Pleurotolysin
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Pleurotolysin
PleurotolysinTC# 1.C.97.1.1, a sphingomyelin-specific cytolysin. Its A (17 kDaQ8X1M9 and B (59 kDaQ5W9E8 components are assembled into a transmembrane pore complex. The Pleurotolysin Pore-Forming (Pleurotolysin) FamilyTC# 1.C.97 is a family of pore forming proteins belonging to the MACPF superfamily. Function Proteins with membrane-attack complex/perforin (MACPF) domains have a variety of biological roles, including defense and attack, organismal development, and cell adhesion and signaling. The distribution of these proteins in fungi appears to be restricted to some Pezizomycotina and Basidiomycota species only, in correlation with the aegerolysinsPF06355. These two protein groups coincide in only a few species, and they operate as cytolytic bi-component pore-forming agents. Representative proteins include pleurotolysin B, which has a MACPF domain, the aegerolysin-like protein pleurotolysin A, and the very similar ostreolysin ATC# 1.C.97.3.2 that has been purified from oyster mu ...
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MACPF
The Membrane Attack Complex/Perforin (MACPF) superfamily, sometimes referred to as the MACPF/CDC superfamily, is named after a domain that is common to the membrane attack complex (MAC) proteins of the complement system (C6, C7, C8α, C8β and C9) and perforin (PF). Members of this protein family are pore-forming toxins (PFTs). In eukaryotes, MACPF proteins play a role in immunity and development. Archetypal members of the family are complement C9 and perforin, both of which function in human immunity. C9 functions by punching holes in the membranes of Gram-negative bacteria. Perforin is released by cytotoxic T cells and lyses virally infected and transformed cells. In addition, perforin permits delivery of cytotoxic proteases called granzymes that cause cell death. Deficiency of either protein can result in human disease. Structural studies reveal that MACPF domains are related to cholesterol-dependent cytolysins (CDCs), a family of pore forming toxins previously thought ...
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Sphingomyelin
Sphingomyelin (SPH, ˌsfɪŋɡoˈmaɪəlɪn) is a type of sphingolipid found in animal cell membranes, especially in the membranous myelin sheath that surrounds some nerve cell axons. It usually consists of phosphocholine and ceramide, or a ethanolamine, phosphoethanolamine head group; therefore, sphingomyelins can also be classified as sphingophospholipids. In humans, SPH represents ~85% of all sphingolipids, and typically make up 10–20 mol % of plasma membrane lipids. Sphingomyelin was first isolated by Germans, German chemist Johann Ludwig Wilhelm Thudichum, Johann L.W. Thudicum in the 1880s. The structure of sphingomyelin was first reported in 1927 as N-acyl-sphingosine-1-phosphorylcholine. Sphingomyelin content in mammals ranges from 2 to 15% in most tissues, with higher concentrations found in nerve tissues, red blood cells, and the ocular lenses. Sphingomyelin has significant structural and functional roles in the cell. It is a plasma membrane component and parti ...
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Cytolysin
Cytolysin refers to the substance secreted by microorganisms, plants or animals that is specifically toxic to individual cells, in many cases causing their dissolution through lysis. Cytolysins that have a specific action for certain cells are named accordingly. For instance, the cytolysins responsible for the destruction of red blood cells, thereby liberating hemoglobins, are named ''hemolysins'', and so on. Cytolysins may be involved in immunity as well as in venoms. Hemolysin is also used by certain bacteria, such as ''Listeria monocytogenes'', to disrupt the phagosome membrane of macrophages and escape into the cytoplasm of the cell. History and background The term "Cytolysin" or "Cytolytic toxin" was first introduced by Alan Bernheimer to describe membrane damaging toxins ( MDTs) that have cytolytic effects to cells. The first kind of cytolytic toxin discovered have hemolytic effects on erythrocytes of certain sensitive species, such as Human. For this reason "Hemolysin" wa ...
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Pezizomycotina
Pezizomycotina make up most of the Ascomycota fungi and include most lichenized fungi too. Pezizomycotina contains the filamentous ascomycetes and is a subdivision of the Ascomycota (fungi that form their spores in a sac-like ''ascus''). It is more or less synonymous with the older taxon Euascomycota. These fungi reproduce by fission rather than budding and this subdivision includes almost all the ascus fungi that have fruiting bodies visible to the naked eye (exception: genus ''Neolecta'', which belongs to the Taphrinomycotina). See the taxobox for a list of the classes that make up the Pezizomycotina. The old class Loculoascomycetes (consisting of all the bitunicate Ascomycota) has been replaced by the two classes Eurotiomycetes and Dothideomycetes. The rest of the Pezizomycotina also include the previously defined hymenial groups Discomycetes (now Leotiomycetes) and Pyrenomycetes (Sordariomycetes). Some important groups in Pezizomycotina include: Pezizomycetes (the opercula ...
