User:Laura Carbone
From Proteopedia
Green fluorescent protein (GFP) is a bioluminescent polypeptide consisting of 238 residues isolated from the body of Aequorea victoria jellyfish (PDBsum, 2009). GFP converts the blue chemiluminescent of aequorin in the jellyfish into green fluorescent light (Yang, Moss, & Phillips, 1996; Phillips, 2007). In the laboratory, GFP can be incorporated into a variety of biological systems in order to function as a marker protein. Since its discovery in 1962, GFP has become a significant contributor to the research of monitoring gene expression, localization, mobility, traffic, interactions between various membrane and cytoplasmic proteins, as well as many others (Haldar & Chattopadhyay, 2009). Aequorea victoria was first discovered and investigated for its bioluminescence by Frank Johnson, who invited Osamu Shimonmura to work with him in on a small island not far from British Columbia, where the jellyfish is abundant (Shimonmura, 2009). Found off the west coast of the United States between British Columbia and central California (Cowles & Cowles, 2007), the jellyfish was considered a local phenomenon as it would drift in and out of the harbors (Shimonmura, 2009). Shimonmura was originally looking only to isolate the blue luminescent protein of Aequorea victoria, traditionally thought to be luciferase, but it would soon become apparent that the glow was in fact due to aequorin, a substance related, but slightly varying from luciferase (Shimonmura, 2009; Haldar & Chattopadhyay, 2009). However, the light emitted from aequorin still differed from the light emitted from the wild jellyfish. This quandary led to the discovery of the green fluorescent protein responsible for this disparity, but sufficient amounts of the protein could not be collected for study until 1979. The journey to discover the nature of GFP had begun (Shimonmura, 2009).
