title: Single-molecule FRET characterization of RNA remodeling induced by an antitermination protein.
abstract: Single-molecule Förster Resonance Energy Transfer (smFRET) is a useful technique to probe conformational changes within bio-macromolecules. Here, we introduce how to perform smFRET measurements in solution to investigate RNA remodeling and RNA-protein interactions. In particular, we focus on how the close-to-open transition of an antiterminator hairpin is influenced by the binding of the antitermination protein and the competition by oligonucleotides.
authors.affiliation: CNRS UMR5048, Centre de Biochimie Structurale, 29 rue de Navacelles, 34090, Montpellier, France.
authors.forename: Soraya
authors.initials: S
authors.lastname: Ait-Bara
authors.forename: Caroline
authors.initials: C
authors.lastname: Clerté
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Margeat
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D011485:Protein Binding; D012313:RNA / Q000737:chemistry* / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D016601:RNA-Binding Proteins; C064872:antiterminator proteins, Bacteria; D012313:RNA