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At least 19 recordsLinked to original sources
PubMed1978

Isolation of glucosyltransferase from Streptomyces aureofaciens.

Streptomyces aureofaciens B 96 grown on a synthetic medium glucosylated exogenous 1,2-dihydroxy-9,10-anthraquinone (alizarin). The glucosylation was inhibited by 2,4-dinitrophenol added to the cultivation medium. A cell-free preparation was obtained from the mycelium isolated after 16 h of growth and was found to catalyze the transfer of glucose from glucosyluridyl diphosphate to 1,2-dihydroxy-9,10-anthraquinone, giving rise to 1-hydroxy-2-(beta-D-glucopyranosyloxy)-9,10-anthraquinone.

Anthraquinones↗
PubMed1998

Iron deficiency-induced tetracycline production in submerged cultures by Streptomyces aureofaciens.

Streptomyces aureofaciens ATCC 10762 grown in rotary-shaken submerged cultures produced substantial amounts of tetracycline only when the defined medium was deprived of iron. The biosynthesis of tetracycline was inhibited either by free iron at concentrations above 1-2 mumol l-1, or by chelated iron provided by the siderophores of this bacterial strain. Late static iron-containing cultures allowed cell differentiation and sporulation and led to tetracyclines synthesis. A nitrosoguanidine-induced mutant able to synthesize tetracycline in the presence of iron in shaken submerged cultures was isolated and compared to the wild-type strain. However, no constitutive siderophore-mediated iron transport occurred in the mutant. These results suggest the involvement of a putative iron-controlled repressor in the biosynthesis of these secondary metabolites during vegetative growth and primary metabolism of the bacterium.

Iron↗
PubMed1966

Genetic Recombination in Crosses Between Streptomyces aureofaciens and Streptomyces rimosus.

Polsinelli, M. (University of Pavia, Pavia, Italy), and Maria Beretta. Genetic recombination in crosses between Streptomyces aureofaciens and Streptomyces rimosus. J. Bacteriol. 91:63-68. 1966.-Biochemical mutants were obtained from Streptomyces rimosus and S. aureofaciens by ultraviolet irradiation. Crosses were performed between auxotrophic strains of S. rimosus and S. aureofaciens with positive results. Data are reported which indicate that the interaction observed in some crosses is due to gene recombination.

Journal Article↗
PubMed1997

Disruption of a sigma factor gene, sigF, affects an intermediate stage of spore pigment production in Streptomyces aureofaciens.

The Streptomyces aureofaciens sigF gene encodes a sigma factor. By integrative transformation, via double cross-over, a stable null mutant of sigF gene was obtained. This mutation appeared to have no obvious effect on vegetative growth, but affected the late stage of spore maturation. Microscopic examination showed that spores were deformed, and spore wall was thinner, compared with the wild-type spores. The spore pigment of sigF mutant was green, compared to wild-type grey-pink spore pigmentation. The plasmid-born wild-type sigF gene complemented the mutation after transformation of the mutant strain.

Bacterial Proteins↗
PubMed1999

Cloning of the putative aldehyde dehydrogenase, aldA, gene from Streptomyces aureofaciens.

A Streptomyces aureofaciens gene, gap, encoding glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was previously identified. Hybridization studies suggested the presence of a second gap gene in S. aureofaciens. To clone the gene, S. aureofaciens subgenomic library was screened with an oligonucleotide probe encoding a peptide motif conserved in all GAPDH. 3352 bp positive BamHI fragment was identified, the length of which correlated with the hybridization signal. The nucleotide sequence of the fragment was determined, and analysis of the sequence revealed the presence of three open reading frames (ORF). However, none of the genes coded for GAPDH. All three genes formed an operon, consisting of gene orf251, with a high homology to a conserved gene present only in archaeabacteria, and the aldA and adhA genes homologous to various eukaryotic and prokaryotic aldehyde- and alcohol-dehydrogenases, with maximum homology to the phenylacetaldehyde dehydrogenases and arylalcohol dehydrogenases, respectively.

