원문정보
초록
영어
Twin-Arginine translocation (Tat) pathway has been known with a unique cellular protein folding quality control mechanism in gram negative bacteria, which exports only correctly folded proteins across cytoplasmic membrane. Recently, we identified for the first time that a certain type of translocation intermediate of the recombinant Tat substrate is stably displayed on the surface of Escherichia coli. Furthermore, it was revealed that this display is dependent on a functional signal sequence and a folding efficiency of substrate. Taking advantage of the features of the display, a new protein engineering technology permitting simultaneous engineering of in vivo folding and affinity of proteins was exploited. This display technology should accelerate screening and engineering processes for the development of therapeutically valuable proteins such as single-chain variable fragment (scFv) and alternative binding scaffolds readily expressed in bacteria.