Streptomyces pristinaespiralis ATCC 25486
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ABSTRACT:
PROVIDER: PRJNA28553 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR004368.fastq.gz | Fastqsanger.gz | |||
| SRR017401.fastq.gz | Fastqsanger.gz |
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Project description:Pristinamycin, produced by Streptomyces pristinaespiralis Pr11, is a streptogramin antibiotic consisting of two chemically unrelated compounds, pristinamycin I and pristinamycin II. The semi-synthetic derivatives of these compounds are used in human medicine as therapeutic agents against methicillin-resistant Staphylococcus aureus strains. Only the partial sequence of the pristinamycin biosynthetic gene cluster has been previously reported. To complete the sequence, overlapping cosmids were isolated from a S. pristinaespiralis Pr11 gene library and sequenced. The boundaries of the cluster were deduced, limiting the cluster size to approximately 210 kb. In the central region of the cluster, previously unknown pristinamycin biosynthetic genes were identified. Combining the current and previously identified sequence information, we propose that all essential pristinamycin biosynthetic genes are included in the 210 kb region. A pristinamycin biosynthetic pathway was established. Furthermore, the pristinamycin gene cluster was found to be interspersed by a cryptic secondary metabolite cluster, which probably codes for a glycosylated aromatic polyketide. Gene inactivation experiments revealed that this cluster has no influence on pristinamycin production. Overall, this work provides new insights into pristinamycin biosynthesis and the unique genetic organization of the pristinamycin gene region, which is the largest antibiotic 'supercluster' known so far.
| S-EPMC3818860 | biostudies-literature
Project description:Streptomyces pristinaespiralis overview
| PRJNA36845 | ENA
Project description:Pristinamycin production in Streptomyces pristinaespiralis Pr11 is tightly regulated by an interplay between different repressors and activators. A γ-butyrolactone receptor gene (spbR), two TetR repressor genes (papR3 and papR5), three SARP (Streptomyces antibiotic regulatory protein) genes (papR1, papR2, and papR4), and a response regulator gene (papR6) are carried on the large 210-kb pristinamycin biosynthetic gene region of Streptomyces pristinaespiralis Pr11. A detailed investigation of all pristinamycin regulators revealed insight into a complex signaling cascade, which is responsible for the fine-tuned regulation of pristinamycin production in S. pristinaespiralis.
| S-EPMC4561715 | biostudies-literature
Project description:Produces anticancer agents
| PRJNA13658 | ENA
Project description:Pristinamycin biosynthesis in Streptomyces pristinaespiralis is governed by a complex hierarchical signaling cascade involving seven different transcriptional regulators (SpbR, PapR1, PapR2, PapR3, PapR4, PapR5, and PapR6). The signaling cascade is triggered by ?-butyrolactone (GBL)-like effector molecules, whereby the chemical structure of the effector, as well as its biosynthetic origin is unknown so far. Three of the pristinamycin transcriptional regulators (SpbR, PapR3, and PapR5) belong to the type of ?-butyrolactone receptor (GBLR). GBLRs are known to either act as "real" GBLRs, which bind GBLs as ligands or as "pseudo" GBLRs binding antibiotics or intermediates thereof as effector molecules. In this study, we performed electromobility shift assays (EMSAs) with SpbR, PapR3, and PapR5, respectively, in the presence of potential ligand samples. Thereby we could show that all three GBLRs bind synthetic 1,4-butyrolactone but not pristinamycin as ligand, suggesting that SpbR, PapR3, and PapR5 act as "real" GBLRs in S. pristinaespiralis. Furthermore, we identified a cytochrome P450 monooxygenase encoding gene snbU as potential biosynthesis gene for the GBLR-interacting ligand. Inactivation of snbU resulted in an increased pristinamycin production, which indicated that SnbU has a regulatory influence on pristinamycin production. EMSAs with culture extract samples from the snbU mutant did not influence the target binding ability of SpbR, PapR3, and PapR5 anymore, in contrast to culture supernatant samples from the S. pristinaespiralis wild-type or the pristinamycin deficient mutant papR2::apra, which demonstrates that SnbU is involved in the synthesis of the GBLR-interacting ligand.
