Studying DNA-protein interactions with single-molecule Förster resonance energy transfer

Protoplasma. 2014 Mar;251(2):317-32. doi: 10.1007/s00709-013-0596-6. Epub 2013 Dec 28.

Abstract

Single-molecule Förster resonance energy transfer (smFRET) has emerged as a powerful tool for elucidating biological structure and mechanisms on the molecular level. Here, we focus on applications of smFRET to study interactions between DNA and enzymes such as DNA and RNA polymerases. SmFRET, used as a nanoscopic ruler, allows for the detection and precise characterisation of dynamic and rarely occurring events, which are otherwise averaged out in ensemble-based experiments. In this review, we will highlight some recent developments that provide new means of studying complex biological systems either by combining smFRET with force-based techniques or by using data obtained from smFRET experiments as constrains for computer-aided modelling.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • DNA / chemistry*
  • DNA / metabolism
  • Fluorescence Resonance Energy Transfer / instrumentation
  • Fluorescence Resonance Energy Transfer / methods*
  • Microscopy, Fluorescence / methods
  • Nanotechnology
  • Proteins / chemistry*
  • Proteins / metabolism

Substances

  • Proteins
  • DNA