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Prokaryotic Elongation Factor
Elongation factors are a set of proteins that function at the ribosome, during protein synthesis, to facilitate translational elongation from the formation of the first to the last peptide bond of a growing polypeptide. Most common elongation factors in prokaryotes are EF-Tu, EF-Ts, EF-G. Bacteria and eukaryotes use elongation factors that are largely homologous to each other, but with distinct structures and different research nomenclatures. Elongation is the most rapid step in translation. In bacteria, it proceeds at a rate of 15 to 20 amino acids added per second (about 45-60 nucleotides per second). In eukaryotes the rate is about two amino acids per second (about 6 nucleotides read per second). Elongation factors play a role in orchestrating the events of this process, and in ensuring the high accuracy translation at these speeds. Nomenclature of homologous EFs In addition to their cytoplasmic machinery, eukaryotic mitochondria and plastids have their own translat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EEF-2
Eukaryotic elongation factor 2 is a protein that in humans is encoded by the ''EEF2'' gene. It is the archaeal and eukaryotic counterpart of bacterial EF-G. This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the ribosome. This protein is completely inactivated by EF-2 kinase phosphorylation. aEF2/eEF2 found in most archaea and eukaryotes, including humans, contains a post translationally modified histidine diphthamide. It is the target of diphtheria toxin (from ''Corynebacterium diphtheriae''), and exotoxin A (from ''Pseudomonas aeruginosa ''Pseudomonas aeruginosa'' is a common encapsulated, gram-negative, aerobic–facultatively anaerobic, rod-shaped bacterium that can cause disease in plants and animals, including humans. A species of considerable medical importance, ''P. aerugi ...''). The inactivation of EF-2 by toxins inhibits protei ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Diphtheria Toxin
Diphtheria toxin is an exotoxin secreted by '' Corynebacterium diphtheriae'', the pathogenic bacterium that causes diphtheria. The toxin gene is encoded by a prophageA prophage is a virus that has inserted itself into the genome of the host bacterium. called corynephage β. The toxin causes the disease in humans by gaining entry into the cell cytoplasm and inhibiting protein synthesis. Structure Diphtheria toxin is a single polypeptide chain of 535 amino acids consisting of two subunits linked by disulfide bridges, known as an A-B toxin. Binding to the cell surface of the B subunit (the less stable of the two subunits) allows the A subunit (the more stable part of the protein) to penetrate the host cell. The crystal structure of the diphtheria toxin homodimer has been determined to 2.5 Ångstrom resolution. The structure reveals a Y-shaped molecule consisting of three domains. Fragment A contains the catalytic C domain, and fragment B consists of the T and R domains: ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Corynebacterium Diphtheriae
''Corynebacterium diphtheriae'' is the pathogenic bacterium that causes diphtheria. It is also known as the Klebs–Löffler bacillus, because it was discovered in 1884 by German bacteriologists Edwin Klebs (1834–1912) and Friedrich Löffler (1852–1915). The bacteria are usually harmless unless they are infected by a bacteriophage that carries a gene that gives rise to a toxin. This toxin causes the disease. Diphtheria is caused by the adhesion and infiltration of the bacteria into the mucosal layers of the body, primarily affecting the respiratory tract and the subsequent release of an endotoxin. The toxin has a localized effect on skin lesions, as well as a metastatic, proteolytic effects on other organ systems in severe infections. Originally a major cause of childhood mortality, diphtheria has been almost entirely eradicated due to the vigorous administration of the diphtheria vaccination in the 1910s. Diphtheria is no longer transmitted as frequently due to the d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Selenocysteine
