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Dedicated chaperone at the ribosome safeguards the proteostasis network during eEF1A biogenesis

ABSTRACT: Dedicated chaperone at the ribosome safeguards the proteostasis network during eEF1A biogenesis

PROVIDER: PRJNA915314 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR22878229.fastq.gz	Fastqsanger.gz
	SRR22878230.fastq.gz	Fastqsanger.gz
	SRR22878231.fastq.gz	Fastqsanger.gz
	SRR22878232.fastq.gz	Fastqsanger.gz
	SRR22878233.fastq.gz	Fastqsanger.gz

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Dedicated chaperone at the ribosome safeguards the proteostasis network during eEF1A biogenesis

Project description:Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we find that the universal cotranslational machinery adapts to accommodate the challenging biogenesis of abundantly expressed eukaryotic translation elongation factor 1A (eEF1A). During eEF1A synthesis, chaperone Chp1 is recruited to the ribosome with the help of the nascent polypeptide-associated complex (NAC), where it safeguards eEF1A biogenesis. Aberrant eEF1A production triggers instant proteolysis, widespread protein aggregation, activation of Hsf1 stress transcription and compromises cellular fitness. The expression of pathogenic eEF1A2 variants linked to epileptic-dyskinetic encephalopathy is protected by Chp1. Thus, eEF1A is a difficult to fold protein that necessitates dedicated folding factor Chp1 at the ribosomal tunnel exit to protect the eukaryotic cell from proteostasis collapse.

2024-01-16 | GSE221651 | GEO

MS data for Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis

Project description:Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. It is not clear how this promiscuous mechanism ensure efficient production of challenging clients such as highly expressed proteins. Here we find that the biogenesis of the abundantly expressed eukaryotic translation elongation factor 1A (eEF1A) depends on the dedicated ribosome-associated chaperone Chp1.

2024-06-16 | PXD043391 | Pride

Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis.

Project description: Not available

| S-EPMC10869706 | biostudies-literature

PDCD2 functions as an evolutionarily conserved chaperone dedicated for the 40S ribosomal protein uS5

Project description:PDCD2 is an evolutionarily conserved protein that is essential for cell proliferation and embryonic development. To date, however, the function of PDCD2 underlying its fundamental cellular role has remained elusive. Here we used quantitative proteomics approaches to define the protein-protein interaction network of human PDCD2. Our data revealed that PDCD2 specifically interacts with the 40S ribosomal protein uS5 (RPS2) and that the PDCD2-uS5 complex is assembled co-translationally. Loss of PDCD2 expression leas to defects in the synthesis of small ribosomal subunit that phenocopies a uS5 deficiency. Notably, we showed that PDCD2 is important for the accumulation of soluble uS5 proteins as well as its incorporation into 40S ribosomal subunit. Our findings support that the essential molecular function of PDCD2 is to act as a dedicated chaperone that recognizes the ribosomal protein uS5 co-translationally in the cytoplasm and accompanies uS5 to ribosome assembly sites in the nucleolus. As most dedicated ribosomal protein chaperones have been identified in yeast, our study indicates that similar mechanisms exist in human cells to assist ribosomal proteins coordinate their folding, nuclear import, and assembly in pre-ribosomal particles.

2020-09-01 | GSE151094 | GEO

PDCD2 functions as an evolutionarily conserved chaperone dedicated for the 40S ribosomal protein uS5

Project description:PDCD2 functions as an evolutionarily conserved chaperone dedicated for the 40S ribosomal protein uS5

| PRJNA634665 | ENA

Expression data from Saccharomyces cerevisiae with eEF1A overexpression

Project description:The canonical role of eEF1A is to deliver the aminoacyl tRNA to the ribosome, we have used the yeast model system to investigate further roles for this protein. We used microarray to study the transcriptomic effects of elevated levels of eEF1A on yeast cells during log phase growth

2016-10-29 | GSE89286 | GEO

The zinc finger transcription factor PQM-1 is a mediator of transcellular chaperone signalling and novel regulator of proteostasis in C. elegans

Project description:The goal of this RNA-Seq analysis was to identify genes differentially expressed in a C. elegans strain overexpressing HSP-90 in the neurons compared to control (N2) animals. C. elegans overexpressing HSP-90 protein in the neurons activate transcellular chaperone signalling that enhances organismal proteostasis. This study aimed to identify components of the signalling pathway responsible for this effect.

2018-06-05 | GSE108005 | GEO

Ypl225w-3xFLAG IP-mass spectrometry

Project description:Eukaryotic translation elongation factor 1A (eEF1A) is a highly abundant, multi-domain GTPase. Post-translational steps essential for eEF1A biogenesis are carried out by bespoke chaperones but co-translational mechanisms tailored to eEF1A folding remain unexplored. Here, we find that the N-terminal, GTP-binding domain of eEF1A is prone to co-translational misfolding and using computational approaches, yeast genetics, and microscopy analysis, we identify the conserved yet uncharacterized yeast protein Ypl225w as a chaperone dedicated to solving this problem. Proteomics and biochemical reconstitution reveal that the Ypl225w-ribosomal eEF1A nascent chain interaction depends on additional binding of Ypl225w to the UBA domain of nascent polypeptide-associated complex (NAC). Lastly, we show by orthogonal chemical genetics that Ypl225w primes eEF1A nascent chains for their subsequent binding to GTP and release from Ypl225w. Our work establishes eEF1A as a model system for chaperone-dependent co-translational folding and unveils a novel mechanism for GTP-driven folding on the ribosome.

2025-02-05 | PXD058955 | Pride

The dual methyltransferase METTL13 targets N-terminus and Lys55 of eEF1A and regulates codon-specific translation rates

Project description:Eukaryotic elongation factor 1 alpha (eEF1A) delivers aminoacyl-tRNA to the ribosome and thereby plays a key role in protein synthesis. Human eEF1A is post-translationally methylated on several lysine residues as well as on the N-terminus and until recently the responsible methyltransferases were largely elusive. Using mass spectrometry based screens, gene targeted cells and in vitro enzymology we identify the human methyltransferase like proteins 13 (METTL13), which contains two distinct methyltransferase domains, as an enzyme catalyzing both dimethylation of Lys55 and trimethylation of the N-terminus of eEF1A. Moreover, through ribosome profiling we demonstrate that loss of METTL13 function alters translation dynamics and results in changed translation rate of specific codons. In line with the established descriptive nomenclature for this type of enzymes we suggest that METTL13 is redubbed eEF1A dual methyltransferase (eEF1A-DMT / EEF1ADMT).

2018-07-04 | GSE104033 | GEO

eEF1A peptide pull-down LC-MS/MS

Project description:Peptide pull-down using synthetic peptides corresponding to unmodified and methylated human eEF1A.

2018-07-04 | PXD008115 | Pride