APPLICATION OF A CHIMERIC GREEN FLUORESCENT PROTEIN TO STUDY PROTEIN-PROTEIN INTERACTIONS

The green fluorescent protein (GFP) of the jellyfish Aequorea victoria is an emerging tool to monitor gene expression in situ and in vivo. B ecause of its fluorescence properties, when GFP is fused in-frame to a specific protein of interest, various aspects of the behavior of this protein can be analyzed noninvasively. Here we describe a fusion betw een GFP and human calmodulin-like protein (CLP) and show that this pro tein retains fluorescence and known characteristics of CLP, including Ca2+-dependent interaction with phenyl-Sepharose(R) and interaction wi th a specific cellular target protein. The results suggest a novel app lication for GFP fusion proteins in the rapid, nonradioactive detectio n of interacting proteins on gel overlays.