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Monitoring fluorescence resonance energy transfer (FRET) between GFP,,, fusions in lysates of the yeast Saccharomyces cerevisiae using the ,,, Varian,,, Cary Eclipse

Monitoring fluorescence resonance energy transfer (FRET) between GFP
fusions in lysates of the yeast Saccharomyces cerevisiae using the Varian
Cary Eclipse

Paul Gavin# and Mark Prescott#, Ph.D

Daren J. Fyfe, Ph.D*

# Department of Biochemistry and Molecular Biology, Monash University, Clayton campus Victoria 3800, Australia

* Technical assistance: Varian Australia Pty Ltd, Mulgrave, Victoria 3170, Australia E-mail: fluorescence@varianinc.com

Introduction

Fluorescence resonance energy transfer (FRET) is a non-destructive, spectroscopic approach that can be used to monitor the proximity and angular orientation of donor and acceptor fluorophores in living cells1. The resonant energy of an excited donor fluorophore (in this example blue fluorescent proteinBFP) is absorbed by an acceptor fluorophore (green fluorescent proteinGFP) providing that donor and acceptor are in close proximity (between 1080 ngstroms2) (Figure 1). Emission spectra of donor fluorophores must significantly overlap the absorption spectra of the acceptor, while overlap between respective absorption and emission spectra of donor and acceptor should be minimized 3 .

Due to the attractive attributes of GFP (previously described in fluorescence application note No. 5)4, the application of FRET to GFP and GFP variants has become a powerful tool to monitor interactions at the protein level, within an intact cell or organism. It is possible to use FRET to measure conformational changes in a molecule tagged with two GFP variants in response to the binding of ligands such as calcium1, or the interaction betw
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