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At least 19 recordsLinked to original sources
PubMed1999

Identification and characterization of 6-dehydroVB-A reductase from Streptomyces antibioticus.

Streptomyces antibioticus NF-18 is a hyperproducing strain of a Streptomyces hormone, virginiae butanolide A (VB-A), that induces virginiamycin production of S. virginiae at nanomolar concentrations. To characterize the biosynthetic pathway of VB-A, we identified and characterized for the first time the 6-dehydro VB-A reductase that is responsible for the final reduction step in the biosynthesis. Assay protocols and stabilization conditions were established. The 6-dehydro VB-A reductase was found to require NADPH, not NADH, as a coenzyme. The K(m) values of the enzyme for NADPH and (+/-)-6-dehydro VB-A were determined to be 50 +/- 2 microM and 100 +/- 5 microM, respectively. Ultracentrifugation experiments revealed that 6-dehydro VB-A reductase was present almost exclusively in the 100,000 x g supernatant fraction, indicating that the enzyme is a cytoplasmic-soluble protein. The M(r) of the native 6-dehydro VB-A reductase was estimated to be 82,000 +/- 3000 by molecular sieve HPLC. The optimal pH was found to be 6.7 +/- 0.2.

4-Butyrolactone↗
PubMed1991

Nutritional regulation of differentiation and synthesis of an exocytoplasmic deoxyriboendonuclease in Streptomyces antibioticus.

Streptomyces antibioticus produces a cell-wall-located deoxyriboendonuclease (DNAase) the synthesis of which in submerged and surface cultures is related to the growth rate. DNAase synthesis always preceded aerial mycelium formation in surface cultures. Production of aerial mycelium began at the end of exponential growth or in the early stationary phase; it was absent in cultures grown on nutrient agar/glucose or in media with a high concentration of casein hydrolysate. These nutritional conditions also impaired production of the DNAase. External DNA substrates were not degraded by mycelium producing the DNAase. These observations lead us to suggest a role for the enzyme in the developmental cycle of S. antibioticus.

Amino Acids↗
PubMed1986

Glycogen and trehalose accumulation during colony development in Streptomyces antibioticus.

Streptomyces antibioticus accumulated glycogen and trehalose in a characteristic way during growth on solid medium. Glycogen storage in the substrate mycelium took place during development of the aerial mycelium. The concentration of nitrogen source in the culture medium influenced the time at which accumulation started as well as the maximum levels of polysaccharide stored. Degradation of these glycogen reserves was observed near the beginning of sporulation. The onset of sporogenesis was always accompanied by a new accumulation of glycogen in sporulating hyphae. During spore maturation the accumulated polysaccharide was degraded. No glycogen was observed in aerial non-sporulating hyphae or in mature spores. Trehalose was detected during all phases of colony development. A preferential accumulation was found in aerial hyphae and spores, where it reached levels up to 12% of the cell dry weight. The possible roles of both carbohydrates in the developmental cycle of Streptomyces are discussed.

Disaccharides↗
PubMed1980

Regulatory control of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthetase in Streptomyces antibioticus.

Streptomyces antibioticus possesses a tryptophan-inhibitable 3-deoxy-D-arabino-heptulosonic acid 7-phosphate (DAHP) synthetase whose synthesis is also repressed by L-tryptophan. Studies of the DAHP synthetase obtained by ammonium sulfate fractionation of a crude extract derived from S. Antibioticus revealed that the enzymic activity was only partially inhibited by tryptophan. Inhibition of the DAHP synthetase activity was strongly pH dependent at values below 7.0. A number of tryptophan analogues was noted to inhibit the enzyme; by contrast, other aromatic amino acid end products failed to affect DAHP synthetase activity. Chorismic acid, a key intermediate in aromatic amino acid biosynthesis, was ineffective as an inhibitor when used alone; however, if supplied with L-tryptophan, a further reduction of DAHP synthetase activity (15--25%) was routinely observed.

3-Deoxy-7-Phosphoheptulonate Synthase↗
PubMed1978

Glutamate-induced uptake of proline by Streptomyces antibioticus.

