| Aequorea macrodactyla | |
|---|---|
Scientific classification  | |
| Domain: | Eukaryota |
| Kingdom: | Animalia |
| Phylum: | Cnidaria |
| Class: | Hydrozoa |
| Order: | Leptothecata |
| Family: | Aequoreidae |
| Genus: | Aequorea |
| Species: | A. macrodactyla |
| Binomial name | |
| Aequorea macrodactyla (Brandt, 1835) | |
Aequorea macrodactyla is a species of hydrozoan in the family Aequoreidae. It was first described by Johann Friedrich von Brandt in 1835. [1]
It can have up to 150 tentacles and grow up to 25 cm. [2]
Bioluminescence is a common feature among marine organisms. The luminescent system of A. macrodactyla is similar to a related species, A. victoria, and consists of a 27-kDa green fluorescent protein and the aequorin complex which consists of a 22-kDa apoaequorin, the luminophore coelenterazine, and molecular oxygen. These proteins function together. As calcium binds to coelenterazine, (a bioluminescent molecule in sea life), the molecule oxidizes which results in the release of carbon dioxide and blue light. The blue light emitted from the aequorin activates GFP causing it to emit a green light. The difference between the two organisms is color; A. macrodactyla is brighter, and bolder in color. This is due to a difference in intron length in GFP. [3]
Fluorescence is the emission of light by a substance that has absorbed light or other electromagnetic radiation. It is a form of luminescence. In most cases, the emitted light has a longer wavelength, and therefore a lower photon energy, than the absorbed radiation. A perceptible example of fluorescence occurs when the absorbed radiation is in the ultraviolet region of the electromagnetic spectrum, while the emitted light is in the visible region; this gives the fluorescent substance a distinct color that can only be seen when the substance has been exposed to UV light. Fluorescent materials cease to glow nearly immediately when the radiation source stops, unlike phosphorescent materials, which continue to emit light for some time after.
The green fluorescent protein (GFP) is a protein that exhibits green fluorescence when exposed to light in the blue to ultraviolet range. The label GFP traditionally refers to the protein first isolated from the jellyfish Aequorea victoria and is sometimes called avGFP. However, GFPs have been found in other organisms including corals, sea anemones, zoanithids, copepods and lancelets.
Bioluminescence is the production and emission of light by living organisms. It is a form of chemiluminescence. Bioluminescence occurs widely in marine vertebrates and invertebrates, as well as in some fungi, microorganisms including some bioluminescent bacteria, and terrestrial arthropods such as fireflies. In some animals, the light is bacteriogenic, produced by symbiotic bacteria such as those from the genus Vibrio; in others, it is autogenic, produced by the animals themselves.
In molecular biology and biotechnology, a fluorescent tag, also known as a fluorescent label or fluorescent probe, is a molecule that is attached chemically to aid in the detection of a biomolecule such as a protein, antibody, or amino acid. Generally, fluorescent tagging, or labeling, uses a reactive derivative of a fluorescent molecule known as a fluorophore. The fluorophore selectively binds to a specific region or functional group on the target molecule and can be attached chemically or biologically. Various labeling techniques such as enzymatic labeling, protein labeling, and genetic labeling are widely utilized. Ethidium bromide, fluorescein and green fluorescent protein are common tags. The most commonly labelled molecules are antibodies, proteins, amino acids and peptides which are then used as specific probes for detection of a particular target.
Chemiluminescence is the emission of light (luminescence) as the result of a chemical reaction. There may also be limited emission of heat. Given reactants A and B, with an excited intermediate ◊,
Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein. The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. Both words are derived from the Latin word lucifer, meaning "lightbearer", which in turn is derived from the Latin words for "light" (lux) and "to bring or carry" (ferre).
Luciferin is a generic term for the light-emitting compound found in organisms that generate bioluminescence. Luciferins typically undergo an enzyme-catalyzed reaction with molecular oxygen. The resulting transformation, which usually involves breaking off a molecular fragment, produces an excited state intermediate that emits light upon decaying to its ground state. The term may refer to molecules that are substrates for both luciferases and photoproteins.
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 pGLO plasmid is an engineered plasmid used in biotechnology as a vector for creating genetically modified organisms. The plasmid contains several reporter genes, most notably the green fluorescent protein (GFP) and the ampicillin resistance gene. GFP was isolated from the jelly fish Aequorea victoria. Because it shares a bidirectional promoter with a gene for metabolizing arabinose, the GFP gene is expressed in the presence of arabinose, which makes the transgenic organism express its fluorescence under UV light. GFP can be induced in bacteria containing the pGLO plasmid by growing them on +arabinose plates. pGLO is made by Bio-Rad Laboratories.
