The Vivid History of GFP
|If you work with fluorescent images, you have probably used GFP or one of its variants at some point in your career. If you haven't, well… you will. And if you don't, your paper will be rejected by all journals (be prepared!). OK, I exaggerate, but a lot of people use GFP in their applications. Thanks to its diverse applications and the innovation it brought to the biomedical field in general, GFP was the focus of special attention in 2008. That year, the Nobel prize in Chemistry was awarded to Professor Emeritus Osamu Shimomura of Boston University School of Medicine, Professor Martin Chalfie of Columbia University, and local Professor Roger Tsien at UC San Diego, for "the discovery and development of the green fluorescent protein, GFP".||
Structure of GFP (chromophore in green)
|So what is GFP? The Green Fluorescent Protein is a 238 amino acid protein and, like other fluorescent molecules, it absorbs energy and emits a fraction of that energy. In the early 1960s, research began on this byproduct of the first photoprotein discovered, Aequorin. Aequorin is a protein isolated from the Aequorea victoria jellyfish. It was finally named GFP in 1971. Following many years of research, Dr. Shimomura described the nature of the fluorochrome in GFP as part of the protein, opening the possibility of cloning the whole molecule, preserving the fluorescent function.|
Aequorea victoria jellyfish
|GFP displayed its exciting potential after it was shown that it could be expressed and function in other organisms. Complete stardom came with further modifications that greatly improved its excitation/emission properties, making it one of the most useful tools in biomedical research. These two technological applications were mastered by Chalfie and Tsien. However, this would have never been possible without the critical contribution of Dr. Douglas Prasher. Prasher was the first person to actually clone the GFP gene.|
|The diversity of fluorescent proteins is illustrated with living bacteria expressing several colors of fluorescent proteins (GFP, BFP, mTFP1, Emerald, Citrine, mOrange, mApple, mCherry, mGrape, and dsRed). Image taken by Paul Steinbach and Roger Tsien.|
|Back when he was cloning the GFP protein, Prasher had a tiny lab with an extremely limited budget. Despite the enormous potential of GFP, Prasher was unable to obtain further funding and tenure. Realizing he wouldn't be able to follow up on the GFP research, he passed a plasmid containing GFP to Chalfie. After some years, Prasher ended up working in a NASA-funded project. Unfortunately for him, this project would also run out of funding. Struggling to find a position in science, Prasher ended up working as a courtesy shuttle driver for a Toyota dealer. You read right…driver.|
|Wanted: Courtesy Van Driver
Ace Ventura 2: When Nature Calls, Warner Bros. Pictures.
|Prasher is a vivid example of the tournament market model in science, in which an excess of talented, qualified people compete for a few positions and tight budgets. With this model, a myriad of bright scientists choose (or are forced) to follow other avenues, parallel or completely divergent from science. However, your education, training to think, and other academia-acquired skills is what shape you as a human being. Intellectually, Prasher never quit science (you may think science quit on him…) and, although it wasn't a smooth process, he kept on applying for science related positions. Talent is always useful, so Prasher is now a Research Scientist in Roger Tsien's lab at the University of California, San Diego.||
Julian Voss-Andreae's GFP-based sculpture Steel Jellyfish (2006). The image shows the stainless-steel sculpture at Friday Harbor Laboratories on San Juan Island (Wash., USA), the place of GFP's discovery.
If you still want a piece of GFP on your own you can get green glowing fish at: https://www.glofish.com. Somehow fishes seem to be less controversial than rabbits…
|Alba is an albino rabbit that expresses GFP. It was created by contemporary artist Eduardo Kac in collaboration with a French laboratory. It sparked great controversy back in 2000, after an article was published by the Boston Globe (https://ekac.org/bostong.html)|
|Comments or questions? Just email me at email@example.com|