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Intein‐mediated protein ligation: Harnessing nature's escape artists
Author(s) -
Evans Thomas C.,
Xu MingQun
Publication year - 1999
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1999)51:5<333::aid-bip3>3.0.co;2-#
Subject(s) - intein , chemistry , ligation , protein evolution , microbiology and biotechnology , biophysics , biochemistry , gene , rna splicing , biology , rna
Inteins are naturally occurring proteins that are involved in the precise cleavage and formation of peptide bonds in a process known as protein splicing. Genetic engineering has allowed the controllable cleavage of peptide bonds at either the N‐ or C‐terminus of the intein. Inteins displaying controllable cleavage have been used in the isolation of bacterially expressed proteins possessing either a C‐terminal thioester or an N‐terminal cysteine. The specific placement of these reactive groups has allowed either protein–protein or protein–peptide condensation through a native peptide bond. This review describes the methods used to specifically generate these reactive groups on bacterially expressed proteins and some applications of this technique, known as intein‐mediated protein ligation. Furthermore, a versatile two intein (TWIN) system will be described which enables the circularization and polymerization of bacterially expressed proteins or peptides. © 2000 John Wiley & Sons, Inc. Biopoly 51: 333–342, 1999