Streptomyces antibioticus possesses an energy-dependent, carrier mediated transport system for the uptake of L-glutamate and L-proline. Amino acid transport was found to have a temperature optimum of 35 degrees C and a pH optimum from 7.0 to 8.0 for glutamate and 6.5 to 7.5 for proline uptake. Uptake did not depend upon Mg2+, Ca2+, Zn2+, Na+, or Fe2+ ions. Reversible p-hydroxymercuribenzoate inhibition of uptake indicated the involvement of an active sulfhydryl group. L-Glutamate uptake was mediated by a glutamate-inducible, nonspecific transport system, which was extremely stable and was not subject to substrate inhibition by L-proline. On the other hand, L-proline transport was mediated by at least two systems. The L-glutamate-inducible nonspecific system can account for uptake of proline by the mycelium grown in glutamate. In addition, a proline-specific, constitutive transport system was found to be present in the mycelium grown in organic and inorganic nitrogen sources other than L-glutamate. Shift experiments revealed that proline transport is not as stable as glutamate transport when the glutamate-inducible nonspecific system is utilized.

Bacterial Proteins↗
PubMed1988

An exocytoplasmic endonuclease with restriction function in Streptomyces antibioticus.

Streptomyces antibioticus produces a strong endo-DNase which is located between the cytoplasmic membrane and the cell wall. All DNA substrates assayed, including the chromosomal DNA of this species and several bacteriophage DNAs, were completely degraded in vitro by the enzyme. The rate of synthesis of the nuclease depended on the growth medium. In NBG medium, in which the enzyme is not produced, the size of lytic plaques of several actinophages was larger than that in GYM or GAE medium, in which synthesis of the nuclease takes place late in growth. In addition, one of the phages assayed, phi A6, showed a diminution of its efficiency of plating in GYM medium with respect to that in NBG medium; another phage, phi A9, grew in NBG medium but not in the other two media. It is postulated that the presence of the host nuclease, together with the capability of the particular phage to absorb on S. antibioticus of different growth phases, determines the efficiency of growth and the plaque size of the phages on productive media. This hypothesis was confirmed when the growth of phi A6 and phi A9 in a mutant of S. antibioticus lacking the endonuclease activity was analyzed. It is concluded that the enzyme can assume, under some circumstances, a role in in vivo restriction.

Bacteriophages↗
PubMed1983

Cloning and expression of the tyrosinase gene from Streptomyces antibioticus in Streptomyces lividans.

In two separate studies a BclI-generated DNA fragment coding for the enzyme tyrosinase, responsible for melanin synthesis, was cloned from Streptomyces antibioticus DNA into two SLP1.2-based plasmid vectors (pIJ37 and pIJ41) to generate the hybrid plasmids, designated pIJ700 and pIJ701, using S. lividans 66 as the host. The fragment (1.55 kb) was subcloned into the multicopy plasmid pIJ350 (which carries thiostrepton resistance and has two non-essential BclI sites) to generate four new plasmids (pIJ702-pIJ705) with the tyrosinase insert located in either orientation at each site. All six plasmids conferred melanin production (the Mel+ phenotype) on their host. As in the S. antibioticus parent, strains of S. lividans carrying the gene specifying tyrosinase synthesis possessed an enzyme activity which was inducible. Most of the tyrosinase activity was secreted during growth of S. antibioticus; in contrast, the majority remained intracellular in the S. lividans clones. The specific activity of the induced tyrosinase activity (intracellular) was higher (up to 36-fold) when the gene was present on the multicopy vector in comparison with its location on the low copy plasmids, pIJ700 or pIJ701, or in S. antibioticus. Restriction mapping of the tyrosinase fragment in pIJ702 revealed endonuclease cleavage sites for several enzymes, including single sites for BglII, SphI and SstI that are absent from the parent vector (pIJ350). Insertion of DNA fragments at any one of these sites abolished the Mel+ phenotype. The results indicate that pIJ702 is a useful cloning vector with insertional inactivation of the Mel+ character as the basis of clone recognition.

