{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Huang CT"],"funding":["Ministry of Science and Technology, Taiwan","Academia Sinica"],"pagination":["375-386"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10539794"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["2(1)"],"pubmed_abstract":["Trigger factor (TF) is a highly conserved multi-domain molecular chaperone that exerts its chaperone activity at the ribosomal tunnel exit from which newly synthesized nascent chains emerge. TF also displays promiscuous substrate binding for a large number of cytosolic proteins independent of ribosome binding. We asked how TF recognizes a variety of substrates while existing in a monomer-dimer equilibrium. Paramagnetic nuclear magnetic resonance (NMR) and electron spin resonance (ESR) spectroscopy were used to show that dimeric TF displays a high degree of structural polymorphism in solution. A series of peptides has been generated to quantify their TF binding affinities in relation with their sequence compositions. The results confirmed a previous predication that TF preferentially binds "],"journal":["Magnetic resonance (Gottingen, Germany)"],"pubmed_title":["Structural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone."],"pmcid":["PMC10539794"],"funding_grant_id":["102-2113-M-001-017-MY2","NA","100-2113-M-001-031-MY2"],"pubmed_authors":["Hsu SD","Lai YC","Chen SY","Huang CT","Ho MR","Chiang YW"],"additional_accession":[]},"is_claimable":false,"name":"Structural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone.","description":"Trigger factor (TF) is a highly conserved multi-domain molecular chaperone that exerts its chaperone activity at the ribosomal tunnel exit from which newly synthesized nascent chains emerge. TF also displays promiscuous substrate binding for a large number of cytosolic proteins independent of ribosome binding. We asked how TF recognizes a variety of substrates while existing in a monomer-dimer equilibrium. Paramagnetic nuclear magnetic resonance (NMR) and electron spin resonance (ESR) spectroscopy were used to show that dimeric TF displays a high degree of structural polymorphism in solution. A series of peptides has been generated to quantify their TF binding affinities in relation with their sequence compositions. The results confirmed a previous predication that TF preferentially binds ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021","modification":"2026-05-28T21:34:36.858Z","creation":"2025-04-20T01:32:10.578Z"},"accession":"S-EPMC10539794","cross_references":{"pubmed":["37904759"],"doi":["10.5194/mr-2-375-2021"]}}