| S-EPMC7554373 | biostudies-literature
Project description:Three genes encoding AfsK, AfsR, AfsS homologues in Streptomyces pristinaespiralis were studied, respectively, to investigate regulatory role of AfsKRS system for pristinamycin biosynthesis. Transcription change and gene inactivation analysis indicated that these genes had active transcription and positive regulation for the improvement of pristinamycin production in S. pristinaespiralis. The analysis of AfsKRS-defective mutagenesis indicated that there might be a positive correlation between the product of afsK and pristinamycin I biosynthesis, and a negative correlation to pristinamycin II biosynthesis. However, both afsR and afsS might have negative correlation to pristinamycin I production and positive correlation to pristinamycin II production. The effects on pristinamycin production of AfsKRS disruptants by protein kinase inhibitor K252a indicated that AfsR, both not AfsK and AfsS, was the inhibition target of K252a in S. pristinaespiralis, and AfsR should serve as a pleiotropic regulator to have differential regulation on biosynthesis of pristinamycin I and II components. Based on above study, it might be deduced that different signal transduction patterns via AfsK, AfsR, AfsS of AfsKRS system should be involved in respective regulation for biosynthesis of pristinamycin I and II in S. pristinaespiralis. In conclusion, the investigation could give some valuable clues for exploring furtherly regulatory function of AfsKRS system in S. pristinaespiralis.
| S-EPMC8382812 | biostudies-literature
Project description:Draft genome sequencing of Streptomyces sp. A012304, which produces an antibiotic alaremycin.
| PRJDB12995 | ENA
Project description:α-Glucuronidase from Streptomyces pristinaespiralis (SpGlcA115A) is composed of a single-chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 115, a novel family of hemicellulolytic α-glucuronidases. The enzyme catalyzes the hydrolysis of α-linked 4-O-methylglucuronosyl and glucuronosyl residues from both polymeric xylans and oligosaccharides. SpGlcA115A was crystallized at 293 K using the sitting-drop vapour-diffusion method. The crystals belonged to space group R3 and diffracted to a resolution of 1.9 Å.
| S-EPMC3079975 | biostudies-literature
Project description:Streptomyces pristinaespiralis strain:PR11 Genome sequencing
| PRJNA649107 | ENA
Project description:The terminal compartments of Streptomyces are less prone to transcription than the rest of the chromosome. Indeed, the expression of the highly variable regions enriched in those compartments is generally conditional and often requires an empirical approach to characterize the inducing conditions. For instance, in the context of identifying adequate antibiotic production conditions, an OSMAC (“One Strain Many Compounds”) approach is frequently implemented, based on strain cultivation in different environmental conditions (composition of the medium, growth time, temperature, co-cultures, etc.). Likewise, to find the expression conditions of a complete prophage of Streptomyces ambofaciens ATCC 23877 (named 'Samy' phage/prophage), we conducted a similar approach by analyzing the transcriptomes in five solid media (HT, SAF, ONA, MMM, MMM+NAG). The terminal compartments of Streptomyces are less prone to transcription than the rest of the chromosome. Indeed, the expression of the highly variable regions enriched in those compartments is generally conditional and often requires an empirical approach to characterize the inducing conditions. For instance, in the context of identifying adequate antibiotic production conditions, an OSMAC (“One Strain Many Compounds”) approach is frequently implemented, based on strain cultivation in different environmental conditions (composition of the medium, growth time, temperature, co-cultures, etc.). Likewise, to find the expression conditions of a complete prophage of Streptomyces ambofaciens ATCC 23877 (named 'Samy' phage/prophage), we conducted a similar approach by analyzing the transcriptomes in five solid media (HT, SAF, ONA, MMM, MMM+NAG).
2023-07-01 | GSE232795 | GEO