{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Michael N"],"funding":["NSF | BIO | Division of Molecular and Cellular Biosciences (MCB)","NSF | National Science Foundation Graduate Research Fellowship Program (GRFP)","NIGMS NIH HHS"],"pagination":["e2509408122"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12646239"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["122(46)"],"pubmed_abstract":["Peptide release factor 2 (RF2) catalyzes the release of the nascent polypeptide chain from the bacterial ribosomal complex during translation termination and a subset of ribosome rescue pathways. Despite its critical role, the mechanisms that govern RF2 function and regulation remain elusive. Here, using single-molecule fluorescence resonance energy transfer, we characterize the conformational landscape that RF2 explores on the ribosomal complex and show that RF2 binding and dissociation from the ribosome follows a series of conformational rearrangements which depend on its ribosomal binding platform. We also show how further interactions with the ribosomal complex are necessary to properly position RF2 for polypeptide release. This work investigates not only the dynamics RF2 undergoes whi"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome."],"pmcid":["PMC12646239"],"funding_grant_id":["R35 GM153724","R01 GM137608","DGE-11-44155","MCB 0644262","R01 GM084288"],"pubmed_authors":["Huang BY","Michael N","Ray KK","Gonzalez RL","Kinz-Thompson CD"],"additional_accession":[]},"is_claimable":false,"name":"A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.","description":"Peptide release factor 2 (RF2) catalyzes the release of the nascent polypeptide chain from the bacterial ribosomal complex during translation termination and a subset of ribosome rescue pathways. Despite its critical role, the mechanisms that govern RF2 function and regulation remain elusive. Here, using single-molecule fluorescence resonance energy transfer, we characterize the conformational landscape that RF2 explores on the ribosomal complex and show that RF2 binding and dissociation from the ribosome follows a series of conformational rearrangements which depend on its ribosomal binding platform. We also show how further interactions with the ribosomal complex are necessary to properly position RF2 for polypeptide release. This work investigates not only the dynamics RF2 undergoes whi","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-06T20:05:55.923Z","creation":"2026-06-04T03:14:13.491Z"},"accession":"S-EPMC12646239","cross_references":{"pubmed":["41231940"],"doi":["10.1073/pnas.2509408122"]}}