||Bacteria Escherichia coli
||Sourjik V, Berg HC. Binding of the Escherichia coli response regulator CheY to its target measured in vivo by fluorescence resonance energy transfer. Proc Natl Acad Sci U S A. 2002 Oct 1 99(20):12669-74. abstract & p.12674 left column top paragraphPubMed ID12232047
||P.12669 left column bottom paragraph: "To learn more about the binding of CheY∼P to FliM and about the kinetics of the chemotactic response, [investigators] extended [their] recent analysis of phosphorylation-dependent interactions of CheY with CheZ (ref 9) and measured fluorescence resonance energy transfer (FRET) between cyan fluorescent protein (CFP) fused to the N terminus of FliM (CFP-FliM) and yellow fluorescent protein (YFP) fused to the C terminus of CheY (CheY-YFP). The FRET technique relies on the distance-dependent transfer of energy from an excited donor fluorophore (CFP) to an acceptor fluorophore (YFP) and allows one to monitor changes in protein interactions in real time in vivo (refs 10, 11)."
||Abstract: "Following sudden addition of attractant, the amount of CheY approximately P bound to FliM decayed exponentially with a rate constant of about 2 s^(-1)." p.12674 left column top paragraph: "To match the rate constant of decay in FliM occupancy observed on addition of attractant (≈2 s^-1 Fig. 5B), [investigators] had to set the concentration of CheZ in the cytoplasm to 1.1µM."