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L-bodies are novel RNA-protein condensates driving RNA transport in Xenopus oocytes

ABSTRACT: L-bodies are novel RNA-protein condensates driving RNA transport in Xenopus oocytes

PROVIDER: PRJNA664513 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12676663_1.fastq.gz	Fastqsanger.gz
	SRR12676663_2.fastq.gz	Fastqsanger.gz
	SRR12676664_1.fastq.gz	Fastqsanger.gz
	SRR12676664_2.fastq.gz	Fastqsanger.gz
	SRR12676665_1.fastq.gz	Fastqsanger.gz

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L-bodies are novel RNA-protein condensates driving RNA transport in Xenopus oocytes

Project description:RNP granules are membrane-less compartments within cells, formed by phase separation, that function as regulatory hubs for diverse biological processes. However, the mechanisms by which RNAs and proteins interact to promote RNP granule assembly and function in vivo remain unclear. In Xenopus laevis oocytes, maternal mRNAs are transported as large RNPs to the vegetal hemisphere of the developing oocyte, where local translation is critical for proper embryonic patterning. Here, we demonstrate that vegetal transport RNPs represent a new class of cytoplasmic RNP granule, termed Localization-bodies (L-bodies). We show that L-bodies are multiphase RNP granules, containing a dynamic liquid-like protein-containing phase surrounding a non-dynamic RNA-containing substructure. Our results support a role for RNA as a critical scaffold component within these RNP granules and suggest that cis-elements within localized mRNAs may drive subcellular RNA localization through control over phase behavior.

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L-Bodies are Novel RNA-Protein Condensates Driving RNA Transport in Xenopus Oocytes

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L-bodies are RNA-protein condensates driving RNA localization in <i>Xenopus</i> oocytes.

Project description:Ribonucleoprotein (RNP) granules are membraneless compartments within cells, formed by phase separation, that function as regulatory hubs for diverse biological processes. However, the mechanisms by which RNAs and proteins interact to promote RNP granule structure and function in vivo remain unclear. In Xenopus laevis oocytes, maternal mRNAs are localized as large RNPs to the vegetal hemisphere of the developing oocyte, where local translation is critical for proper embryonic patterning. Here we demonstrate that RNPs containing vegetally localized RNAs represent a new class of cytoplasmic RNP granule, termed localization-bodies (L-bodies). We show that L-bodies contain a dynamic protein-containing phase surrounding a nondynamic RNA-containing phase. Our results support a role for RNA as a critical component within these RNP granules and suggest that cis-elements within localized mRNAs may drive subcellular RNA localization through control over phase behavior.

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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: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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