Using FRET to monitor protein-induced DNA bending: the TBP-TATA complex as a model system. Journal Article uri icon

Overview

abstract

  • Proteins that bind to DNA can elicit changes in DNA conformation, such as bending and looping, which are important signals for later events such as transcription. TATA-binding protein (TBP) is one example of a protein that elicits a conformational change in DNA; TBP binds and sharply bends its recognition sequence, which is thought to facilitate the recruitment of other protein factors. Here we describe the use of fluorescence resonance energy transfer (FRET) to evaluate DNA bending using TBP as a model system. FRET is a useful technique to measure changes in DNA conformation due to protein binding because small changes in the distance between two fluorophores (2-10 nm) translate into large changes in energy transfer.

publication date

  • January 1, 2013

Full Author List

  • Blair RH; Goodrich JA; Kugel JF

Other Profiles

Additional Document Info

start page

  • 203

end page

  • 215

volume

  • 977