Please use this identifier to cite or link to this item:
|標題:||Coexpression of TorD enhances the trans-port of GFP via the TAT pathway||作者:||Li, S.Y.
|關鍵字:||twin-arginine pathway;green fluorescence protein;secretion;TorD;green fluorescent protein;arginine translocation pathway;high-level;expression;escherichia-coli;signal peptide;export pathway;complex;system;bacteria;identification||Project:||Journal of Biotechnology||期刊/報告no：:||Journal of Biotechnology, Volume 122, Issue 4, Page(s) 412-421.||摘要:||
Twin-arginine translocation (Tat) pathway is capable of secreting fully folded proteins into the periplasm, of Gram-negative bacteria and may thus be an ideal system for the expression of active cofactor-containing proteins. However, the applications of Tat system for such purpose have been plagued by low translocation efficiencies. In this study, we demonstrate that the coexpression of a soluble chaperone, TorD, in conjunction with the TorA signal peptide, the translocation efficiency of GFP can be enhanced by more than three-fold. The enhancement in translocation efficiency is believed to be a result of reduced proteolysis mediated by the binding of TorD toward the TorA signal peptide. We believe this approach can be further exploited for the expression and secretion of other heterologous proteins as well as traditional Tat substrate proteins. (c) 2005 Elsevier B.V. All rights reserved.
|Appears in Collections:||化學工程學系所|
Show full item record
TAIR Related Article
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.