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Late Embryogenesis Abundant Proteins
Late embryogenesis abundant proteins (LEA proteins) are proteins in plants, and some bacteria and invertebrates that protect against protein aggregation due to desiccation or osmotic stresses associated with low temperature. LEA proteins were initially discovered accumulating late in embryogenesis of cotton seeds. Although abundant in seeds and pollens, LEA proteins have been found to protect against desiccation, cold, or high salinity in a variety of organisms, including the bacterium '' Deinococcus radiodurans'', nematode ''Caenorhabditis elegans'', ''Artemia'' (brine shrimp), and rotifers. LEA proteins function by mechanisms which are distinct from those displayed by heat shock molecular chaperones. Although the causes of LEA protein induction have not yet been determined, conformational changes in transcription factors or integral membrane proteins due to water loss have been suggested. LEA proteins are particularly protective of mitochondrial membranes against dehydration ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Deinococcus Radiodurans
''Deinococcus radiodurans'' is an extremophilic bacterium and one of the most radiation-resistant organisms known. It can survive cold, dehydration, vacuum, and acid, and therefore is known as a polyextremophile. It has been listed as the world's toughest known bacterium in ''The Guinness Book Of World Records''. Name and classification The name ''Deinococcus radiodurans'' derives from the Ancient Greek δεινός () and κόκκος () meaning "terrible grain/berry" and the Latin and , meaning "radiation surviving". The species was formerly called ''Micrococcus radiodurans''. As a consequence of its hardiness, it has been nicknamed “Conan the Bacterium”, in reference to Conan the Barbarian. Initially, it was placed in the genus ''Micrococcus''. After evaluation of ribosomal RNA sequences and other evidence, it was placed in its own genus ''Deinococcus'', which is closely related to the genus ''Thermus''. ''Deinococcus'' is one genus of three in the order ''Deinococcale ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cryptobiosis
Cryptobiosis or anabiosis is a metabolic state of life entered by an organism in response to adverse environmental conditions such as desiccation, freezing, and oxygen deficiency. In the cryptobiotic state, all measurable metabolic processes stop, preventing reproduction, development, and repair. When environmental conditions return to being hospitable, the organism will return to its metabolic state of life as it was prior to the cryptobiosis. Forms Anhydrobiosis Anhydrobiosis is the most studied form of cryptobiosis and occurs in situations of extreme desiccation. The term ''anhydrobiosis'' derives from the Greek for "life without water" and is most commonly used for the desiccation tolerance observed in certain invertebrate animals such as bdelloid rotifers, tardigrades, brine shrimp, nematodes, and at least one insect, a species of chironomid (''Polypedilum vanderplanki''). However, other life forms exhibit desiccation tolerance. These include the resurrection plant ' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mitochondria
A mitochondrion (; ) is an organelle found in the Cell (biology), cells of most Eukaryotes, such as animals, plants and Fungus, fungi. Mitochondria have a double lipid bilayer, membrane structure and use aerobic respiration to generate adenosine triphosphate (ATP), which is used throughout the cell as a source of chemical energy. They were discovered by Albert von Kölliker in 1857 in the voluntary muscles of insects. The term ''mitochondrion'' was coined by Carl Benda in 1898. The mitochondrion is popularly nicknamed the "powerhouse of the cell", a phrase coined by Philip Siekevitz in a 1957 article of the same name. Some cells in some multicellular organisms lack mitochondria (for example, mature mammalian red blood cells). A large number of unicellular organisms, such as microsporidia, parabasalids and diplomonads, have reduced or transformed their mitochondria into mitosome, other structures. One eukaryote, ''Monocercomonoides'', is known to have completely lost its mitocho ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Integral Membrane Protein
An integral, or intrinsic, membrane protein (IMP) is a type of membrane protein that is permanently attached to the biological membrane. All ''transmembrane proteins'' are IMPs, but not all IMPs are transmembrane proteins. IMPs comprise a significant fraction of the proteins encoded in an organism's genome. Proteins that cross the membrane are surrounded by annular lipids, which are defined as lipids that are in direct contact with a membrane protein. Such proteins can only be separated from the membranes by using detergents, nonpolar solvents, or sometimes denaturing agents. Structure Three-dimensional structures of ~160 different integral membrane proteins have been determined at atomic resolution by X-ray crystallography or nuclear magnetic resonance spectroscopy. They are challenging subjects for study owing to the difficulties associated with extraction and crystallization. In addition, structures of many water-soluble protein domains of IMPs are available in the Prote ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transcription Factor
In molecular biology, a transcription factor (TF) (or sequence-specific DNA-binding factor) is a protein that controls the rate of transcription of genetic information from DNA to messenger RNA, by binding to a specific DNA sequence. The function of TFs is to regulate—turn on and off—genes in order to make sure that they are expressed in the desired cells at the right time and in the right amount throughout the life of the cell and the organism. Groups of TFs function in a coordinated fashion to direct cell division, cell growth, and cell death throughout life; cell migration and organization (body plan) during embryonic development; and intermittently in response to signals from outside the cell, such as a hormone. There are up to 1600 TFs in the human genome. Transcription factors are members of the proteome as well as regulome. TFs work alone or with other proteins in a complex, by promoting (as an activator), or blocking (as a repressor) the recruitment of RNA ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chaperone (protein)