Catechol Oxidase↗
PubMed2000

Microbial growth and production kinetics of Streptomyces antibioticus Tü 6040.

Streptomyces antibioticus Tü 6040 is the producer of simocyclinones, which belong to a novel family of angucyclinone antibiotics some of which show antitumor activities. Growth and antibiotic production is dependent on the medium composition, especially on the carbon and nitrogen source, and on the fermentation conditions. The best results with respect to antibiotic productivity were achieved using a chemically defined medium with glycerol and L-lysine as carbon and nitrogen source, respectively, in an airlift fermenter with minimised shear stress at low gas flow rates withour oxygen limitation. These conditions led to a homogeneous formation of pellets of 1-2 mm in diameter and guaranteed reproducible product yields of the main compound, simocyclinone D8, in the range of 300 mg/l.

Anti-Bacterial Agents↗
PubMed1978

Fine structure, physiology and biochemistry of arthrospore germination in Streptomyces antibioticus.

During germination, Streptomyces antibioticus arthrospores passed through stages: darkening, swelling and germ tube emergence. The first stage, darkening, whose main features were a decrease in absorbance and a loss of refractility, only required exogenous divalent cations (Ca2+, Mg2+ or Fe2+) and energy that can be obtained from the spore reserves. This stage was blocked by agents that inhibit ATP formation but not by antibiotics that inhibit macromolecular synthesis. The second stage, swelling, needed an exogenous carbon source and was not blocked by mitomycin C. In this stage, the spores exhibited the highest cytochrome oxidase and catalase activities and respiratory quotient. The last stage, germ tube emergence, required additional carbon and nitrogen sources. Ammonium compounds were superior to nitrate. Dry weight remained constant during the stages of darkening and swelling, with a rapid increase from the moment of germ tube emergence. Optimum pH and temperature for germination were 8.0 and 45 degrees C, respectively. Heat treatment (55 degrees C for 10 min) had no effect on germination. The fine structure of the spore underwent important changes during germination. The wall of the swollen spore became stratified and the inner layer was continuous with the germ tube wall. Macromolecular synthesis occurred in the sequence RNA, protein and then DNA. Rifampicin, streptomycin and mitomycin C prevented synthesis when added at the start of incubation. The same effect was obtained if the addition was made during germination, except with mitomycin C which inhibited DNA, but not RNA and protein synthesis.

Anti-Bacterial Agents↗
PubMed1988

[Fusion of protoplasts in Streptomyces antibioticus].

The analysis of Streptomyces antibioticus recombinants isolated under non-selective conditions for stability of inheritance of parental properties demonstrated the existence of non-stable diploids and stable haploid recombinants. Also, genetic analysis of heteroclones isolated on selective medium after plating spores of regenerants was conducted. The results of analysis of haploid recombinant and heteroclones pointed to linkage of genetic loci and the possibility to use the technique of protoplast fusion for establishment of genetic map of S. antibioticus.

Alleles↗
PubMed1978

The possible involvement of a plasmid(s) in actinomycin synthesis by Streptomyces parvulus and Streptomyces antibioticus.

The treatment of Streptomyces parvulus and Streptomyces antibioticus with acriflavine or novobiocin resulted in the loss of ability to produce actinomycin. The concomitant loss of ability to form aerial mycelium and the incidence of auxotrophic progeny (S. parvulus) were both low relative to the loss of the antibiotic-producing property. Protoplast fusion induced by polyethylene glycol 4000, using suitable auxotrophic strains of S. parvulus, resulted in high recombination frequencies to prototrophy (9.6 approximately 15%). When fusion was carried out between auxotrophic act+ and act- strains, respectively, there was a high frequency (84 approximately 95%) of the actinomycin synthesizing character among the prototrophic recombinants examined. No actinomycin-producing recombinant was detected in similar experiments between auxotrophic non-producing strains.

