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Cyclophilin A supports translation of intrinsically disordered proteins and affects haematopoietic stem cell ageing

ABSTRACT: Cyclophilin A supports translation of intrinsically disordered proteins and affects haematopoietic stem cell ageing

PROVIDER: PRJNA634795 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11839153_1.fastq.gz	Fastqsanger.gz
	SRR11839153_2.fastq.gz	Fastqsanger.gz
	SRR11839154_1.fastq.gz	Fastqsanger.gz
	SRR11839154_2.fastq.gz	Fastqsanger.gz
	SRR11839155_1.fastq.gz	Fastqsanger.gz

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Cyclophilin A supports translation of intrinsically disordered proteins and affects haematopoietic stem cell ageing.

Project description:Loss of protein function is a driving force of ageing. We have identified peptidyl-prolyl isomerase A (PPIA or cyclophilin A) as a dominant chaperone in haematopoietic stem and progenitor cells. Depletion of PPIA accelerates stem cell ageing. We found that proteins with intrinsically disordered regions (IDRs) are frequent PPIA substrates. IDRs facilitate interactions with other proteins or nucleic acids and can trigger liquid-liquid phase separation. Over 20% of PPIA substrates are involved in the formation of supramolecular membrane-less organelles. PPIA affects regulators of stress granules (PABPC1), P-bodies (DDX6) and nucleoli (NPM1) to promote phase separation and increase cellular stress resistance. Haematopoietic stem cell ageing is associated with a post-transcriptional decrease in PPIA expression and reduced translation of IDR-rich proteins. Here we link the chaperone PPIA to the synthesis of intrinsically disordered proteins, which indicates that impaired protein interaction networks and macromolecular condensation may be potential determinants of haematopoietic stem cell ageing.

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Cyclophilin A supports translation of intrinsically disordered proteins and affects haematopoietic stem cell ageing

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Project description:RNA granules are cellular condensates that contain RNAs and proteins. The mechanism that drive the recruitment of many mRNAs to RNA granules are not fully understood. Here we characterize the assembly and transcriptome of the germ (P) granules of C. elegans. We find that mRNAs are recruited into P granules by condensation with the intrinsically-disordered protein MEG-3. MEG-3 binds ~500 mRNAs in C. elegans embryos in a sequence-independent manner that favors mRNAs with low ribosome coverage. Translational stress causes additional mRNAs to localize to P granules and translational activation correlates with P granule exit for two mRNAs coding for germ cell fate regulators. MEG-3/RNA condensates assembled in vitro are gel-like and trap mRNAs in a non-dynamic state. Our observations reveal similarities between P granules and stress granules and identify gelation with intrinsically-disordered proteins as a sequence-independent mechanism to enrich low-translation mRNAs in RNA granules

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