Aldehyde Dehydrogenase↗
PubMed1991

Highly transformable mutants of Streptomyces aureofaciens containing restriction-modification systems.

Streptomyces aureofaciens 13 is a mutant defective in chlortetracycline production. It was chosen as a potentially useful host for gene cloning in investigations of the organization of the biosynthetic genes for the tetracycline antibiotic pathway. From the Streptomyces aureofaciens 13 strain, three suitable clones were used for our work. The conditions for optimal formation and efficient transformation of protoplasts with plasmid DNAs have been determined. Transformation frequencies of about 10(4) to 10(5) per microgram of plasmid DNA were obtained when plasmids were isolated from Streptomyces strains. From the patterns of restriction enzyme digestion of plasmid DNA isolated from Streptomyces aureofaciens transformants, it was observed that the clones express modification systems which render plasmid DNAs resistant to cleavage by HindIII and EcoRI. Additionally, one of the clones produces the restriction endonuclease Sau13I (isoschizomer of SauI). The presence of the restriction-modification system of Sau13I does not reduce the efficiency of plasmid transformation.

DNA Restriction Enzymes↗
PubMed1978

Specific endonucleases in Streptomyces aureofaciens.

Two strains of Streptomyces aureofaciens were found to contain restriction endodeoxynucleases; S. aureofaciens IKA 18/4 contains Sau I which splits lambda DNA into three fragments, S. aureofaciens IKA 22201 Sau Ii which splits lambda DNA into more than 15 fragments.

Coliphages↗
PubMed1987

DNA-dependent RNA polymerase from the chlorotetracycline producing strain of Streptomyces aureofaciens.

RNA polymerase from Streptomyces aureofaciens has been purified by polyethyleneimine precipitation followed by chromatography first on DEAE-cellulose, then heparin-Sepharose and finally on an aminooxybutylcellulose matrix containing immobilised S. aureofaciens DNA. The enzyme is composed of three subunits of approximately 145, 136 and 44 kDa that are in a ratio of approx. 1:1:2. In many isolations two additional subunits of approximately 68 and 39 kDa and some minor protein bands of approximately 110, 85 and 61 kDa are also present. Thus, the structure of this enzyme is very similar to other bacterial RNA polymerases, exhibiting an alpha 2 beta beta' core and the additional proteins rho and sigma.

Chlortetracycline↗
PubMed1994

Cloning of a second non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces lividans and enzyme purification.

The gene for BPO-A1, one of two non-haem bromoperoxidases in the tetracycline and 7-chlorotetracycline producer Streptomyces aureofaciens ATCC 10762, was cloned in the positive selection vector pIJ699 and expressed in Streptomyces lividans TK64. The cloned bromoperoxidase was over-produced up to 2800-fold by the S. lividans TK64 transformant. By taking advantage of the over-production of BPO-A1 and the heat stability of the enzyme, a new and simple purification procedure was developed. Subcloning into the vector pIJ487 and screening of recombinants by a newly developed histochemical assay located the bpoA1 gene on a 2.1 kb BamHI-HindIII fragment. The nucleotide sequence of the 2.1 kb fragment was determined; the bpoA1 gene was identified within the sequence on the basis of the biased codon usage of Streptomyces genes and the presence of a nucleotide sequence encoding the N-terminal amino acid sequence obtained from the purified BPO-A1. Comparison of the deduced primary structure of BPO-A1 with those deduced for the non-haem chloroperoxidase CPO-P from Pseudomonas pyrrocinia and the bromoperoxidase BPO-A2 from S. aureofaciens ATCC 10762 gave amino acid sequence identities of 49% and 40%, respectively.

Amino Acid Sequence↗
PubMed1968

Effect of temperature on the coproduction of chlortetracycline and tetracycline by Streptomyces aureofaciens.