Dactinomycin↗
PubMed1992

Role of glycosylation and deglycosylation in biosynthesis of and resistance to oleandomycin in the producer organism, Streptomyces antibioticus.

Cell extracts of Streptomyces antibioticus, an oleandomycin producer, can inactivate oleandomycin in the presence of UDP-glucose. The inactivation can be detected through the loss of biological activity or by alteration in the chromatographic mobility of the antibiotic. This enzyme activity also inactivates other macrolides (rosaramicin, methymycin, and lankamycin) which contain a free 2'-OH group in a monosaccharide linked to the lactone ring (with the exception of erythromycin), but not those which contain a disaccharide (tylosin, spiramycin, carbomycin, josamycin, niddamycin, and relomycin). Interestingly, the culture supernatant contains another enzyme activity capable of reactivating the glycosylated oleandomycin and regenerating the biological activity through the release of a glucose molecule. It is proposed that these two enzyme activities could be an integral part of the oleandomycin biosynthetic pathway.

Anti-Bacterial Agents↗
PubMed1984

Activation of phenoxazinone synthase expression in Streptomyces lividans by cloned DNA sequences from Streptomyces antibioticus.

Recombinant plasmids carrying Streptomyces antibioticus DNA (phenoxazinone synthase plasmids 1.8 and 4.3) have been used as templates in a streptomycete-coupled transcription-translation system. Analysis of the synthetic products from these experiments shows that PHS 1.8 and 4.3 appear to code for polypeptides which are not structurally related, as judged by immunoprecipitability, to the phenoxazinone synthase subunit. 35S-labeled cell extracts of Streptomyces lividans and S. lividans transformed with the phenoxazinone synthase plasmids each contain a protein which is precipitable with antiserum to S. antibioticus phenoxazinone synthase. These proteins have exactly the same electrophoretic mobility as the S. antibioticus phenoxazinone synthase subunit on one-and two-dimensional gels and the peptide maps of the proteins from the S. lividans clones are essentially indistinguishable from the map of the S. antibioticus phenoxazinone synthase subunit. Glycerol-gradient centrifugation of extracts of cells transformed with PHS 1.8 and 4.3 showed that both the large and small phenoxazinone synthase enzyme forms were present. Southern hybridization experiments demonstrated that pIJ2505, a pBR322 derivative containing the phenoxazinone synthase structural gene, hybridized to S. lividans DNA digested with BclI, SphI, SstI, and XhoI. The results obtained are discussed in terms of the hypothesis that the expression of phenoxazinone synthase activity in cells transformed with the PHS 1.8 and 4.3 plasmids results from the activation of an endogenous phenoxazinone synthase gene in S. lividans (and perhaps in other streptomycetes in the case of PHS 4.3) which is normally "silent" or expressed at very low levels.

Centrifugation, Density Gradient↗
PubMed1984

Molecular cloning and expression of the phenoxazinone synthase gene from Streptomyces antibioticus.

DNA fragments from the Streptomyces antibioticus genome have been cloned in Streptomyces lividans using the SphI site of the vector, pIJ702. Using a sib selection procedure, transformants were screened for their ability to produce levels of the enzyme, phenoxazinone synthase, which were detectable by enzyme assay. Three clones were obtained by this procedure. The recombinant plasmids from these clones contained inserts of 1.77, 2.45, and 4.28 kilobases in size. The clones and the corresponding recombinant plasmids were, therefore, referred to as PHS 1.8, PHS 2.4 and PHS 4.3. PHS 2.4 produced transformants with significantly higher phenoxazinone synthase specific activities than those observed in comparably grown S. antibioticus. Southern blotting showed that the cloned 2.45-kilobase insert hybridized to a fragment of exactly the same size in an SphI digest of S. antibioticus total DNA. Using a streptomycete-coupled transcription-translation system, PHS 2.4 was shown to code for the synthesis of a protein with the electrophoretic and immunological properties of the phenoxazinone synthase subunit. Thus, the 2.45-kilobase insert represents the structural gene for that subunit. The protein produced by S. lividans transformed with PHS 2.4 was shown to be virtually identical to the S. antibioticus subunit in terms of its electrophoretic mobility, peptide profile, and amino acid composition. It was further observed that cloning of the 2.45-kilobase insert in the orientation opposite to that obtained originally still resulted in high levels of phenoxazinone synthase expression in transformed S. lividans. However, the repression of phenoxazinone synthase synthesis by glucose which has been observed in S. antibioticus was not found when PHS 2.4 was used to transform S. lividans.

