Single-molecule FRET characterization of RNA remodeling induced by an antitermination protein

Methods Mol Biol. 2015:1259:349-68. doi: 10.1007/978-1-4939-2214-7_21.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism*
  • Fluorescence Resonance Energy Transfer / methods*
  • Protein Binding
  • RNA / chemistry*
  • RNA / metabolism*
  • RNA-Binding Proteins / metabolism*

Substances

  • Bacterial Proteins
  • RNA-Binding Proteins
  • antiterminator proteins, Bacteria
  • RNA