Five strains of Streptomyces aureofaciens of diverse origin and ability to incorporate chloride into chlortetracycline (CTC) were grown at five temperatures of incubation ranging from 20 to 31 C in media of high and low chloride content. Maximal accumulation of CTC and tetracycline (TC) occurred in the 23 to 25 C range. Departure from this range affected the different strains to various degrees in total accumulation. Lower temperatures favored a relative increase in the amount of CTC produced by all strains. Higher temperatures were conducive to the almost exclusive production of TC by some strains but at the expense of an 80 to 90% reduction in potential total yield obtained at lower temperatures. The optimal temperature for maximal biochemical chlorination by some strains of S. aureofaciens was less than the optimal temperature for maximal accumulation of the tetracycline nucleus.

Chlorides↗
PubMed1991

Crystallization and preliminary X-ray data of bromoperoxidase from Streptomyces aureofaciens ATCC 10762.

Bromoperoxidase from Streptomyces aureofaciens ATCC 10762, a non-haem haloperoxidase, has been crystallized using the hanging drop method. Preliminary X-ray diffraction studies show that the crystals belong to the cubic space group P2(1)3 with a = 123.4 A. The asymmetric unit contains a dimer of Mr = 60,200. The crystals diffract to at least 2.3 A resolution and are suitable for crystallographic structure analysis.

Crystallization↗
PubMed2004

Identification and cloning of the gene involved in the final step of chlortetracycline biosynthesis in Streptomyces aureofaciens.

For chlortetracycline biosynthesis in Streptomyces aureofaciens, the final reduction step is essential to give an antibiotic activity to its intermediate, which is catalyzed by tetracycline dehydrogenase with 7,8-dedimethyl-8-hydroxy-5-deazariboflavin (FO) as a cofactor. We identified and cloned the gene, which is essential for the biosynthesis of 6-demethyltetracycline and participates in the final step of its biosynthesis, from the genomic DNA of the 6-demethyltetracycline producer S. aureofaciens HP77. DNA sequence analysis revealed that the gene (tchA) had an open reading frame of 455 amino acids with an estimated molecular mass of 48.1 kDa. Southern hybridization analysis revealed that the tchA gene was located external to the chlortetracycline biosynthetic gene cluster in the genome. A conserved domain search of protein sequence databases indicated that TchA showed a similarity to FbiB, which is involved in the modification of FO in Mycobacterium bovis.

Base Sequence↗
PubMed2002

[Cloning and expression of Vitreoscilla hemoglobin in Streptomyces aureofaciens].

Vitreoscilla hemoglobin Gene was cloned in Streptomyces aureofaciens through E. coli-Streptomyces shuttle plasmids constructed by both pIJ699-pUC19(vhb) and pIJ702-pBR322(vhb). Under low dissolved oxygen conditions, expression of hemoglobin enhanced CTC yield of engineering strain more about 40%-60% that that of control by improving oxygen transmission in cells. Hemoglobin expression by Promoter of tetracycline resistance gene was more effective for oxygen transmission than that by its native promoter regulated by dissolved oxygen concentrations in environments of locally low concentrations of dissolved oxygen.

Bacterial Proteins↗
PubMed1998

Purification and characterization of the malate dehydrogenase from Streptomyces aureofaciens.

The malate dehydrogenase (MDH) from Streptomyces aureofaciens was purified to homogeneity and its physical and biochemical properties were studied. Its amino-terminal sequence perfectly matched the amino-terminal sequence of the MDH from Streptomyces atratus whose biochemical characteristics have never been determined. The molecular mass of the native enzyme, estimated by size-exclusion chromatography, was 70 kDa. The protein was a homodimer, with a 38-kDa subunit molecular mass. It showed a strong specificity for NADH and was much more efficient for the reduction of oxaloacetate than for the oxidation of malate, with a pH optimum of 8. Unlike MDHs from other sources, it was not inhibited by excess oxaloacetate. This first complete functional characterization of an MDH from Streptomyces shows that the enzyme is very similar in many respects to other bacterial MDHs with the notable exception of a lack of inhibition by excess substrate.

Amino Acid Sequence↗