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PubMed2026

Streptomyces xingningensis sp. nov. and Streptomyces rhizosphaerae sp. nov. isolated from the rhizosphere soil of Camellia oleifera.

Two novel actinobacteria strains, designated YCB024T and YCB041T, were isolated from rhizosphere soil samples of Camellia oleifera collected from Xingning City, Guangdong Province, PR China. Both strains exhibited mycelial filaments and intertwined hyphal cells. Phylogenetic analysis revealed that strain YCB024T exhibited the highest 98.8% 16S rRNA gene similarity with Streptomyces yogyakartensis NBRC 100779T, Streptomyces javensis NBRC 100777T and Streptomyces violaceusniger NBRC 13459T, and strain YCB041T exhibited the highest 98.9% similarity with Streptomyces albospinus NBRC 13846T. The average nucleotide identities (ANI) and digital DNA-DNA hybridization (dDDH) values among the two strains and their closely related species indicated that they were clearly different from other known Streptomyces species. The draft genome sizes of the two strains were 6.9 Mbp and 9.5 Mbp with DNA G+C contents of 70.4 mol% and 71.7 mol%. The major cellular fatty acids in strain YCB024T included iso-C14 : 0, iso-C15 : 0, anteiso-C15 : 0, iso-C16 : 0 and C16 : 0, and strain YCB041T included iso-C15 : 0, anteiso-C15 : 0, iso-C16 : 0 and C16 : 0. The major polar lipids of the two strains were diphosphatidylglycerol, phosphatidylethanolamine, phosphatidylinositol mannoside or unidentified aminophospholipid. The respiratory quinones of both strains included MK-9 (H6), MK-9 (H8) and MK-10 (H4). Based on phylogenetic analysis, ANI and dDDH values, physiological and chemical properties, strains YCB024T and YCB041T represent two novel species of the genus Streptomyces, for which the names Streptomyces xingningensis sp. nov. (type strain YCB024T=GDMCC 4.314T=JCM 36249T) and Streptomyces rhizosphaerae sp. nov. (type strain YCB041T=GDMCC 4.469T=JCM 38170T) are proposed, respectively.

Streptomyces↗
PubMed1986

Clavamycins, new clavam antibiotics from two variants of Streptomyces hygroscopicus. II. Isolation and structures of clavamycins A, B and C from Streptomyces hygroscopicus NRRL 15846, and of clavamycins D, E and F from Streptomyces hygroscopicus NRRL 15879.

Clavamycins A, B, C, D, E and F represent new members of the clavam antibiotics group. Their purification was achieved by a variety of preparative chromatographic methods, essentially on reversed phase carrier. The structures were deduced from spectroscopic properties, especially from extensive NMR studies.

Antifungal Agents↗
PubMed1998

Streptomyces thermocarboxydovorans sp. nov. and Streptomyces thermocarboxydus sp. nov., two moderately thermophilic carboxydotrophic species from soil.

Four moderately thermophilic, carboxydotrophic streptomycetes were the subject of a comparative taxonomic investigation designed to establish their taxonomic relationships. Almost complete sequences of the 16S rRNA genes of the test strains were determined following the isolation and direct sequencing of the amplified genes. The resultant nucleotide sequences were aligned with the sequences of previously studied streptomycetes, and phylogenetic trees generated by using the neighbour-joining, Fitch-Margoliash, maximum-likelihood and maximum-parsimony methods. It was evident from the phylogenetic analyses that strains AT50, AT51 and AT52 were most closely related to Streptomyces thermodiastaticus DSM 40573T and strain AT37 to Streptomyces glaucescens DSM 40716 and Streptomyces pseudogriseolus NRRL 3985. Random DNA amplification profiles clearly distinguished strains AT50, AT51 and AT52 from Streptomyces thermodiastaticus and from strain AT37. The molecular systematic evidence, together with phenotypic data derived from this and previous studies, indicate that the test strains merit species status within the genus Streptomyces. The name Streptomyces thermocarboxydovorans sp. nov. is proposed for strains AT50, AT51 and AT52 (type strain) and Streptomyces thermocarboxydus sp. nov. for strain AT37.

