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A hemeprotein, or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both.
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.
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.
A fluorophore is a fluorescent chemical compound that can re-emit light upon light excitation. Fluorophores typically contain several combined aromatic groups, or planar or cyclic molecules with several π bonds.
Phytochromes are a class of photoreceptor proteins found in plants, bacteria and fungi. They respond to light in the red and far-red regions of the visible spectrum and can be classed as either Type I, which are activated by far-red light, or Type II that are activated by red light. Recent advances have suggested that phytochromes also act as temperature sensors, as warmer temperatures enhance their de-activation. All of these factors contribute to the plant's ability to germinate.
In developmental biology, photomorphogenesis is light-mediated development, where plant growth patterns respond to the light spectrum. This is a completely separate process from photosynthesis where light is used as a source of energy. Phytochromes, cryptochromes, and phototropins are photochromic sensory receptors that restrict the photomorphogenic effect of light to the UV-A, UV-B, blue, and red portions of the electromagnetic spectrum.
Biliverdin is a green tetrapyrrolic bile pigment, and is a product of heme catabolism. It is the pigment responsible for a greenish color sometimes seen in bruises.
Yellow fluorescent protein (YFP) is a genetic mutant of green fluorescent protein (GFP) originally derived from the jellyfish Aequorea victoria. Its excitation peak is 513 nm and its emission peak is 527 nm. Like the parent GFP, YFP is a useful tool in cell and molecular biology because the excitation and emission peaks of YFP are distinguishable from GFP which allows for the study of multiple processes/proteins within the same experiment.
Photoreceptor proteins are light-sensitive proteins involved in the sensing and response to light in a variety of organisms. Some examples are rhodopsin in the photoreceptor cells of the vertebrate retina, phytochrome in plants, and bacteriorhodopsin and bacteriophytochromes in some bacteria. They mediate light responses as varied as visual perception, phototropism and phototaxis, as well as responses to light-dark cycles such as circadian rhythm and other photoperiodisms including control of flowering times in plants and mating seasons in animals.
Roger Yonchien Tsien was an American biochemist. He was a professor of chemistry and biochemistry at the University of California, San Diego and was awarded the Nobel Prize in Chemistry in 2008 for his discovery and development of the green fluorescent protein, in collaboration with organic chemist Osamu Shimomura and neurobiologist Martin Chalfie. Tsien was also a pioneer of calcium imaging.
EosFP is a photoactivatable green to red fluorescent protein. Its green fluorescence (516 nm) switches to red (581 nm) upon UV irradiation of ~390 nm due to a photo-induced modification resulting from a break in the peptide backbone near the chromophore. Eos was first discovered as a tetrameric protein in the stony coral Lobophyllia hemprichii. Like other fluorescent proteins, Eos allows for applications such as the tracking of fusion proteins, multicolour labelling and tracking of cell movement. Several variants of Eos have been engineered for use in specific study systems including mEos2, mEos4 and CaMPARI.
mCherry is a member of the mFruits family of monomeric red fluorescent proteins (mRFPs). As an RFP, mCherry was derived from DsRed of Discosoma sea anemones, unlike green fluorescent proteins (GFPs) which are often derived from Aequorea victoria jellyfish. Fluorescent proteins are used to tag components in cells so that they can be studied using fluorescence spectroscopy and fluorescence microscopy. mCherry absorbs light between 540 and 590 nm and emits light in the range of 550-650 nm. mCherry belongs to the group of fluorescent protein chromophores used as instruments to visualize genes and analyze their functions in experiments. Genome editing has been improved greatly through the precise insertion of these fluorescent protein tags into the genetic material of many diverse organisms. Most comparisons between the brightness and photostability of different fluorescent proteins have been made in vitro, removed from biological variables that affect protein performance in cells or organisms. It is hard to perfectly simulate cellular environments in vitro, and the difference in environment could have an effect on the brightness and photostability.
Dronpa is a reversibly switchable photoactivatable fluorescent protein that is 2.5 times as bright as EGFP. Dronpa gets switched off by strong illumination with 488 nm (blue) light and this can be reversed by weak 405 nm UV light. A single dronpa molecule can be switched on and off over 100 times. It has an excitation peak at 503 nm and an emission peak at 518 nm.
A Light-oxygen-voltage-sensing domain is a protein sensor used by a large variety of higher plants, microalgae, fungi and bacteria to sense environmental conditions. In higher plants, they are used to control phototropism, chloroplast relocation, and stomatal opening, whereas in fungal organisms, they are used for adjusting the circadian temporal organization of the cells to the daily and seasonal periods. They are a subset of PAS domains.
A FMN-binding fluorescent protein (FbFP), also known as a LOV-based fluorescent protein, is a small, oxygen-independent fluorescent protein that binds flavin mononucleotide (FMN) as a chromophore.
Kaliseptine (AsKS) is a neurotoxin which can be found in the snakelocks anemone Anemonia viridis. It belongs to a class of sea anemone neurotoxins that inhibits voltage-gated potassium channels.
