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Preservation of orphan ribosomal proteins during stress in chaperone-stirred condensates

ABSTRACT: Preservation of orphan ribosomal proteins during stress in chaperone-stirred condensates

PROVIDER: PRJNA994119 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25248672.fastq.gz	Fastqsanger.gz
	SRR25248673.fastq.gz	Fastqsanger.gz
	SRR25248674.fastq.gz	Fastqsanger.gz
	SRR25248675.fastq.gz	Fastqsanger.gz
	SRR25248676.fastq.gz	Fastqsanger.gz

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Preservation of orphan ribosomal proteins during stress in chaperone-stirred condensates

Project description:Ribosome biogenesis is among the most resource-intensive cellular processes, with ribosomal proteins accounting for up to half of all newly synthesized proteins in eukaryotic cells. During stress, cells shut down ribosome biogenesis in part by halting rRNA synthesis, potentially leading to massive accumulation of aggregation-prone “orphan” ribosomal proteins (oRPs). Here we show that during heat shock in yeast and human cells, oRPs accumulate as reversible condensates at the nucleolar periphery recognized by the Hsp70 co-chaperone Sis1/DnaJB6. oRP condensates are liquid-like in cell-free lysate but solidify upon depletion of Sis1 or inhibition of Hsp70. When cells recover from heat shock, oRP condensates disperse in a Sis1-dependent manner, and their ribosomal protein constituents are incorporated into functional ribosomes in the cytosol, enabling cells to efficiently resume growth.

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A chaperone-like function of FUS ensures TAZ condensates dynamics and transcriptional activation

Project description:The Hippo pathway plays important roles in organ development, tissue homeostasis, and tumor growth, and its downstream effector TAZ is a transcriptional coactivator that promotes target gene expression through the formation of biomolecular condensates. However, the mechanisms that regulate the biophysical properties of TAZ condensates to enable Hippo signaling are not well understood. Here, using chemical cross-linking combined with an unbiased proteomic approach, we show that FUS associates with TAZ condensates and exerts a chaperone-like effect to maintain their proper liquidity and robust- transcriptional activity. Mechanistically, the low complexity sequence domain of FUS targets the coiled-coil domain of TAZ in a phosphorylation-regulated manner, which ensures the liquidity and dynamicity of TAZ condensates. In cells lacking FUS, TAZ condensates transition into gel/solid-like assembles with immobilized TAZ, leading to reduced expression of target genes and inhibition of pro-tumorigenic activity. Thus, our findings identify a chaperone-like function of FUS in Hippo regulation and demonstrate that appropriate biophysical properties of transcriptional condensates are essential for gene activation.

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Project description:Molecular Chaperone RUVBL2 Activates Oncogenes by Modulation of Transcriptional Condensates [RNA-Seq]

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Project description:Molecular Chaperone RUVBL2 Activates Oncogenes by Modulation of Transcriptional Condensates [PRO-Seq]

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