DNA, Bacterial↗
PubMed2006

Streptomyces turgidiscabies and Streptomyces reticuliscabiei: one genomic species, two pathogenic groups.

Three strains of Streptomyces reticuliscabiei and two strains of Streptomyces turgidiscabies were analysed, together with reference and type strains of other Streptomyces species, for phenotypic traits, DNA-DNA relatedness, comparison of 16S rRNA gene sequences and presence of necrotic protein gene (nec1) homologues in order to clarify their phylogenetic relationships. A numerical analysis of phenotypic characteristics showed that S. reticuliscabiei and S. turgidiscabies belong to the same cluster and share almost all morphological and biochemical traits that are important in the identification of Streptomyces species. DNA-DNA hybridization and phylogenetic comparisons of 16S rRNA gene sequences confirmed that the two species are genomically closely related. In contrast, pathological data showed that S. turgidiscabies and S. reticuliscabiei cause two distinct diseases. Gene homologues of nec1 were detected in S. turgidiscabies and other common scab species (Streptomyces scabiei, Streptomyces europaeiscabiei and Streptomyces stelliscabiei), but not in S. reticuliscabiei. To avoid confusion between agents causing separate diseases, it is proposed that the existing distinct species names are retained: S. turgidiscabies involved in common scab and S. reticuliscabiei involved in netted scab.

Bacterial Proteins↗
PubMed2005

Expression of the melC operon in several Streptomyces strains is positively regulated by AdpA, an AraC family transcriptional regulator involved in morphological development in Streptomyces coelicolor.

Dark brown haloes of melanin around colonies are an easily visualized phenotype displayed by many Streptomyces strains harboring plasmid pIJ702 carrying the melC operon of Streptomyces antibioticus IMRU3270. Spontaneous melanin-negative mutants of pIJ702 occur with a frequency of ca. 1%, and often mutation occurs in the melC operon, which removes the BglII site as part of an inverted repeat. Other melanin-negative mutations seem to occur spontaneously in Streptomyces lividans, resulting in white colonies from which intact, melanin-producing pIJ702 can be isolated by introduction into a new host. S. lividans ZX66 was found to be such a mutant and to have a secondary mutation influencing expression of the melC operon on the chromosome. A 3.3-kb DNA fragment was isolated from its progenitor strain, JT46, and a gene able to restore melC operon expression was found to encode a member of an AraC family of transcriptional regulators, which was equivalent to AdpA(c) in Streptomyces coelicolor and therefore was designated AdpA(l). Lack of melC operon expression was correlated with a single A-to-C transversion, which altered a single key amino acid residue from Thr to Pro. The transcription of the melC operon was found to be greatly reduced in the adpA mutant background. The counterpart gene (adpA(a)) in the S. antibioticus strain in which the melC operon carried on pIJ702 originated was also isolated and was found to have an identical regulatory role. Thus, we concluded that the melC operon is under general direct positive control by AdpA family proteins, perhaps at the transcriptional level and certainly at the translational level via bldA, in Streptomyces.

Bacterial Proteins↗
PubMed1986

Biotransformation of aklanonic acid by blocked mutants of anthracycline-producing strains of Streptomyces galilaeus and Streptomyces peucetius.