Small ultra red fluorescent protein (smURFP) is a class of far-red fluorescent protein evolved from a cyanobacterial phycobiliprotein, α-allophycocyanin. Native α-allophycocyanin requires an exogenous protein, known as a lyase, to attach the chromophore, phycocyanobilin. Phycocyanobilin is not present in mammalian cells. smURFP was evolved to covalently attach phycocyanobilin without a lyase and fluoresce, covalently attach biliverdin and fluoresce, blue-shift fluorescence to match the organic fluorophore, Cy5, and not inhibit E. coli growth. smURFP was found after 12 rounds of random mutagenesis and manually screening 10,000,000 bacterial colonies.
Red fluorescent protein (RFP) is a protein which acts as a fluorophore, fluorescing red-orange when excited. The original variant occurs naturally in the coral genus Discosoma, and is named DsRed. Several new variants have been developed using directed mutagenesis which fluoresce orange, red, and far-red.
FAST is a genetically-encoded protein tag which, upon reversible combination with a fluorogenic chromophore, allows the reporting of proteins of interest. FAST, a small 14 kDa protein, was engineered from the photoactive yellow protein (PYP) by directed evolution. It was disclosed for the first time in 2016 by researchers from Ecole normale supérieure de Paris. FAST was further evolved into splitFAST (2019), a complementation system for protein-protein interaction monitoring, and CATCHFIRE (2023), a self-reporting protein dimerizing system.
Biliproteins are pigment protein compounds that are located in photosynthesising organisms such as algae, and sometimes also in certain insects. They refer to any protein that contains a bilin chromophore. In plants and algae, the main function of biliproteins is to make the process of light accumulation required for photosynthesis more efficient; while in insects they play a role in growth and development. Some of their properties: including light-receptivity, light-harvesting and fluorescence have made them suitable for applications in bioimaging and as indicators; while other properties such as anti-oxidation, anti-aging and anti-inflammation in phycobiliproteins have given them potential for use in medicine, cosmetics and food technology. While research on biliproteins dates back as far as 1950, it was hindered due to issues regarding biliprotein structure, lack of methods available for isolating individual biliprotein components, as well as limited information on lyase reactions . Research on biliproteins has also been primarily focused on phycobiliproteins; but advances in technology and methodology, along with the discovery of different types of lyases, has renewed interest in biliprotein research, allowing new opportunities for investigating biliprotein processes such as assembly/disassembly and protein folding.
References
- ↑ Fearon WR (1940). An Introduction to Biochemistry. Elsevier. p. 131. ISBN 9781483225395.
- ↑ Kanegae T, Hayashida E, Kuramoto C, Wada M (November 2006). "A single chromoprotein with triple chromophores acts as both a phytochrome and a phototropin". Proceedings of the National Academy of Sciences of the United States of America. 103 (47): 17997–18001. Bibcode:2006PNAS..10317997K. doi: 10.1073/pnas.0603569103 . PMC 1693861 . PMID 17093054.
- ↑ Zagranichny VE, Rudenko NV, Gorokhovatsky AY, Zakharov MV, Balashova TA, Arseniev AS (October 2004). "Traditional GFP-type cyclization and unexpected fragmentation site in a purple chromoprotein from Anemonia sulcata, asFP595". Biochemistry. 43 (42): 13598–13603. doi:10.1021/bi0488247. PMID 15491166.
- 1 2 Chang HY, Ko TP, Chang YC, Huang KF, Lin CY, Chou HY, et al. (June 2019). "Crystal structure of the blue fluorescent protein with a Leu-Leu-Gly tri-peptide chromophore derived from the purple chromoprotein of Stichodactyla haddoni". International Journal of Biological Macromolecules. 130: 675–684. doi:10.1016/j.ijbiomac.2019.02.138. PMID 30836182. S2CID 73497504.
- ↑ Liljeruhm J, Funk SK, Tietscher S, Edlund AD, Jamal S, Wistrand-Yuen P, et al. (2018-05-10). "Engineering a palette of eukaryotic chromoproteins for bacterial synthetic biology". Journal of Biological Engineering. 12 (1): 8. doi: 10.1186/s13036-018-0100-0 . PMC 5946454 . PMID 29760772.
- ↑ Campbell RE, Tour O, Palmer AE, Steinbach PA, Baird GS, Zacharias DA, Tsien RY (June 2002). "A monomeric red fluorescent protein". Proceedings of the National Academy of Sciences of the United States of America. 99 (12): 7877–82. Bibcode:2002PNAS...99.7877C. doi: 10.1073/pnas.082243699 . PMC 122988 . PMID 12060735.
- ↑ Bao L, Menon PN, Liljeruhm J, Forster AC (December 2020). "Overcoming chromoprotein limitations by engineering a red fluorescent protein". Analytical Biochemistry. 611: 113936. doi: 10.1016/j.ab.2020.113936 . PMID 32891596. S2CID 221523489.
- ↑ Ahmed, F. Hafna; Caputo, Alessandro T.; French, Nigel G.; Peat, Thomas S.; Whitfield, Jason; Warden, Andrew C.; Newman, Janet; Scott, Colin (2022-05-01). "Over the rainbow: structural characterization of the chromoproteins gfasPurple, amilCP, spisPink and eforRed". Acta Crystallographica Section D. 78 (Pt 5): 599–612. doi:10.1107/S2059798322002625. ISSN 2059-7983. PMC 9063845 . PMID 35503208.
- ↑ Tsang, Jennifer. "Chromoproteins: Colorful Proteins For Molecular Biology Experiments". blog.addgene.org. Retrieved 2024-10-28.
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