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Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation I

ABSTRACT: Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation I

PROVIDER: PRJNA1007678 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25715233_1.fastq.gz	Fastqsanger.gz
	SRR25715233_2.fastq.gz	Fastqsanger.gz
	SRR25715234_1.fastq.gz	Fastqsanger.gz
	SRR25715234_2.fastq.gz	Fastqsanger.gz
	SRR25715235_1.fastq.gz	Fastqsanger.gz

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Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation

Project description:Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation

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Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation III

Project description:Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation III

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Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation II

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Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation III

Project description:How biomolecules condense to organize subcellular processes is of fundamental significance. Nitrogen-starved Escherichia coli form a single condensate, which we termed Bacterial Stress Body (BSB). Its formation is triggered by long polyphosphate chains, which scaffold the RNA chaperone Hfq into high molecular weight complexes with distinct sequence-specific RNA and DNA binding properties. We show that polyP is crucial for the stabilization of select RNAs, the sequestration of translation- and RNA metabolism-associated proteins that likely stall protein synthesis, and the specific nucleoid-associated localization of BSBs. Together, these functions ensure bacterial survival and recovery from N-starvation. Mammalian polyphosphate associates with P-bodies but not stress granules suggesting that polyphosphate’s interaction with select RNA binding proteins contributed to the evolution of functionally and compositionally distinct condensates in higher organisms.

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Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation II

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Bacterial Stress Bodies – Ancestral Condensates Regulating RNA Turnover and Protein Translation I

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Local Translation in Nuclear Condensate Amyloid-bodies

Project description:We report that solid-like condensates Amyloid-bodies are hubs of stress-resistant local nuclear translation in cells responding to high temperature. RNA-seq. analysis of purified Amyloid-bodies confirms that HSF1-transcribed mRNAs accumulate in these solid-like condensates during stress.

2021-01-15 | GSE164846 | GEO

HP-Bodies - Ancestral Condensates that Regulate RNA Turnover and Protein Translation in Bacteria.

Project description:Uncovering what drives select biomolecules to form phase-separated condensates in vivo and identifying their physiological significance are topics of fundamental importance. Here we show that nitrogen-starved Escherichia coli produce long-chain polyphosphates, which scaffold the RNA chaperone Hfq into phase-separating high molecular weight complexes together with components of the RNA translation and processing machinery. The presence of polyphosphate within these condensates, which we termed HP-bodies, controls Hfq function by selectively stabilizing polyadenylated RNAs involved in transcription and protein translation, and promoting interactions with translation- and RNA-metabolism-associated proteins involved in de novo protein synthesis. Lack of polyphosphate prevents HP-body formation, which increases cell death and significantly hinders recovery from N-starvation. In functional analogy, we demonstrate that polyP contributes specifically to the formation of Processing (P)-bodies in human cell lines, revealing that a single, highly conserved and ancestral polyanion serves as the universal scaffold for functional phase-separated condensate formation across the tree of life.

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RIP-Seq of An Integrated Signaling Network Controls P-Bodies Dynamics and mRNA Translation in Human Glioblastoma

Project description:Processing (P)-bodies are cytoplasmic membrane-less condensates including translationally repressed mRNAs and proteins involved in the mRNA decay machinery. The mechanisms underlying P-bodies nucleation and mRNA decay have been largely described. However, the impact of signaling networks in P-bodies dynamics and mRNA translation is still not well understood. Here, we identify a ribonucleoprotein network assembled by the E3 ubiquitin ligase Praja2 at P-bodies that coordinates protein translation and mRNA turnover in human glioblastoma (GBM). Praja2 physically interacts and spatially colocalizes with the RNA helicase DDX6, a core component and nucleating factor of P-bodies. Stimulation of the G protein-coupled receptor (GPCR)-cAMP pathway in GBM cells induces a non-proteolytic polyubiquitylation of DDX6 by Praja2. DDX6 ubiquitylation is required for P-bodies assembly and mRNA translation repression. Interfering with DDX6 ubiquitylation or downregulation of expression markedly affects P-bodies assembly. Moreover, genetic deletion of praja2 dramatically impacts the assembly of DDX6/mRNA complexes and the amount of translating polysomes, leading to cellular senescence and GBM growth arrest. These findings identify a cAMP-driven post-transcriptional control mechanism operating at P-bodies by the ubiquitin system that profoundly impacts on mRNA translation and cancer cell growth. This regulatory system may, thus, contribute to the adaptive metabolic rewiring underlying cancer growth and drug resistance.

2025-03-30 | E-MTAB-14331 | biostudies-arrayexpress

RNA-Seq of An Integrated Signaling Network Controls P-Bodies Dynamics and mRNA Translation in Human Glioblastoma

Project description:Processing (P)-bodies are cytoplasmic membrane-less condensates including translationally repressed mRNAs and proteins involved in the mRNA decay machinery. The mechanisms underlying P-bodies nucleation and mRNA decay have been largely described. However, the impact of signaling networks in P-bodies dynamics and mRNA translation is still not well understood. Here, we identify a ribonucleoprotein network assembled by the E3 ubiquitin ligase Praja2 at P-bodies that coordinates protein translation and mRNA turnover in human glioblastoma (GBM). Praja2 physically interacts and spaBally co-localizes with the RNA helicase DDX6, a core component and nucleating factor of P-bodies. Stimulation of the G protein-coupled receptor (GPCR)-cAMP pathway in GBM cells induces a non-proteolytic polyubiquitylation of DDX6 by Praja2. DDX6 ubiquitylation is required for P-bodies assembly and mRNA translation repression. Interfering with DDX6 ubiquitylation or downregulation of expression markedly affects P-bodies assembly. Moreover, geneBc deleBon of praja2 dramatically impacts the assembly of DDX6/mRNA complexes and the amount of translating polysomes, leading to cellular senescence and GBM growth arrest. These findings identify a cAMP-driven post-transcriptional control mechanism operating at P- bodies by the ubiquitin system that profoundly impacts on mRNA translation and cancer cell growth. This regulatory system may, thus, contribute to the adaptive metabolic rewiring underlying cancer growth and drug resistance.

2025-03-30 | E-MTAB-14326 | biostudies-arrayexpress

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