- Intein
An intein is a segment of a protein that is able to excise itself and rejoin the remaining portions the exteins ... a role in intein propagation. In fact, many gene s have unrelated intein coding segments inserted .... Intein mediated protein splicing occurs after mRNA has been translated into a protein. This precursor protein contains three segments an N extein followed by the intein followed by a C extein. After splicing has taken place, the result is also called an extein. The first intein was discovered ... 5 263 19 9102 12 ref vacuolar ATPase without intein and the homologous gene in yeast with intein that was first ... 10.1038 nmeth886 ref Pharmaceutical inhibition of intein excision may be a useful tool for drug development , the protein that contains the intein will not carry out its normal function if the intein ... intein may allow this import to proceed. Excision of the intein after import would then restore the protein to wild type . Intein naming conventions The first part of an intein name is based on the Binomial ... is based on the name of the corresponding gene or extein. For example, the intein found in Thermoplasma ..., additional letters may be added to indicate a strain. If more than one intein is encoded in the corresponding .... For example, Msm dnaB 1 . The segment of the gene that encodes the intein is usually given the same name as the intein, but to avoid confusion, the name of the intein proper is usually ... domain in addition to the splicing domains. This domain is responsible for the spread of the intein by cleaving DNA at an intein free allele on the homologous chromosome , triggering the DNA repair ... copying the intein into a previously intein free site. The HEG domain is not necessary for intein splicing, and so it can be lost, forming a minimal, or mini intein. Several studies have demonstrated ... construct. Split inteins Sometimes, the intein of the precursor protein comes from two genes. In this case, the intein is said to be a split intein. For example, in Cyanobacteria , DnaE , the catalytic ... more details
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- Protein splicing
Protein splicing is an intramolecular reaction of a particular protein in which an internal protein segment called an intein is removed from a precursor protein with a ligation of C terminal and N terminal external proteins called extein s on both sides. The splicing junction of the precursor protein is mainly a cysteine or a serine , which are amino acid s containing a nucleophilic side chain . The protein splicing reactions which are known now do not require exogenous cofactors or energy sources such as adenosine triphosphate ATP or guanosine triphosphate GTP . Normally, splicing is associated only with Splicing genetics pre mRNA splicing . Types of inteins The type of the splicing proteins is categorized into four classes maxi intein, mini intein, trans splicing intein, and alanine intein. The maxi inteins are N and C terminal splicing domains containing an endonuclease domain. The mini inteins are typical N and C terminal splicing domains however, the endonuclease domain is not present. The trans splicing inteins are split inteins which are divided into N termini and C termini. Alanine inteins have the splicing junction of an alanine instead of a cysteine or a serine, in both of which the protein splicing occurs. History Protein splicing was reported by two groups Anraku and Stevens in 1990. They both discovered a Saccharomyces cerevisiae VMA1 in a precursor of a vacuolar H sup sup ATPase . The amino acid sequence of the N and C termini corresponded to 70 of that of a vacuolar H sup sup ATPase from other organisms, while the amino acid sequence of the central position corresponded to 30 of that of the yeast HO nuclease External links http starokadomskyy.narod.ru work intein eng.html Short rewiev http starokadomskyy.narod.ru Protein splicing eng.pdf Starokadomskyy PL. Protein Splicing, 2007 http www.neb.com neb inteins.html Protein splicing mechanism and intein structure MeshName Protein Splicing Category Proteins Category Protein biosynthesis ru ... more details
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- Homing endonuclease
encoded within an intron, PI for protein instert for those encoded within an intein. Some authors have ... pmc 49335 ref that is the second enzyme encoded by an intein found in the archaea Thermococcus ... reading frames encoding homing endonucleases have been found in intron s, intein s, and in freestanding ... The Intein Database and Registry from New England Biolabs accessdate 2010 08 09 . ref name pmid11752343 cite journal author Perler FB title InBase the Intein Database journal Nucleic Acids Res volume ... . Meganucleases . Restriction enzyme . Intron s and intein s. Intragenomic conflict Homing endonuclease ... more details
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- Protein tag
Unreferenced date December 2009 Protein tags are peptide sequences genetically grafted onto a recombinant protein. Often these tags are removable by chemical agents or by enzymatic means, such as proteolysis or intein splicing. Tags are attached to proteins for various purposes. Affinity tags are appended to proteins so that they can be purified from their crude biological source using an affinity technique. These include chitin binding protein CBP , maltose binding protein MBP , and glutathione S transferase GST . The poly histidine His tag is a widely used protein tag it binds to metal matrices. Solubilization tags are used, especially for recombinant proteins expressed in chaperone deficient species such as E. coli , to assist in the proper folding in proteins and keep them from precipitating. These include thioredoxin TRX and poly NANP . Some affinity tags have a dual role as a solubilization agent, such as MBP, and GST. Chromatography tags are used to alter chromatographic properties of the protein to afford different resolution across a particular separation technique. Often, these consist of polyanionic amino acids, such as FLAG tag . Epitope tags are short peptide sequences which are chosen because high affinity antibodies can be reliably produced in many different species. These are usually derived from viral genes, which explain their high immunoreactivity. Epitope tags include V5 tag , Myc c myc tag , and HA tag . These tags are particularly useful for western blotting and immunoprecipitation experiments, although they also find use in antibody purification. Fluorescence tags are used to give visual readout on a protein. GFP and its variants are the most commonly used fluorescence tags. More advanced applications of GFP include using it as a folding reporter fluorescent if folded, colorless if not . Protein tags find many other usages, such as specific enzymatic modification such as biotin ligase tags and chemical modification FlAsH tag. Often tags are co ... more details
