Streptomyces hygroscopicus subsp. hygroscopicus
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA323631 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| BCAN01.dat.gz | Other | |||
| BCAN01.fasta.gz | Fasta.gz | |||
| BCAN01.master.dat | Other | |||
| MDFG01.dat.gz | Other |
Items per page: 5 1 - 5 of 7 |
Similar Datasets
Project description:Streptomyces endus overview
| PRJNA319125 | ENA
Project description:Here, we report the draft genome sequence of strain NBRC 16556, deposited as Streptomyces hygroscopicus subsp. hygroscopicus into the NBRC culture collection. An average nucleotide identity analysis confirmed that the taxonomic identification is correct. The genome sequence will serve as a valuable reference for genome mining to search new secondary metabolites.
| S-EPMC4889001 | biostudies-literature
Project description:Streptomyces hygroscopicus overview
| PRJNA37181 | ENA
Project description:The RNA sequencing approach was utilized to carry out a comparative transcriptome analysis between Streptomyces hygroscopicus 5008 wild-type and a genetically engineered strain. The A-factor-like cascade play an important role in the regulation of validamycin biosynthesis by Streptomyces hygroscopicus 5008, and the pleiotropic regulator AdpA-H may positively regulate the transcription of gene cluster for the biosynthesis. shbR1 and shbR3 as the A-factor receptor homolog genes, could repress the transcription of AdpA-H. By tandem deletions of these genes, the production and productivity of validamcyin was significantly enhanced. To explore the effects of the shbR1/R3 double deletion of the overall cellular metabolism, the RNA sequencing approach was utilized to carry out a comparative transcriptome analysis between wild-type and shbR1/shbR3 double mutant (genetically engineered strain).
2014-05-31 | GSE58115 | GEO
Project description:Malaria is one of the life-threatening diseases in the world. The spread of resistance to antimalarial drugs is a major challenge, and resistance to artemisinin has been reported in the Southeast Asian region. In the previous study, the active compound of Streptomyces hygroscopicus subsp. Hygroscopicus (S. hygroscopicus), eponemycin, has been shown to have antimalarial effects. To further analyze the effects of other active compounds on the Plasmodium parasite, identifying and analyzing the effectiveness of compounds contained in S. hygroscopicus through instrumentation of liquid chromatography/mass spectrometry (LC/MS) and in silico studies were very useful. This study aimed at identifying other derivative compounds from S. hygroscopicus and screening the antimalarial activity of the compound by assessing the binding affinity, pharmacokinetic profile, and bond interaction. The derivative compounds were identified using LC/MS. Protein targets for derivative compounds were found through literature studies, and the results of identification of compounds and protein targets were reconstructed into three-dimensional models. Prediction of pharmacokinetic profiles was carried out using Swiss ADME. Screening of protein targets for the derivative compound was carried out using the reverse molecular docking method. Analyzing bond interaction was done by LigPlot. One compound from S. hygroscopicus, i.e., 6,7-dinitro-2-[1, 2, 4]triazole-4-yl-benzo[de]isoquinoline-1,3-dione, was successfully identified using LC/MS. This compound was an isoquinoline derivative compound. Through literature studies with inclusion criteria, thirteen protein targets were obtained for reverse molecular docking. This isoquinoline derivative had the potential to bind to each protein target. The pharmacokinetic profile showed that this compound had the drug-likeness criteria. Conclusion. 6,7-Dinitro-2-[1, 2, 4]triazole-4-yl-benzo[de]isoquinoline-1,3-dione has antimalarial activity as shown by reverse molecular docking studies and pharmacokinetic profiles. The best inhibitory ability of compounds based on bond affinity is with adenylosuccinate synthetase.
| S-EPMC6973190 | biostudies-literature
Project description:The RNA sequencing approach was utilized to carry out a comparative transcriptome analysis between Streptomyces hygroscopicus 5008 wild-type and a genetically engineered strain. The A-factor-like cascade play an important role in the regulation of validamycin biosynthesis by Streptomyces hygroscopicus 5008, and the pleiotropic regulator AdpA-H may positively regulate the transcription of gene cluster for the biosynthesis. shbR1 and shbR3 as the A-factor receptor homolog genes, could repress the transcription of AdpA-H. By tandem deletions of these genes, the production and productivity of validamcyin was significantly enhanced. To explore the effects of the shbR1/R3 double deletion of the overall cellular metabolism, the RNA sequencing approach was utilized to carry out a comparative transcriptome analysis between wild-type and shbR1/shbR3 double mutant (genetically engineered strain). The trancriptome analysis between 5008 and DM98 was carried out respectively.
2014-05-31 | E-GEOD-58115 | biostudies-arrayexpress
Project description:A gene cluster responsible for the biosynthesis of validamycin, an aminocyclitol antibiotic widely used as a control agent for sheath blight disease of rice plants, was identified from Streptomyces hygroscopicus subsp. jinggangensis 5008 using heterologous probe acbC, a gene involved in the cyclization of D-sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone of the acarbose biosynthetic gene cluster originated from Actinoplanes sp. strain SE50/110. Deletion of a 30-kb DNA fragment from this cluster in the chromosome resulted in loss of validamycin production, confirming a direct involvement of the gene cluster in the biosynthesis of this important plant protectant. A sequenced 6-kb fragment contained valA (an acbC homologue encoding a putative cyclase) as well as two additional complete open reading frames (valB and valC, encoding a putative adenyltransferase and a kinase, respectively), which are organized as an operon. The function of ValA was genetically demonstrated to be essential for validamycin production and biochemically shown to be responsible specifically for the cyclization of D-sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in vitro using the ValA protein heterologously overexpressed in E. coli. The information obtained should pave the way for further detailed analysis of the complete biosynthetic pathway, which would lead to a complete understanding of validamycin biosynthesis.
| S-EPMC1214664 | biostudies-literature
Project description:Streptomyces endus NBRC 12859 genome sequencing project
| PRJDB3203 | ENA
Project description:Streptomyces sporocinereus NBRC 100766 genome sequencing project
| PRJDB3204 | ENA
Project description:Streptomyces sporocinereus OsiSh-2 Genome sequencing and assembly
| PRJNA318960 | ENA