Aklanonic acid is an anthracyclinone-related pigment that was found to be an intermediate at an early stage of the biosynthesis of daunomycinone glycosides by Streptomyces griseus. We now isolated anthracycline-negative mutants of other Streptomyces species and used them in feeding experiments with both natural and radioactive aklanonic acid. In cultures of the mutant Streptomyces galilaeus S 727 exogenous aklanonic acid was biotransformed to cinerubin A as the major product. The spectrum of the conversion products was qualitatively comparable to that of the parent strain. In cultures of mutant 21/8 derived from Streptomyces peucetius var. caesius the predominant conversion product was epsilon-rhodomycinone. Daunomycinone glycosides were isolated in small amounts. According to results obtained with the radioactively labelled precursor aklanonic acid was completely incorporated into the molecules of the conversion products. Our findings suggest that aklanonic acid is also a natural intermediate in the biosynthesis of anthracyclines by Streptomyces galilaeus and Streptomyces peucetius. Proposed biosynthetic pathways have been constructed.

Anthracyclines↗
PubMed1987

Primary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene.

An 11,450-base DNA fragment containing the gene for the extracellular active-site serine DD-peptidase of Streptomyces R61 was cloned in Streptomyces lividans using the high-copy-number plasmid pIJ702 as vector. Amplified expression of the excreted enzyme was observed. Producing clones were identified with the help of a specific antiserum directed against the pure DD-peptidase. The coding sequence of the gene was then located by hybridization with a specific nucleotide probe and sub-fragments were obtained from which the nucleotide sequence of the structural gene and the putative promoter and terminator regions were determined. The sequence suggests that the gene codes for a 406-amino-acid protein precursor. When compared with the excreted, mature DD-peptidase, this precursor possesses a cleavable 31-amino-acid N-terminal extension which has the characteristics of a signal peptide, and a cleavable 26-amino-acid C-terminal extension. On the basis of the data of Joris et al. (following paper in this journal), the open reading frame coding for the synthesis of the DD-peptidase was established. Comparison of the primary structure of the Streptomyces R61 DD-peptidase with those of several active-site serine beta-lactamases and penicillin-binding proteins of Escherichia coli shows homology in those sequences that comprise the active-site serine residue. When the comparison is broadened to the complete amino acid sequences, significant homology is observed only for the pair Streptomyces R61 DD-peptidase/Escherichia coli ampC beta-lactamase (class C). Since the Streptomyces R61 DD-peptidase and beta-lactamases of class A have very similar three-dimensional structures [Kelly et al. (1986) Science (Wash. DC) 231, 1429-1431; Samraoui et al. (1986) Nature (Lond.) 320, 378-380], it is concluded that these tertiary features are probably also shared by the beta-lactamases of class C, i.e. that the Streptomyces R61 DD-peptidase and the beta-lactamases of classes A and C are related in an evolutionary sense.

Amino Acid Sequence↗
PubMed2003

Intergeneric conjugation in Streptomyces peucetius and Streptomyces sp. strain C5: chromosomal integration and expression of recombinant plasmids carrying the chiC gene.

Intergeneric conjugal transfer of plasmid DNA from Escherichia coli to Streptomyces circumvents problems such as host-controlled restriction and instability of foreign DNA during the transformation of Streptomyces protoplasts. The anthracycline antibiotic-producing strains Streptomyces peucetius and Streptomyces sp. strain C5 were transformed using E. coli ET12567(pUZ8002) as a conjugal donor. When this donor species, carrying pSET152, was mated with Streptomyces strains, the resident plasmid was mobilized to the recipient and the transferred DNA was also integrated into the recipient chromosome. Analysis of the exconjugants showed stable integration of the plasmid at a single chromosomal site (attB) of the Streptomyces genome. The DNA sequence of the chromosomal integration site was determined and shown to be conserved. However, the core sequence, where the crossover presumably occurred in C5 and S. peucetius, is TTC. These results also showed that the phiC31 integrative recombination is active and the phage attP site is functional in S. peucetius as well as in C5. The efficiency and specificity of phiC31-mediated site-specific integration of the plasmid in the presence of a 3.7-kb homologous DNA sequence indicates that integrative recombination is preferred under these conditions. The integration of plasmid DNA did not affect antibiotic biosynthesis or biosynthesis of essential amino acids. Integration of a single copy of a mutant chiC into the wild-type S. peucetius chromosome led to the production of 30-fold more chitinase.

