Detection of green fluorescence proteins in marine organisms
Researchers from Scripps Institution of Oceanography at the University of California at San Diego and the Salk Biological Research Institute have discovered a family of green fluorescent proteins (GFPs) in primitive marine animals, along with new evidence. about the role of these proteins.
GFPs have recently gained worldwide attention with the 2008 Nobel Prize in Chemistry for Roger Tsien, a scientist at the University of California in San Diego. GFPs, which are only present in luminous jellyfish, are now widely used in science, from radioactive markers used in biochemicals, to the dipstick used in environmental quality surveys. However, while the value of GFPs in biochemistry and biotechnology has been widely acknowledged, the abundance in the biological world as well as its role in nature has not been fully decoded.
The first knowledge was revealed when a team discovered an unprecedentedly large GFPs. This group includes Erin Bomati, Ph.D., who previously worked at Scripps Institute, Gerard Manning of Salk Institute and Dimitri Deheyn of Scripps Institute. They found 16 related forms of GFPs in bivalent - long, fish-like, nocturnal animals living in the sea, spending most of their lives digging in the sand. This finding is found in the body of Branchiostoma floridae, an amphibian species in Tampa, Fla. Details are available in BioMed Central (BMC) Evolutionary Biology.
The injections are the closest surviving invertebrate cousins of vertebrates, and bipolarism evolved much more than jellyfish. In the report, the researchers described that 1 6 newly discovered GFPs have very different light-emitting characteristics, some with very clear fluorescence, while others have little or no light.
'In addition to knowledge about the biochemical characteristics of GFPs, we know almost nothing about their biological function. The results of our research indicate that the function of GFPs is not only related to fluorescence, ' Deheyn said.
Fluorescence in amphibian species is only strong in certain mouth areas. The rest of the body has little or no fluorescence at all. The irregular distribution of fluorescence may be due to 16 bipolar GFPs having different fluorescence functions. (Photo: Scripps Institution of Oceanography at the University of California at San Diego)
Using a series of tools and gene analysis, including sequencing and cloning, researchers have found that some GFPs, especially those with less fluorescence, can Self-defense function as an antioxidant, works to protect the animal's body in case of illness or stress. This is the first evidence that proteins have a role other than fluorescence in the same organism.
'Maybe GFPs had light absorption and playback functions at first, but here we show that GFPs can also play an anti-oxidant role,' Deheyn said. 'This is the first time we have identified the different functions of the GFPs that coexist in one body.'
Deheyn said that GFPs seem to prevent oxygen radicals from harming the bipolar body, similar to the role of antioxidants taken in the human body.
Deheyn also said that these new findings help scientists understand the evolution of this protein in the animal world, while also providing new biological engineers and biotechnologists. discovered in this app. The colors and functions specified by these GFPs can also explain which components of the protein sequence are responsible for which functions, and help create new GFP probe types.
The research is supported by the Air Force Science Research Office.
References:
Erin K Bomati, Gerard Manning, Dimitri D Deheyn.Amphioxus encodes are the largest known family of green fluorescent proteins, which have been transformed into distinct functional classes.BMC Evolutionary Biology, 2009;9 (1): 77 DOI: 10.1186 / 1471-2148-9-77
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