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The genome of Streptomyces rimosus shows a novel structure compared to other Streptomyces

ABSTRACT: The genome of Streptomyces rimosus shows a novel structure compared to other Streptomyces

PROVIDER: PRJNA108673 | ENA |

REPOSITORIES: ENA

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The genome of Streptomyces rimosus shows a novel structure compared to other Streptomyces

Project description:This study compared the genome of Streptomyces rimosus rimosus against that of Streptomyces coelicolor. It also compared 4 strains with changes in oxytetracycline production and derived from G7, the type strain, against G7. Keywords: Comparative genomic hybridization

2008-01-11 | GSE10126 | GEO

The genome of Streptomyces rimosus shows a novel structure compared to other Streptomyces

2010-05-26 | E-GEOD-10126 | biostudies-arrayexpress

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Streptomyces rimosus subsp. rimosus ATCC 10970

Project description:Streptomyces rimosus subsp. rimosus ATCC 10970 Genome sequencing

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Streptomyces rimosus subsp. rimosus strain:DV3

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Streptomyces rimosus subsp. rimosus strain:HP126

Project description:Streptomyces rimosus subsp. rimosus HP126 Genome sequencing and assembly

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Streptomyces rimosus subsp. rimosus strain:R7

Project description:Streptomyces rimosus subsp. rimosus ATCC 10970 Genome sequencing and assembly

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Phosphoproteome dynamics of Streptomyces rimosus during submerged growth and antibiotic production

Project description:Streptomyces rimosus is an industrial streptomycete, best known as a producer of oxytetracycline, one of the most widely used antibiotics. Despite the significant contribution of Streptomyces species to the pharmaceutical industry, most omics analyses have only been conducted on the model organism, Streptomyces coelicolor. In recent years, protein phosphorylation on serine, threonine and tyrosine (Ser/Thr/Tyr) has been shown to play a crucial role in the regulation of numerous cellular processes, including metabolic changes leading to antibiotic production and morphological changes. In this study, we performed a comprehensive quantitative (phospho)proteomic analysis during the growth of S. rimosus under conditions of oxytetracycline production and pellet fragmentation. LC-MS/MS analysis combined with phosphopeptide enrichment detected a total of 3,725 proteins, corresponding to 45.6% of the proteome and 417 phosphorylation sites from 230 phosphoproteins. Significant changes in abundance during three distinct growth phases were determined for 494 proteins and 98 phosphorylation sites. Functional analysis revealed changes in phosphorylation events of proteins involved in important cellular processes, including regulatory mechanisms, primary and secondary metabolism, cell division and stress response. About 80% of the phosphoproteins detected during submerged growth of S. rimosus have not yet been reported in streptomycetes, and 55 phosphoproteins were not reported in any prokaryote studied so far. This enabled the creation of a unique resource that provides novel insights into the dynamics of (phospho)proteins and reveals many potential regulatory events during antibiotic production in liquid culture of an industrially-important bacterium.

2022-08-22 | PXD034565 | Pride

Streptomyces rimosus R6-500

Project description:Streptomyces rimosus R6-500 Genome sequencing

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