![]() ![]() While the use of fluorescent proteins was once limited to the green fluorescent protein ( GFP), in recent years many other fluorescent proteins have been cloned. Like other fluorescent proteins, Eos can be used to report diverse signals in cells, tissues and organs without disturbing complex biological machinery. Īccording to single-molecule fluorescence spectroscopy, EosFP is tetrameric, and exhibits strong Forster resonance coupling within individual fluorophores. ![]() Formation of the red chromophore involves cleaving the peptide backbone but includes almost no other changes in the protein structure. This mechanism allows for localized tagging of the protein and makes EosFP an appropriate tool for tracking protein movement within living cells. This modification occurs due to a break in the peptide backbone next to the chromophore. Function ĮosFP emits a strong green fluorescence (516 nm) that changes irreversibly to red (581 nm) when irradiated with UV-light of 390 nm. The two fluorescent forms of mEosFP (green and red) are compatible with CFP, GFP, YFP and RFP for multicolour labelling. ![]() They can also be used for the understanding of spatial/ temporal interactions between organelles and vesicles. mEos fusion proteins allow for differential colour labelling in single cells, or groups of cells in developing organs. Since their discovery, monomeric Eos probes (mEos) have been shown to localize in the cytosol, plasma membrane, endosomes, prevacuolar vesicles, vacuoles, the endoplasmic reticulum, golgi bodies, peroxisomes, mitochondria, invaginations, filamentous actin and cortical microtubules. These variants have been successful in the tracking of cellular components without disturbing function in the host cell and maintain the same photophysical properties as wild-type Eos. Unlike the tetrameric fluorescent proteins derived from anthozoan coral, which can interfere with normal cellular function due to interactions between protein subunits, EosFP has been broken up into dimeric and monomeric variants through the introduction of single point mutations. Eos was named after the Greek goddess of dawn. It has since been successfully cloned in Escherichia coli and fusion constructs have been developed for use in human cells. The stony coral, Lobophyllia hemprichii, from which EosFP was discovered.ĮosFP was first discovered in 2005 during a large scale screen for PAFPs (photoactivatable fluorescent proteins) within the stony coral Lobophyllia hemprichii. ![]()
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