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis. The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA. One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress. The majority of molecular chaperones do not convey any steric information for protein folding, and instead assist in protein folding by binding to and stabilizing folding interme ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heat Shock
The heat shock response (HSR) is a cell stress response that increases the number of molecular chaperones to combat the negative effects on proteins caused by stressors such as increased temperatures, oxidative stress, and heavy metals. In a normal cell, proteostasis (protein homeostasis) must be maintained because proteins are the main functional units of the cell. Many proteins take on a defined configuration in a process known as protein folding in order to perform their biological functions. If these structures are altered, critical processes could be affected, leading to cell damage or death. The heat shock response can be employed under stress to induce the expression of heat shock proteins (HSP), many of which are molecular chaperones, that help prevent or reverse protein misfolding and provide an environment for proper folding. Protein folding is already challenging due to the crowded intracellular space where aberrant interactions can arise; it becomes more difficult when ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rotifer
The rotifers (, from the Latin , "wheel", and , "bearing"), commonly called wheel animals or wheel animalcules, make up a phylum (Rotifera ) of microscopic and near-microscopic pseudocoelomate animals. They were first described by Rev. John Harris in 1696, and other forms were described by Antonie van Leeuwenhoek in 1703. Most rotifers are around long (although their size can range from to over ), and are common in freshwater environments throughout the world with a few saltwater species. Some rotifers are free swimming and truly planktonic, others move by inchworming along a substrate, and some are sessile, living inside tubes or gelatinous holdfasts that are attached to a substrate. About 25 species are colonial (e.g., '' Sinantherina semibullata''), either sessile or planktonic. Rotifers are an important part of the freshwater zooplankton, being a major foodsource and with many species also contributing to the decomposition of soil organic matter. Most species of the r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Artemia
''Artemia'' is a genus of aquatic crustaceans also known as brine shrimp. It is the only genus in the family Artemiidae. The first historical record of the existence of ''Artemia'' dates back to the first half of the 10th century AD from Urmia Lake, Iran, with an example called by an Iranian geographer an "aquatic dog," although the first unambiguous record is the report and drawings made by Schlösser in 1757 of animals from Lymington, England. ''Artemia'' populations are found worldwide in inland saltwater lakes, but not in oceans. ''Artemia'' are able to avoid cohabiting with most types of predators, such as fish, by their ability to live in waters of very high salinity (up to 25%). The ability of the ''Artemia'' to produce dormant eggs, known as cysts, has led to extensive use of ''Artemia'' in aquaculture. The cysts may be stored indefinitely and hatched on demand to provide a convenient form of live feed for larval fish and crustaceans. Nauplii of the brine shrimp ''Artemia' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Caenorhabditis Elegans
''Caenorhabditis elegans'' () is a free-living transparent nematode about 1 mm in length that lives in temperate soil environments. It is the type species of its genus. The name is a blend of the Greek ''caeno-'' (recent), ''rhabditis'' (rod-like) and Latin ''elegans'' (elegant). In 1900, Maupas initially named it '' Rhabditides elegans.'' Osche placed it in the subgenus ''Caenorhabditis'' in 1952, and in 1955, Dougherty raised ''Caenorhabditis'' to the status of genus. ''C. elegans'' is an unsegmented pseudocoelomate and lacks respiratory or circulatory systems. Most of these nematodes are hermaphrodites and a few are males. Males have specialised tails for mating that include spicules. In 1963, Sydney Brenner proposed research into ''C. elegans,'' primarily in the area of neuronal development. In 1974, he began research into the molecular and developmental biology of ''C. elegans'', which has since been extensively used as a model organism. It was the first multicellu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nematode
The nematodes ( or grc-gre, Νηματώδη; la, Nematoda) or roundworms constitute the phylum Nematoda (also called Nemathelminthes), with plant-Parasitism, parasitic nematodes also known as eelworms. They are a diverse animal phylum inhabiting a broad range of environments. Less formally, they are categorized as Helminths, but are taxonomically classified along with Arthropod, arthropods, Tardigrade, tardigrades and other moulting animalia, animals in the clade Ecdysozoa, and unlike platyhelminthe, flatworms, have tubular digestion, digestive systems with openings at both ends. Like tardigrades, they have a reduced number of Hox genes, but their sister phylum Nematomorpha has kept the ancestral protostome Hox genotype, which shows that the reduction has occurred within the nematode phylum. Nematode species can be difficult to distinguish from one another. Consequently, estimates of the number of nematode species described to date vary by author and may change rapidly over ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