Attachment Sites, Microbiological↗
PubMedDate not supplied

[Cell wall teichoic acids from Streptomyces daghestanicus VKM Ac-1722T and Streptomyces murinus INA-00524T].

The structure of cell wall teichoic acids was studied by chemical methods and NMR spectroscopy in the type strains of two actinomycete species of the "Streptomyces griseoviridis" phenetic cluster: Streptomyces daghestanicus and Streptomyces murinus. S. daghestanicus VKM Ac-1722T contained two polymers having a 1,5-poly(ribitol phosphate) structure. In one of them, the ribitol units had alpha-rhamnopyranose and 3-O-methyl-alpha-rhamnopyranose substituents; in the other, each ribitol unit was carrying 2,4-ketal-bound pyruvic acid. Such polymers were earlier found in the cell walls of Streptomyces roseolus and Nocardiopsis albus, respectively; however, their simultaneous presence in the cell wall has never been reported. The cell wall teichoic acid of Streptomyces murinus INA-00524T was is a 1,5-poly(glucosylpolyol phosphate), whose repeating unit was [-6)-beta-D-glucopyranosyl-(1 --> 2)-glycerol phosphate-(3-P-]. Such a teichoic acid was earlier found in Spirilliplanes yamanashiensis. The 13C NMR spectrum of this polymer is presented for the first time. The results of the present investigation, together with earlier published data, show that the type strains of four species of the "Streptomyces griseoviridis" phenetic cluster differ in the composition and structure of their teichoic acids; thus, teichoic acids may serve as chemotaxonomic markers of the species.

Cell Wall↗
PubMed2005

Desferrioxamine E produced by Streptomyces griseus stimulates growth and development of Streptomyces tanashiensis.

The authors previously reported that interspecific stimulatory events between Streptomyces species for antibiotic production and/or morphological differentiation mediated by putative diffusible metabolites take place at a high frequency. This paper reports the isolation and characterization of a substance produced by Streptomyces griseus that stimulates the growth and development of Streptomyces tanashiensis. The substance was purified from the culture supernatant of S. griseus by using anion-exchange chromatography, gel filtration chromatography and reverse-phase HPLC. FAB-MS and NMR analyses of the purified preparation indicated the substance to be desferrioxamine E (synonym: nocardamine), a siderophore that is widely produced by Streptomyces species and related organisms. Similar stimulatory effects on the growth and development of S. tanashiensis were exerted by desferrioxamine E produced by another actinomycete strain, but not by other siderophores tested, including ferrichrome and nocobactin and free ferric ion. An exogenous supply of desferrioxamine E stimulated secondary metabolite formation and/or morphological differentiation in various actinomycete strains. Disruption of the desferrioxamine biosynthesis gene cluster in Streptomyces coelicolor A3(2) abolished the production of desferrioxamine E and the activity to stimulate the growth and differentiation of S. tanashiensis. The S. coelicolor mutant showed impaired growth and development on Bennett's/glucose agar medium, but it was rescued by the exogenous supply of desferrioxamine E. These results indicate that desferrioxamines play an important role in streptomycete physiology. Similar to several pathogenic bacteria and fungi, S. tanashiensis may be defective in the production of siderophores; however, it can utilize the siderophores excreted by other organisms.

Chromatography, High Pressure Liquid↗
PubMed1991

Cloning and characterization of the isopenicillin N synthase gene of Streptomyces griseus NRRL 3851 and studies of expression and complementation of the cephamycin pathway in Streptomyces clavuligerus.

