Please use this identifier to cite or link to this item: https://doi.org/10.15480/882.1922
Publisher DOI: 10.1007/s00253-010-2628-x
Title: Inteins, valuable genetic elements in molecular biology and biotechnology
Language: English
Authors: Elleuche, Skander 
Pöggeler, Stefanie 
Keywords: intein;protein splicing;protein purification;cyclic proteins;selenoproteins
Issue Date: 7-May-2010
Publisher: Springer
Source: Applied microbiology and biotechnology 2 (87): 479-489 (2010-06)
Journal or Series Name: Applied microbiology and biotechnology 
Abstract (english): Inteins are internal protein elements that self-excise from their host protein and catalyze ligation of the flanking sequences (exteins) with a peptide bond. They are found in organisms in all three domains of life, and in viral proteins. Intein excision is a posttranslational process that does not require auxiliary enzymes or cofactors. This self-excision process is called protein splicing, by analogy to the splicing of RNA introns from pre-mRNA. Protein splicing involves only four intramolecular reactions, and a small number of key catalytic residues in the intein and exteins. Protein-splicing can also occur in trans. In this case, the intein is separated into N- and C-terminal domains, which are synthesized as separate components, each joined to an extein. The intein domains reassemble and link the joined exteins into a single functional protein. Understanding the cis- and trans-protein splicing mechanisms led to the development of intein-mediated protein-engineering applications, such as protein purification, ligation, cyclization, and selenoprotein production. This review summarizes the catalytic activities and structures of inteins, and focuses on the advantages of some recent intein applications in molecular biology and biotechnology.
URI: http://tubdok.tub.tuhh.de/handle/11420/1925
DOI: 10.15480/882.1922
ISSN: 1432-0614
Institute: Technische Mikrobiologie V-7 
Type: Sonstiges
Appears in Collections:Publications (tub.dok)

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