetobacter↗
PubMed2001

Optimization of fermentation conditions for the production of bacterial cellulose by a newly isolated Acetobacter sp. A9 in shaking cultures.

The optimum fermentation conditions for the production of cellulose by a newly isolated Acetobacter sp. A9 were determined by shaken cultures. The strain was able to produce cellulose at 25-30 degrees C with a maximum at 30 degrees C. Cellulose production occurred at pH 4.5-7.5 with a maximum at pH 6.5. The improved medium composition was 4% (w/v) glucose, 0.1% (w/v) yeast extract, 0.7% (w/v) polypeptone and 0.8% (w/v) Na(2)HPO(4).12H(2)O. Under these culture conditions, 3.8 g/l cellulose was produced after 7 days of cultivation, although this strain produced only 2.2 g/l in the standard medium. The addition of ethanol to the improved medium enhanced cellulose production: in an improved medium containing 1.4% (v/v) ethanol, cellulose production was 15.2 g/l, which was about four times higher than that without ethanol. Addition of ethanol was found to eliminate the spontaneous mutation of Acetobacter sp. A9.

Acetobacter↗
PubMed1990

Cytochrome a1 of acetobacter aceti is a cytochrome ba functioning as ubiquinol oxidase.

Cytochrome a1 is a classic cytochrome that in the 1930s had already been detected in Acetobacter strains and in the 1950s was identified as a terminal oxidase. However, recent studies did not substantiate the previous observations. We have detected a cytochrome a1-like chromophore in Acetobacter aceti, which was purified and characterized in this study. The cytochrome was solubilized from membranes of the strain with octyl beta-D-glucopyranoside and was purified by single column chromatography. The purified cytochrome exhibited a broad alpha peak around 600-610 nm, which turned to a sharp peak at 589 nm in the presence of cyanide. Carbon monoxide difference spectra of the cytochrome indicated the presence of an alpha-type cytochrome. The cytochrome contained 1 mol each of hemes b and a and probably one copper ion. These results suggest that the cytochrome purified from A. aceti is the so-called cytochrome a1, and thus the existence of the classic cytochrome has been reconfirmed. The purified enzyme consisted of four polypeptides of 55, 35, 22, and 18 kDa, and it showed a sedimentation coefficient of 6.3 S in the native form. The enzyme had a high ubiquinol oxidase activity (140-160 mumol of ubiquinol-2 oxidized per min per mg of protein). When reconstituted into proteoliposomes, the cytochrome could generate an electrochemical proton gradient during oxidation of ubiquinol. Thus, cytochrome a1 of A. aceti has been shown to be a cytochrome ba terminal oxidase capable of generating an electrochemical proton gradient concomitant with ubiquinol oxidation.

Acetobacter↗
PubMed1997

A new insertion sequence IS1452 from Acetobacter pasteurianus.

A new insertion sequence element, IS1452, was found to be associated with inactivation of the alcohol dehydrogenase by insertion in the adhS gene encoding subunit III of the three-component membrane-bound alcohol dehydrogenase complex in Acetobacter pasteurianus. Cloning and sequencing analyses of the mutated subunit III gene locus revealed that IS1452 was inserted at or near the ribosome-binding sequence of adhS. Analysis of transcription using the chloramphenicol acetyltransferase gene as the reporter indicated that IS1452 abolished transcription of adhS by separating its promoter from the subunit III structural gene. IS1452 was 1411 bp in length and had a terminal inverted repeat of 21 bp. IS1452 contained one long ORF of 416 amino acids rich in basic amino acids. This protein showed homology with a putative transposes, Tra1, of IS701 isolated from the cyanobacterium Calothrix species PCC 7601. Like IS701, IS1452 was found to generate a 4 bp direct repeat at the site of insertion upon transposition. The target site specificity was rather strict, and a CTA(A or G) sequence appeared to be preferentially recognized. Transposition of IS1452 was replicative, since it was accompanied by an increase in the copy number of IS1452. Several strains belonging to the genus Acetobacter also contained IS1452 at varying copy numbers from one to more than ten. These observations suggest that IS1452 is one of the insertion sequences that are responsible for genetic instability leading to deficiencies in various physiological properties in acetic acid bacteria.

Acetobacter↗
PubMed1994

Structure elucidation and biosynthesis of 31-methylhopanoids from Acetobacter europaeus. Studies on a new series of bacterial triterpenoids.

Apart from a mixture of bacteriohopanetetrols already found in other Acetobacter species, four new 3 beta-methylhopanoids have been isolated from Acetobacter europaeus. All of them present an ether linkage between a bacteriohopanetetrol or a bacteriohopanepentol and a carbapseudopentose moiety often found in bacterial hopanoids. Three of these ethers were shown by comparison with synthetic reference hopanoids to posess a supplementary methyl group at C31. This novel series of methylhopanoids may be the precursor of yet unidentified molecular fossils found in sediments. [methyl-2H3]Methionine was efficiently incorporated into the 31-methylhopanoids with retention of all three deuterium atoms in the transferred methyl group. This labelling pattern might be consistent with a rather rarely found methylation reaction of an enol.

Acetobacter↗
PubMed1995

Phylogenetic position of Gluconobacter species as a coherent cluster separated from all Acetobacter species on the basis of 16S ribosomal RNA sequences.

The 16S rRNA sequences from the Gluconobacter species G. asaii, G. cerinus and G. frateurii were determined and compared with homologous sequences from published databases and sequences of G. oxydans and Acetobacter species previously described [Sievers, M., Ludwig, W. and Teuber, M. (1994) System. Appl. Microbiol. 17, 189-196]. The Gluconobacter species have unique 16S rRNA sequences and exhibit sequence similarity values of 97.4 to 99.1%, corresponding to 36 to 14 base differences. The phylogenetic tree inferring methods (distance matrix, maximum parsimony and maximum likelihood) show that the species of Gluconobacter form a coherent, closely related cluster. Based on the distance matrix method including Rhodopila globiformis as an outgroup reference organism, Gluconobacter is well separated from Acetobacter.

Acetobacter↗