A gene, pcbC, encoding the isopenicillin N synthase of Streptomyces griseus NRRL 3851, has been cloned in a 6.4-kb Bg/II DNA fragment and located in an internal 1.55-kb PvuII segment by hybridization with the Penicillium chrysogenum pcbC gene. Hybridization studies revealed the presence of homologous sequences in the DNAs of several Streptomyces strains and Nocardia lactamdurans. The S. griseus pcbC gene was not expressed in Streptomyces lividans but was expressed in Streptomyces clavuligerus and complemented a mutation, nce2, that impaired isopenicillin N synthase and cephamycin biosynthesis. The pcbC gene contained an open reading frame of 990 nucleotides that encodes a protein of 329 amino acids with a deduced Mr of 37,371. The isopenicillin N synthase formed after expression of the pcbC gene in the S. clavuligerus nce2 mutant strain was found to have an Mr of 38,000 by gel filtration. A protein of about 38 kDa was observed in sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels of extracts of a transformant of the nce2 mutant strain; this protein was absent from the untransformed mutant strain. The G+C content of the pcbC gene was 63.6%, and the strongly biased codon usage was typical of that of Streptomyces strains. A transcription initiation site was found 44 nucleotides upstream of the ATG translation initiation triplet. A transcript of 1.1 kb was observed in the donor S. griseus strain and also in the S. clavuligerus nce2 mutant strain transformed with the pcbC gene, suggesting that it is transcribed as a monocistronic mRNA.

Actinomycetales↗
PubMed1977

Studies on the production of daunomycinone-derived glycosides and related metabolites in Streptomyces coeruleorubidus and Streptomyces peucetius.

Strains of Streptomyces coeruleorubidus ISP 5145, JA 10092 and 39-146, differing mutually in antibiotic activity, were found to produce identical spectrum of metabolites (at least nine antibiotically active glycosides, 13-dihydrodaunomycinone, epsilon-rhodomycinone and a larger number of unidentified compounds); only trace quantities of daunomycin and daunomycinone could be detected. A fraction of glycosides with a higher RF (0.4-0.7), isolated from strain 39-146, could be transformed to daunomycin by mild hydrolysis and to daunomycinone by total hydrolysis. Streptomyces peucetius IMI 101 335 differed from Streptomyces coeruleorubidus in an increased production of epsilon-rhodomycinone and a lower content of glycosides; the zone of daunomycin was most pronounced among the glycoside spots. Streptomyces coeruleorubidus 39-146 exhibited the highest activity in a medium containing 3.5% soluble starch, 3.0% soybean meal, 0.3% NaCl and 0.3% CaCo3; glucose was a more useful carbon source for the remaining strains. The activity of Streptomyces coeruleoribidus was inhibited by 1-propanol, Na-propionate, 5,5-diethylbarbiturate and bacitracin. Ferrous sulphate stimulated the production of glycosides only in strain JA 10092, decreasing simultaneously the production of aglycones.

Chromatography, Thin Layer↗
PubMed1988

The hyg gene promoter from Streptomyces hygroscopicus: a novel form of Streptomyces promoters.

A 207 bp DNA fragment from the 5' region of the hyg gene of Streptomyces hygroscopicus was located preceding a DNA sequence encoding the mature form of human interferon alpha 2. This gene fusion, inserted in the Streptomyces vector pIJ702, expressed interferon activity in Streptomyces lividans indicating that the 207 bp sequence has promoter activity. The transcription initiation site was located. No significant homology with previously described Streptomyces promoters could be found. It appears therefore, it represents a novel class of Streptomyces promoters.

Base Sequence↗
PubMed2004

Genome analyses of Streptomyces peucetius ATCC 27952 for the identification and comparison of cytochrome P450 complement with other Streptomyces.