Noctiluca scintillans is a marine species of dinoflagellate that can exist in a green or red form, depending on the pigmentation in its vacuoles. It can be found worldwide, but its geographical distribution varies depending on whether it is green or red. This unicellular microorganism is known for its ability to bioluminesce, giving the water a bright blue glow seen at night. However, blooms of this species can be responsible for environmental hazards, such as toxic red tides. They may also be an indicator of anthropogenic eutrophication.
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.
Biological pigments, also known simply as pigments or biochromes, are substances produced by living organisms that have a color resulting from selective color absorption. Biological pigments include plant pigments and flower pigments. Many biological structures, such as skin, eyes, feathers, fur and hair contain pigments such as melanin in specialized cells called chromatophores. In some species, pigments accrue over very long periods during an individual's lifespan.
Aequorea forskalea is a species of hydrozoan in the family Aequoreidae. Discovered in 1810 by Péron and Lesueur, A. forskalea was initially found in coastal to offshore waters of the Mediterranean Sea. This species is commonly referred to as the many-ribbed jellyfish. The species is often mixed up with some other members of the genus due to some similarities including the capability of bioluminescence.
In enzymology, an Oplophorus-luciferin 2-monooxygenase, also known as Oplophorus luciferase is a luciferase, an enzyme, from the deep-sea shrimp Oplophorus gracilirostris [2], belonging to a group of coelenterazine luciferases. Unlike other luciferases, it has a broader substrate specificity [3,4,6] and can also bind to bisdeoxycoelenterazine efficiently [3,4]. It is the third example of a luciferase to be purified in lab [2]. The systematic name of this enzyme class is Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating). This enzyme is also called Oplophorus luciferase.
Renilla-luciferin 2-monooxygenase, Renilla luciferase, or RLuc, is a bioluminescent enzyme found in Renilla reniformis, belonging to a group of coelenterazine luciferases. Of this group of enzymes, the luciferase from Renilla reniformis has been the most extensively studied, and due to its bioluminescence requiring only molecular oxygen, has a wide range of applications, with uses as a reporter gene probe in cell culture, in vivo imaging, and various other areas of biological research. Recently, chimeras of RLuc have been developed and demonstrated to be the brightest luminescent proteins to date, and have proved effective in both noninvasive single-cell and whole body imaging.
Bioreporters are intact, living microbial cells that have been genetically engineered to produce a measurable signal in response to a specific chemical or physical agent in their environment. Bioreporters contain two essential genetic elements, a promoter gene and a reporter gene. The promoter gene is turned on (transcribed) when the target agent is present in the cell’s environment. The promoter gene in a normal bacterial cell is linked to other genes that are then likewise transcribed and then translated into proteins that help the cell in either combating or adapting to the agent to which it has been exposed. In the case of a bioreporter, these genes, or portions thereof, have been removed and replaced with a reporter gene. Consequently, turning on the promoter gene now causes the reporter gene to be turned on. Activation of the reporter gene leads to production of reporter proteins that ultimately generate some type of a detectable signal. Therefore, the presence of a signal indicates that the bioreporter has sensed a particular target agent in its environment.
Douglas C. Prasher is an American molecular biologist. He is known for his work to clone and sequence the genes for the photoprotein aequorin and green fluorescent protein (GFP) and for his proposal to use GFP as a tracer molecule. He communicated his pioneering work to Martin Chalfie and Roger Y. Tsien, but by 1991 he was unable to obtain further research funding, and left academia. Eventually, he had to abandon science. Chalfie and Tsien were awarded the 2008 Nobel Prize in Chemistry for work that they publicly acknowledged was substantially based on Prasher's work; through their efforts and those of others, he returned to scientific research in June 2010.
Coelenterazine is a luciferin, a molecule that emits light after reaction with oxygen, found in many aquatic organisms across eight phyla. It is the substrate of many luciferases such as Renilla reniformis luciferase (Rluc), Gaussia luciferase (Gluc), and photoproteins, including aequorin, and obelin. All these proteins catalyze the oxidation of this substance, a reaction catalogued EC 1.13.12.5.
Photoproteins are a type of enzyme produced by bioluminescent organisms. They add to the function of the luciferins whose usual light-producing reaction is catalyzed by the enzyme luciferase.
Coelenteramide is the oxidized product, or oxyluciferin, of the bioluminescent reactions in many marine organisms that use coelenterazine. It was first isolated as a blue fluorescent protein from Aequorea victoria after the animals were stimulated to emit light. Under basic conditions, the compound will break down further into coelenteramine and 4-hydroxyphenylacetic acid.
 | This Leptothecata-related article is a stub. You can help Wikipedia by expanding it. |