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AMPylation
Adenylylation, more commonly known as AMPylation, is a process in which an adenosine monophosphate (AMP) molecule is covalently attached to the amino acid side chain of a protein. This covalent addition of AMP to a hydroxyl side chain of the protein is a posttranslational modification. Adenylylation involves a phosphodiester bond between a hydroxyl group of the molecule undergoing adenylylation, and the phosphate group of the adenosine monophosphate nucleotide (i.e. adenylic acid). Enzymes that are capable of catalyzing this process are called AMPylators. The known amino acids to be targeted in the protein are tyrosine and threonine, and sometimes serine. When charges on a protein undergo a change, it affects the characteristics of the protein, normally by altering its shape via interactions of the amino acids which make up the protein. AMPylation can have various effects on the protein. These are properties of the protein like, stability, enzymatic activity, co-factor bindin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AMPylation Before
Adenylylation, more commonly known as AMPylation, is a process in which an adenosine monophosphate (AMP) molecule is covalently attached to the amino acid side chain of a protein. This covalent addition of AMP to a hydroxyl side chain of the protein is a posttranslational modification. Adenylylation involves a phosphodiester bond between a hydroxyl group of the molecule undergoing adenylylation, and the phosphate group of the adenosine monophosphate nucleotide (i.e. adenylic acid). Enzymes that are capable of catalyzing this process are called AMPylators. The known amino acids to be targeted in the protein are tyrosine and threonine, and sometimes serine. When charges on a protein undergo a change, it affects the characteristics of the protein, normally by altering its shape via interactions of the amino acids which make up the protein. AMPylation can have various effects on the protein. These are properties of the protein like, stability, enzymatic activity, co-factor binding, and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fic/DOC Protein Family
In molecular biology, the Fic/DOC protein family is a family of proteins which catalyzes the post-translational modification of proteins using phosphate-containing compound as a substrate. Fic domain proteins typically use ATP as a co-factor, but in some cases GTP or UTP is used. Post-translational modification performed by Fic domains is usually NMPylation (AMPylation, GMPylation or UMPylation), however they also catalyze phosphorylation and phosphocholine transfer. This family contains a central conserved motif HPFX /ENGR in most members and it carries the invariant catalytic histidine. Fic domain was found in bacteria, eukaryotes and archaea and can be found organized in almost hundred different multi-domain assemblies. Functions First fic gene was discovered in the late 1980s in Escherichia coli. Mutation in this gene impaired cell division under stress conditions (cyclic AMP in growth medium at high temperature), which led to annotation as fic-1 for filamentation induce ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rho Family Of GTPases
The Rho family of GTPases is a family of small (~21 kDa) signaling G proteins, and is a subfamily of the Ras superfamily. The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants. Three members of the family have been studied in detail: Cdc42, Rac1, and RhoA. All G proteins are "molecular switches", and Rho proteins play a role in organelle development, cytoskeletal dynamics, cell movement, and other common cellular functions. History Identification of the Rho family of GTPases began in the mid-1980s. The first identified Rho member was RhoA, isolated serendipitously in 1985 from a low stringency cDNA screening. Rac1 and Rac2 were identified next, in 1989 followed by Cdc42 in 1990. Eight additional mammalian Rho members were identified from biological screenings until the late 1990s, a turning point in biology where availability of complete genome sequ ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Legionella Pneumophila
''Legionella pneumophila'' is a thin, aerobic, pleomorphic, flagellated, non-spore-forming, Gram-negative bacterium of the genus '' Legionella''. ''L. pneumophila'' is the primary human pathogenic bacterium in this group and is the causative agent of Legionnaires' disease, also known as legionellosis. In nature, ''L. pneumophila'' infects freshwater and soil amoebae of the genera ''Acanthamoeba'' and '' Naegleria''. The mechanism of infection is similar in amoeba and human cells. Characterization ''L. pneumophila'' is a Gram-negative, non-encapsulated, aerobic bacillus with a single, polar flagellum often characterized as being a coccobacillus. It is aerobic and unable to hydrolyse gelatin or produce urease. It is also non- fermentative. ''L. pneumophila'' is neither pigmented nor does it autofluoresce. It is oxidase- and catalase-positive, and produces beta-lactamase. ''L. pneumophila'' colony morphology is gray-white with a textured, cut-glass appearance; it also requi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Guanine Nucleotide Exchange Factor
Guanine nucleotide exchange factors (GEFs) are proteins or protein domains that activate monomeric GTPases by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP). A variety of unrelated structural domains have been shown to exhibit guanine nucleotide exchange activity. Some GEFs can activate multiple GTPases while others are specific to a single GTPase. Function Guanine nucleotide exchange factors (GEFs) are proteins or protein domains involved in the activation of small GTPases. Small GTPases act as molecular switches in intracellular signaling pathways and have many downstream targets. The most well-known GTPases comprise the Ras superfamily and are involved in essential cell processes such as cell differentiation and proliferation, cytoskeletal organization, vesicle trafficking, and nuclear transport. GTPases are active when bound to GTP and inactive when bound to GDP, allowing their activity to be regulated by GEFs and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RAB1B