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- Meganuclease
as homing endonucleases intron endonucleases and intein endonucleases. In nature, these proteins are coded by mobile genetic elements, intron s or intein s. Introns propagate by intervening at a precise ... intron or intein free allele . For inteins and group I introns, this break leads to the duplication of the intron or intein at the cutting site by means of the homologous recombination repair ... more details
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- Chemical ligation
Chemical ligation is a set of techniques used for creating long peptide or protein chains. It is the second step of a convergent synthesis convergent approach . First smaller peptides containing 30 50 amino acid s are prepared by conventional chemical peptide synthesis . They are then completely deprotected. Chemical ligation is the technique of coupling these peptides by chemoselective reaction to give a unique reaction product, usually in aqueous solution. With several coupling steps, proteins of up to 200 300 amino acid s can be produced. Methods of chemical ligation There are various techniques described in literature. The most practical and robust method for the chemoselective reaction of unprotected peptides is native chemical ligation . Native chemical ligation has overcome the limitations of the classical synthetic organic chemistry approach to the total synthesis of proteins, and enables the routine total or semi synthesis of protein molecules. The original chemical ligation methods involved the formation of a non native bond at the ligation site. Subsequently, native chemical ligation was developed. In native chemical ligation, an unprotected peptide thioester reacts with a Cys peptide to give a ligation product with a native amide peptide bond at the ligation site. In this method, the initial thioester linked ligation product intermediate rearranges to form an amide bond . Native chemical ligation relies on the presence of a cysteine residue at the ligation site. Methods using removable auxiliary groups can in some instances extend the use of native chemical ligation to non cysteine residues, as can the use of desulfurization subsequent to the ligation e.g. converting a Cys to an Ala . Expressed protein ligation By exploiting naturally occurring intein s it is possible to prepare a Recombinant DNA recombinant polypeptide C terminal thioester . This enables the use of large recombinant protein derived thioesters in native chemical ligation. The recombinant ... more details
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- List of biomolecules
Intein Interferon Inulin Ionomycin Ionone Isoleucine Iron sulfur cluster J Empty section date July ... more details
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- Native chemical ligation
also Peptide synthesis Protein synthesis Intein References cite journal author Wieland T, Bokelmann ... more details
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- LMO4
. title Stabilization of a binary protein complex by intein mediated cyclization. journal Protein Sci ... more details
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- List of restriction enzyme cutting sites
enzymes EcoRI , HindIII , BglII . Homing endonuclease . Intron s and intein s. Intragenomic conflict ... more details
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- Peptide bond
reactions such as those of intein s. When the functional group attacking the peptide bond is a thiol ... more details
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- Intragenomic conflict
splicing intron s group I & II and intein s. Inteins are internal protein fragments produced from ... more details
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- Tillman Gerngross
intein mediated protein purification using in vivo polyhydroxybutyrate PHB matrix association ... more details
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- List of homing endonuclease cutting sites
List of restriction enzyme cutting sites . Homing endonuclease . Restriction enzyme . Intron s and intein ... quote The Intein Database and Registry accessdate 2010 02 05 ref name pmid11752343 cite journal doi 10.1093 nar 30.1.383 author Perler FB title InBase the Intein Database journal Nucleic Acids Res volume ... more details
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- Protein primary structure
group. Intramolecular transesterification, resulting in a branched polypeptide. In intein s, the new ... more details
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- RNA splicing
, called intein s instead of introns, are removed. The remaining parts, called exteins instead of exons ... more details
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- Central dogma of molecular biology
themselves can be further spliced when this happens, the inside discarded section is known as an intein ... more details
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- Intron
fine structure Splicing Alternative splicing Minor spliceosome Function MicroRNA Others Intein ... more details
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- Index of biochemistry articles
membrane protein intein intercellular adhesion molecule 1 interferon receptor interferon type I ... more details
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- Sonic hedgehog
terminal domain acts as an intein and a cholesterol transferase. Another hydrophobic moiety chemistry ... more details
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- Protein
moz column width 15em column width 15em Cdx protein family Expression cloning Intein List of proteins ... more details
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- Chemical biology
intein biochemistry, thereby allowing the appendage of a synthetic N terminal peptide to the recombinantly ... more details
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