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
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: email@example.com
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 betwPage: All 1 2 3 4 Related biology technology :1
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. Cytosolic expression of Green Fluorescent Protein (GFP) and its derivatives
in the yeast Saccharomyces cerevisiae: Detection in vivo using
the Varian Cary Eclipse11
. Saccharomyces cerevisiae
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