Ras-related protein Rab-1B is a protein that in humans is encoded by the ''RAB1B'' gene. Interactions RAB1B has been shown to interact with GOLGA2 Golgin subfamily A member 2 is a protein that in humans is encoded by the ''GOLGA2'' gene. Function The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of .... References Further reading * * * * * * * * * * * * * * * * * * * {{Gene-11-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Vibrio Parahaemolyticus
''Vibrio parahaemolyticus'' (V. parahaemolyticus) is a curved, rod-shaped, Gram-negative bacterium found in the sea and in estuaries which, when ingested, may cause gastrointestinal illness in humans. ''V. parahaemolyticus'' is oxidase positive, facultatively aerobic, and does not form spores. Like other members of the genus ''Vibrio'', this species is motile, with a single, polar flagellum. Pathogenesis While infection can occur by the fecal-oral route, ingestion of bacteria in raw or undercooked seafood, usually oysters, is the predominant cause of the acute gastroenteritis caused by ''V. parahaemolyticus''. Wound infections also occur, but are less common than seafood-borne disease. The disease mechanism of ''V. parahaemolyticus'' infections has not been fully elucidated. Clinical isolates usually possess a pathogenicity island (PAI) on the second chromosome. The PAI can be acquired by horizontal gene transfer and contains genes for several virulence factors. Two fully ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pathogen
In biology, a pathogen ( el, πάθος, "suffering", "passion" and , "producer of") in the oldest and broadest sense, is any organism or agent that can produce disease. A pathogen may also be referred to as an infectious agent, or simply a germ. The term ''pathogen'' came into use in the 1880s. Typically, the term ''pathogen'' is used to describe an ''infectious'' microorganism or agent, such as a virus, bacterium, protozoan, prion, viroid, or fungus. Small animals, such as helminths and insects, can also cause or transmit disease. However, these animals are usually referred to as parasites rather than pathogens. The scientific study of microscopic organisms, including microscopic pathogenic organisms, is called microbiology, while parasitology refers to the scientific study of parasites and the organisms that host them. There are several pathways through which pathogens can invade a host. The principal pathways have different episodic time frames, but soil has the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phagocytosis
Phagocytosis () is the process by which a cell uses its plasma membrane to engulf a large particle (≥ 0.5 μm), giving rise to an internal compartment called the phagosome. It is one type of endocytosis. A cell that performs phagocytosis is called a phagocyte. In a multicellular organism's immune system, phagocytosis is a major mechanism used to remove pathogens and cell debris. The ingested material is then digested in the phagosome. Bacteria, dead tissue cells, and small mineral particles are all examples of objects that may be phagocytized. Some protozoa use phagocytosis as means to obtain nutrients. History Phagocytosis was first noted by Canadian physician William Osler (1876), and later studied and named by Élie Metchnikoff (1880, 1883). In immune system Phagocytosis is one main mechanisms of the innate immune defense. It is one of the first processes responding to infection, and is also one of the initiating branches of an adaptive immune response. Altho ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytoskeleton
The cytoskeleton is a complex, dynamic network of interlinking protein filaments present in the cytoplasm of all cells, including those of bacteria and archaea. In eukaryotes, it extends from the cell nucleus to the cell membrane and is composed of similar proteins in the various organisms. It is composed of three main components, microfilaments, intermediate filaments and microtubules, and these are all capable of rapid growth or disassembly dependent on the cell's requirements. A multitude of functions can be performed by the cytoskeleton. Its primary function is to give the cell its shape and mechanical resistance to deformation, and through association with extracellular connective tissue and other cells it stabilizes entire tissues. The cytoskeleton can also contract, thereby deforming the cell and the cell's environment and allowing cells to migrate. Moreover, it is involved in many cell signaling pathways and in the uptake of extracellular material (endocytosis), ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Actin
Actin is a protein family, family of Globular protein, globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in myofibril, muscle fibrils. It is found in essentially all Eukaryote, eukaryotic cells, where it may be present at a concentration of over 100 micromolar, μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm. An actin protein is the monomeric Protein subunit, subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the Muscle contraction, contractile apparatus in muscle cells. It can be present as either a free monomer called G-actin (globular) or as part of a linear polymer microfilament called F-actin (filamentous), both of which are essential for such important cellular functions as the Motility, mobility and contraction of cell (biology), cells during cell division. Actin participates in many important cellular pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