Amino Acids↗
PubMed1999

relA is required for actinomycin production in Streptomyces antibioticus.

The relA gene from Streptomyces antibioticus has been cloned and sequenced. The gene encodes a protein with an Mr of 93,653, which is 91% identical to the corresponding protein from Streptomyces coelicolor. Disruption of S. antibioticus relA produces a strain which grows significantly more slowly on actinomycin production medium than the wild type or a disruptant to which the intact relA gene was restored. Moreover, the disruptant was unable to accumulate ppGpp to the levels observed during the normal course of growth and actinomycin production in the wild type. The strain containing the disrupted relA gene did not produce actinomycin and contained significantly lower levels of the enzyme phenoxazinone synthase than the wild-type strain. Actinomycin synthetase I, a key enzyme in the actinomycin biosynthetic pathway, was undetectable in the relA disruptant. Growth of the disruptant on low-phosphate medium did not restore actinomycin production.

Amino Acid Sequence↗
PubMed1995

Nutrient optimization for production of broad spectrum antibiotic by Streptomyces antibioticus SR15.4.

Antibiotic production by Streptomyces antibioticus Sr15.4 was studied under various cultural conditions. During nutrient optimization it was found that the strain utilized glycerol as the best source of carbon at 1.044 molar level, and 0.020 molar arginine as the best source of nitrogen. The strain exhibited significant enhancement in antibiotic production when grown at pH 6.8.

Anti-Bacterial Agents↗
PubMed1996

Characterization of the ATPase activity of the N-terminal nucleotide binding domain of an ABC transporter involved in oleandomycin secretion by Streptomyces antibioticus.

The oleB gene of Streptomyces antibioticus, oleandomycin producer, encodes an ABC transporter containing two putative ATP-binding domains and is involved in oleandomycin resistance and secretion in this organism. We have overexpressed in Escherichia coli the N-terminal nucleotide-binding domain of OleB (OleB') as a fusion protein and purified the fusion protein by affinity chromatography. The fusion protein showed ATPase activity dependent on the presence of Mg2+ ions. ATPase activity was resistant to specific inhibitors of P-, F-, and V-type ATPase whereas sodium azide and 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-C1) were strong inhibitors. The change of Lys71, located within the Walker A motif of the OleB' protein, to Gln or Glu caused a loss of ATPase activity, whereas changing to Gly did not impair the activity. The results suggest that the intrinsic ATPase activity of purified fusion protein can be clearly distinguished from other ATP-hydrolysing enzymes, including ion-translocating ATPases or ABC-traffic ATPases, both on the basis of inhibition by different agents and since it hydrolyzes ATP without interacting with a hydrophobic membrane component.

ATP-Binding Cassette Transporters↗
PubMed1994

Structural changes induced by glycine on Streptomyces antibioticus.

Germination and vegetative growth of Streptomyces antibioticus in liquid medium with different concentrations of glycine was examined. Both processes proved to be sensitive to the amino acid, being inhibited by 5 and 2.5% glycine, respectively. At concentrations of 5% or more, lysis of the vegetative mycelium occurred. Subinhibitory concentrations of glycine induced structural changes on germinating spores. These included an increase in the number of germ tubes produced by spore, in relation to the control. Moreover, soon after outgrowth the tubes bifurcate, giving rise to germinated spores with a characteristic aspect, and anomalous formation of cross-walls that appear both within the spores and in the newly formed germinative tubes, at or close to the region of outgrowth. The branching effect of glycine was also observed during vegetative growth of S. antibioticus.

Dose-Response Relationship, Drug↗