{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sabbarini IM"],"funding":["National Science Foundation (NSF)","U.S. Department of Health & Human Services | National Institutes of Health (NIH)","U.S. Department of Health & Human Services | National Institutes of Health","NIGMS NIH HHS","National Science Foundation"],"pagination":["1277"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11790920"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["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 use AlphaPulldown to identify Ypl225w (also known as Chp1, Chaperone 1 for eEF1A) as a conserved yeast protein predicted to stabilize the N-terminal, GTP-binding (G) domain of eEF1A against its misfolding propensity, as predicted by computational simulations and validated by microscopy analysis of ypl225wΔ cells. Proteomics and biochemical reconstitution reveal that Ypl225w functions as a co-translational chaperone by forming dual interactions with the eEF1A G domain nascent chain and the UBA domain of ribosome-bound na"],"journal":["Nature communications"],"pubmed_title":["A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A."],"pmcid":["PMC11790920"],"funding_grant_id":["DGE1745303","R35 GM127136","R35 GM139571","R35-GM139571"],"pubmed_authors":["McQuown AJ","Park K","Nelliat AR","Reif D","Trejtnar C","Shakhnovich EI","Murray AW","Sabbarini IM","Dotsch V","Denic V"],"additional_accession":[]},"is_claimable":false,"name":"A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A.","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 use AlphaPulldown to identify Ypl225w (also known as Chp1, Chaperone 1 for eEF1A) as a conserved yeast protein predicted to stabilize the N-terminal, GTP-binding (G) domain of eEF1A against its misfolding propensity, as predicted by computational simulations and validated by microscopy analysis of ypl225wΔ cells. Proteomics and biochemical reconstitution reveal that Ypl225w functions as a co-translational chaperone by forming dual interactions with the eEF1A G domain nascent chain and the UBA domain of ribosome-bound na","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-06-01T10:38:15.511Z","creation":"2025-04-04T00:56:02.793Z"},"accession":"S-EPMC11790920","cross_references":{"pubmed":["39900909"],"doi":["10.1038/s41467-025-56489-3"]}}