Intein-mediated protein ligation: Harnessing nature's escape artists

✍ Scribed by Thomas C. Evans Jr.; Ming-Qun Xu

• Book ID: 101241162
• Publisher: Wiley (John Wiley & Sons)
• Year: 1999
• Tongue: English
• Weight: 175 KB
• Volume: 51
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(1999)51:5<333::aid-bip3>3.0.co;2-#

✦ Synopsis

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.