We have determined the genome sequence of 8.7 Mb chromosome of Streptomyces peucetius ATCC 27952, which produces clinically important anthracycline chemotherapeutic agents of the polyketide class of antibiotics, daunorubicin and doxorubicin. The cytochrome P450 (CYP) superfamily is represented by 19 sequences in the S. peucetius. Among those, 15 code for functional genes, whereas the remaining four are pseudo genes. CYPs from S. peucetius are phylogenetically close to those of Streptomyces amermitilis. Four CYPs are associated with modular PKS of avermectin and two with doxorubicin biosynthetic gene cluster. CYP252A1 is the new family found in S. peucetius, which shares 38% identity to CYP51 from Streptomyces coelicolor A3 (2). Nine CYPs from S. peucetius are found in the cluster containing various regulatory genes including rar operon, conserved in S. coelicolor A3 (2) and Streptomyces griseus. Although two ferredoxins and four ferredoxin reductases have been identified so far, only one ferredoxin reductase was found in the cluster of CYP147F1 in S. peucetius. To date, 174 CYPs have been described from 45 Streptomyces species in all searchable databases. However, only 18 CYPs are clustered with ferredoxin. The comparative study of cytochrome P450s, ferredoxins, and ferredoxin reductases should be useful for the future development and manipulation of antibiotic biosynthetic pathways.

Amino Acid Sequence↗
PubMed1980

DNA cloning in Streptomyces: a bifunctional replicon comprising pBR322 inserted into a Streptomyces phage.

The Gram-positive, mycelial, differentiating streptomycetes are responsible for the production of many important antibiotics. The availability of gene cloning systems in this microbial group would have many industrial applications besides allowing more penetrating study of the genetics of Streptomyces coelicolor A3(2) (which, as the best understood streptomycete genetically, serves as a model for much other Streptomyces genetics). Recent successes (see previous paper) in introducing Streptomyces DNA into S. coelicolor and Streptomyces lividans on plasmid vectors would be nicely complemented by the availability of Streptomyces bacteriophage vectors (discussed in ref. 5): for example, many phages have wide and easily defined host ranges; heat-inducible prophages might be used to give high copy number of cloned DNA; efficient phage promoters might be used to increase gene expression; there may be differential stabilities for particular DNA sequences cloned in plasmids vis-à-vis phages; selective insertion of DNA, utilizing packaging constraints, may be possible with phages; and in situ hybridization of radioactive probes to DNA in plaques is likely to be simple. We describe here the use of the moderately wide host range temperate phage, phi C31, for this purpose.

Bacteriophages↗
PubMed1999

Evidence that a single EF-Ts suffices for the recycling of multiple and divergent EF-Tu species in Streptomyces coelicolor A3(2) and Streptomyces ramocissimus.

The tsf genes from Streptomyces coelicolor A3(2) and Streptomyces ramocissimus, encoding the guanine-nucleotide exchange factor EF-Ts, were cloned and sequenced. Streptomycetes have multiple and highly divergent EF-Tu species, with EF-Tu1 and EF-Tu3 showing only about 65% amino acid sequence identity, and yet these can apparently interact with a single EF-Ts species. tsf lies in an operon with rpsB, which encodes ribosomal protein S2. The amino acid sequence of S2 from S. coelicolor differs from most other bacterial S2 homologues in having a C-terminal extension of 70 aa residues with a highly repetitive organization, the function of which is unknown. Transcription analysis of the rpsB-tsf operon of S. coelicolor by promoter probing, nuclease S1 mapping and Northern blotting revealed that the genes give rise to a bicistronic transcript from a single promoter upstream of rpsB. An attenuator was identified in the rpsB-tsf intergenic region; it results in an approximately 2:1 ratio of rpsB vs tsf transcripts. Although tuf1, encoding the major EF-Tu, is located in the rpsL ribosomal protein operon, an additional promoter in the fus-tuf1 intergenic region leads to a significant excess of EF-Tu over ribosomes. Most amino acid residues known from the Escherichia coli crystal structure of the EF-Tu-EF-Ts complex to be directly involved in interaction between the two elongation factors are conserved between E. coli and Streptomyces. However, whenever interaction residues in the EF-Tu moiety show divergence among Streptomyces EF-Tu1, EF-Tu2 and EF-Tu3, the single Streptomyces EF-Ts exhibits compensatory substitutions of the corresponding residues. These apparently enable productive interaction to occur with all three EF-Tus.

Amino Acid Sequence↗