Selenocysteine (symbol Sec or U, in older publications also as Se-Cys) is the 21st proteinogenic amino acid. Selenoproteins contain selenocysteine residues. Selenocysteine is an analogue of the more common cysteine with selenium in place of the sulfur. Selenocysteine is present in several enzymes (for example glutathione peroxidases, tetraiodothyronine 5′ deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases, selenophosphate synthetase 2, methionine-''R''-sulfoxide reductase B1 (SEPX1), and some hydrogenases). It occurs in all three domains of life, including important enzymes (listed above) present in humans. Selenocysteine was discovered by biochemist Thressa Stadtman at the National Institutes of Health. Chemistry Selenocysteine is the Se-analogue of cysteine. It is rarely encountered outside of living tissue (and is not available commercially) because it is very susceptible to air-oxidation. More common is the oxidized derivative selenocystine ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Release Factor
A release factor is a protein that allows for the termination of translation by recognizing the termination codon or stop codon in an mRNA sequence. They are named so because they release new peptides from the ribosome. Background During translation of mRNA, most codons are recognized by "charged" tRNA molecules, called aminoacyl-tRNAs because they are adhered to specific amino acids corresponding to each tRNA's anticodon. In the standard genetic code, there are three mRNA stop codons: UAG ("amber"), UAA ("ochre"), and UGA ("opal" or "umber"). Although these stop codons are triplets just like ordinary codons, they are not decoded by tRNAs. It was discovered by Mario Capecchi in 1967 that, instead, tRNAs do not ordinarily recognize stop codons at all, and that what he named "release factor" was not a tRNA molecule but a protein. Later, it was demonstrated that different release factors recognize different stop codons. Classification There are two classes of release factor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GUF1
GUF1 homolog, GTPase is a protein that in humans is encoded by the GUF1 gene. It is the mitochondrial homolog of elongation factor 4 Elongation factor 4 (EF-4) is an elongation factor that is thought to back-Protein targeting, translocate on the ribosome during the translation of RNA to proteins. It is found near-universally in bacteria and in eukaryotic endosymbiotic organel .... References Further reading * {{gene-4-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GFM2
Ribosome-releasing factor 2, mitochondrial is a protein that in humans is encoded by the ''GFM2'' gene. Unlike the other EF-G homolog GFM1, GFM2 functions as a Ribosome Recycling Factor Ribosome recycling factor or ribosome release factor (RRF) is a protein found in bacterial cells as well as eukaryotic organelles, specifically mitochondria and chloroplasts. It functions to recycle ribosomes after completion of protein synthesis ... in termination. References External links * {{gene-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GFM1
Elongation factor G 1, mitochondrial is a protein that in humans is encoded by the ''GFM1'' gene. It is an EF-G homolog. Eukaryotes contain two protein translational systems, one in the cytoplasm and one in the mitochondria. Mitochondrial translation is crucial for maintaining mitochondrial function and mutations in this system lead to a breakdown in the respiratory chain-oxidative phosphorylation system and to impaired maintenance of mitochondrial DNA. This gene encodes one of the mitochondrial translation elongation factors. Its role in the regulation of normal mitochondrial function and in different disease states attributed to mitochondrial dysfunction is not known. Model organisms Model organisms have been used in the study of GFM1 function. A conditional knockout mouse line, called ''Gfm1tm1a(EUCOMM)Wtsi'' was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TSFM
Elongation factor Ts, mitochondrial is a protein that in humans is encoded by the ''TSFM'' gene. It is an EF-Ts EF-Ts (elongation factor thermo stable) is one of the prokaryotic elongation factors. It is found in human mitochrondria as TSFM. It is similar to eukaryotic EF-1B. EF-Ts serves as the guanine nucleotide exchange factor for EF-Tu (elongatio ... homolog. References Further reading * * * * * * * * External links * * {{gene-12-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TUFM
Elongation factor Tu, mitochondrial is a protein that in humans is encoded by the ''TUFM'' gene. It is an EF-Tu EF-Tu (elongation factor thermo unstable) is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein, and facilitates the selection and binding of an aa-tRNA to th ... homolog. References Further reading * * * * * * * * * * * * * * {{gene-16-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
