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By continuing to use the site, you are accepting our use of cookies. Read the ACS privacy policy. Recently Viewed. The jellyfish produces calcium, which interacts with aequorin and produces blue luminescence. This blue light is absorbed by GFP and re-emitted as green fluorescence. These proteins have been isolated and purified from the jellyfish and are used heavily in research to this day. The structure of the protein can be seen in Fig.
GFP is a barrel shape with the fluorescent portion the chromophore made up of just three amino acids. When this chromophore absorbs blue light, it emits green fluorescence. Some applications and advantages of GFP discussed below.
GFP as a toxicity marker : due to the fact that GFP decreases in fluorescence intensity with increasing toxicity, it can be used as a marker for environmental toxicity. GFP can be added to host organisms with no negative effect, and then the intensity tracked throughout different environments in various organisms.
GFP is heritable , if an organism has GFP knocked-in to its genome, GFP will naturally be passed onto offspring without any additional processes, allowing for non-invasive ways of introducing a fluorescent marker and tracking it across generations of animals or cells. GFP does not interfere with any biological processes.
Transgenic mice can be labeled with GFP, which is then easily observed in their offspring just by exposing them to blue or UV light, as seen in Fig. The team then looked at GFPs from a wide range of sources, including different jellyfish and plankton species, in the presence of benzoquinone and potassium ferricyanide.
All organisms experienced redding, apart from mutant versions of GFP that glow blue and cyan. The researchers also introduced the GFP gene into live mammalian cells grown in the lab, and found the redding process happened there too.
This suggests that scientists could use GFP to detect reduction and oxidation processes inside a cell, Lukyanov says. The team still doesn't know exactly what is happening during redding, but they managed to look in more detail at cytochrome c, and they think it involves the transfer of two electrons.
Two cyctochrome c molecules are reduced, or given an electron, for each GFP molecule that gets excited by light. They report their results in Nature Chemical Biology. Marc Zimmer, a computational chemist at Connecticut College in New London who works with GFP, thinks that Lukyanov has the best evidence yet for what GFP does in nature, and is impressed that the effect is so widespread.
However, the case is not closed: "What about all the other coloured fluorescent proteins? Lukyanov says that the latest work is a hypothesis, but he thinks that other biologists who use GFP as a tag should bear it in mind, because it might affect their experiments.
Bogdanov, A. Nature Chem. Download references. You can also search for this author in PubMed Google Scholar. Reprints and Permissions. Sanderson, K. Green glow deciphered. Nature Download citation.
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