Protein-Chromophore Interactions in Green Fluorescent Protein (GFP) Studied by Split Protein Reconstitution

Chromophore formation in green fluorescent protein.

The green fluorescent protein (GFP) from the jellyfish Aequorea Victoria forms an intrinsic chromophore through cyclization and oxidation of an internal tripeptide motif [Prasher, D. C., et al. (1992) Gene 111, 229-233; Cody, C. E., et al. (1993) Biochemistry 32, 1212-1218]. We monitored the formation of the chromophore in vitro using the S65T-GFP chromophore mutant. S65T-GFP recovered from inc...

Endogenous green fluorescent protein (GFP) in amphioxus.

Discovery of Green Fluorescent Protein, Gfp

I discovered the green fluorescent protein GFP from the jellyfish Aequorea aequorea in 1961 as a byproduct of the Ca-sensitive photoprotein aequorin (Shimomura et al., 1962; Johnson et al., 1962), and identified its chromophore in 1979 (Shimomura, 1979). GFP was a beautiful protein but it remained useless for the next 30 years after the discovery. My story begins in 1945, the year the city of N...

Detection of Homotypic Protein Interactions with Green Fluorescent Protein Proximity Imaging (GFP-PRIM)

Green fluorescent protein (GFP) is a true workhorse of modern cellular biology. GFP and its spectral mutants have been used primarily as passive fluorescent markers to monitor the location of tagged polypeptides within living cells and organisms. A relatively recent but important trend has been the development of GFP-based active indicators of cellular processes and microenvironments (Tsien 199...

Green fluorescent protein chimeras to probe protein-protein interactions.