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Basidiomycota
Basidiomycota () is one of two large divisions that, together with the Ascomycota, constitute the subkingdom Dikarya (often referred to as the "higher fungi") within the kingdom Fungi. Members are known as basidiomycetes. More specifically, Basidiomycota includes these groups: mushrooms, puffballs, stinkhorns, bracket fungi, other polypores, jelly fungi, boletes, chanterelles, earth stars, smuts, bunts, rusts, mirror yeasts, and ''Cryptococcus'', the human pathogenic yeast. Basidiomycota are filamentous fungi composed of hyphae (except for basidiomycota-yeast) and reproduce sexually via the formation of specialized club-shaped end cells called basidia that normally bear external meiospores (usually four). These specialized spores are called basidiospores. However, some Basidiomycota are obligate asexual reproducers. Basidiomycota that reproduce asexually (discussed below) can typically be recognized as members of this division by gross similarity to others, by the form ...
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Pleurotus Ostreatus
''Pleurotus ostreatus'', the oyster mushroom, oyster fungus, or hiratake, is a common edible mushroom. It was first cultivated in Germany as a subsistence measure during World War I and is now grown commercially around the world for food. It is related to the similarly cultivated king oyster mushroom. Oyster mushrooms can also be used industrially for mycoremediation purposes. The oyster mushroom is one of the more commonly sought wild mushrooms, though it can also be cultivated on straw and other media. It has the bittersweet aroma of benzaldehyde (which is also characteristic of bitter almonds). Name Both the Latin and common names refer to the shape of the fruiting body. The Latin ''pleurotus'' (side-ear) refers to the sideways growth of the stem with respect to the cap, while the Latin ''ostreatus'' (and the English common name, oyster) refers to the shape of the cap which resembles the bivalve of the same name. The reference to ''oyster'' may also derive from the slipp ...
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Recombinant DNA
Recombinant DNA (rDNA) molecules are DNA molecules formed by laboratory methods of genetic recombination (such as molecular cloning) that bring together genetic material from multiple sources, creating sequences that would not otherwise be found in the genome. Recombinant DNA is the general name for a piece of DNA that has been created by combining at least two fragments from two different sources. Recombinant DNA is possible because DNA molecules from all organisms share the same chemical structure, and differ only in the nucleotide sequence within that identical overall structure. Recombinant DNA molecules are sometimes called chimeric DNA, because they can be made of material from two different species, like the mythical chimera. R-DNA technology uses palindromic sequences and leads to the production of sticky and blunt ends. The DNA sequences used in the construction of recombinant DNA molecules can originate from any species. For example, plant DNA may be joined to bacter ...
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Methionine
Methionine (symbol Met or M) () is an essential amino acid in humans. As the precursor of other amino acids such as cysteine and taurine, versatile compounds such as SAM-e, and the important antioxidant glutathione, methionine plays a critical role in the metabolism and health of many species, including humans. It is encoded by the codon AUG. Methionine is also an important part of angiogenesis, the growth of new blood vessels. Supplementation may benefit those suffering from copper poisoning. Overconsumption of methionine, the methyl group donor in DNA methylation, is related to cancer growth in a number of studies. Methionine was first isolated in 1921 by John Howard Mueller. Biochemical details Methionine (abbreviated as Met or M; encoded by the codon AUG) is an α-amino acid that is used in the biosynthesis of proteins. It contains a carboxyl group (which is in the deprotonated −COO− form under biological pH conditions), an amino group (which is in the protonated fo ...
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Ceramide Phosphoethanolamine Synthase
In enzymology, a ceramide phosphoethanolamine synthase ( EC 2.7.8.-) is an enzyme that catalyzes the chemical reaction :a ceramide + a phosphoethanolamine head group donor \rightleftharpoons a ceramide-phosphoethanolamine + side product Ceramide phosphoethanolamine (CPE) is a sphingolipid consisted of a ceramide and a phosphoethanolamine head group. Thus, this class of enzymes uses ceramide and a donor molecule for phosphoethanolamine as substrates to produce a ceramide phosphoethanolamine and a side product. The head group donor for phosphoethanolamine can be either phosphatidylethanolamine or CDP-ethanolamine, thus the side product is either a 1,2-diacylglycerol or a CMP, respectively. This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. Mammalian Ceramide Phosphoethanolamine Synthases In mammalian cells, two CPE synthase activities have been described, one resides in the endoplasmic reticulum, and th ...
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Protein Families
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. The most important of these is sequence similarity (usually amino-acid sequence), since it is the strictest indicator of homology and therefore the clearest indicator of common ancestry. A fairly well developed framework exists for evaluating the significance of similarity between a group of sequences using sequence alignment methods. Proteins that do not share a common ancestor are very unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein familie ...
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