Aequorea victoria

Aequorea victoria, also sometimes called the crystal jelly, is a bioluminescent hydrozoan jellyfish, or hydromedusa, that is found off the west coast of North America. The species is best known as the source of aequorin (a photoprotein), and green fluorescent protein (GFP); two proteins involved in bioluminescence. Their discoverers, Osamu Shimomura and colleagues, won the 2008 Nobel Prize in Chemistry for their work on GFP. Almost entirely transparent and colorless, and sometimes difficult to resolve, Aequorea victoria possess a highly contractile mouth and manubrium at the center of up to 100 radial canals that extend to the bell margin. The bell margin is surrounded by uneven tentacles, up to 150 of them in fully-grown specimens. The tentacles possess nematocysts that aid in prey capture, although they have no effect on humans. Specimens larger than 3 cm usually possess gonads for sexual reproduction, which run most of the length of the radial canals and are visible in the photos in this article as whitish thickenings along the radial canals. The bell margin is ringed with the muscular velum, which is typical of hydromedusae, and aids in locomotion through muscular contraction of the bell. Larger specimens are frequently found with symbiotic hyperiid amphipods attached to the subumbrella, or even occasionally living inside the gut or radial canals. Aequorea victoria are found along the North American west coast of the Pacific Ocean from the Bering Sea to southern California. The medusa part of the life cycle is a pelagic organism, which is budded off a bottom-living polyp in late spring. The medusae can be found floating and swimming both nearshore and offshore in the eastern Pacific Ocean; this species is particularly common in Puget Sound. Aequorea species can be fairly difficult to tell apart, as the morphological features on which identifications are made are mostly the numbers of tentacles, numbers of radial canals, numbers of marginal statocysts, and size.

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Förster resonance energy transfer

Förster resonance energy transfer (FRET), fluorescence resonance energy transfer, resonance energy transfer (RET) or electronic energy transfer (EET) is a mechanism describing energy transfer between two light-sensitive molecules (chromophores). A donor chromophore, initially in its electronic excited state, may transfer energy to an acceptor chromophore through nonradiative dipole–dipole coupling. The efficiency of this energy transfer is inversely proportional to the sixth power of the distance between donor and acceptor, making FRET extremely sensitive to small changes in distance.

Aequorea victoria

Aequorin

Aequorin is a calcium-activated photoprotein isolated from the hydrozoan Aequorea victoria. Its bioluminescence was studied decades before the protein was isolated from the animal by Osamu Shimomura in 1962. In the animal, the protein occurs together with the green fluorescent protein to produce green light by resonant energy transfer, while aequorin by itself generates blue light. Discussions of "jellyfish DNA" that can make "glowing" animals often refer to transgenic animals that express the green fluorescent protein, not aequorin, although both originally derive from the same animal.

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