Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/41157
標題: Enhanced translocation of recombinant proteins via the Tat pathway with chaperones in Escherichia coil
作者: Lee, Y.F.
林松池
Hsieh, H.Y.
Tullman-Ercek, D.
Chiang, T.K.
Turner, R.J.
Lin, S.C.
關鍵字: Twin-arginine pathway
Green fluorescence protein
Secretion
DmsD
TorD
green fluorescent protein
leader-binding-protein
export pathway
signal peptide
transport pathway
coli
expression
bacteria
system
tord
期刊/報告no:: Journal of the Taiwan Institute of Chemical Engineers, Volume 41, Issue 5, Page(s) 540-546.
摘要: The twin-arginine translocation (Tat) pathway is capable of translocating folded proteins into the periplasm of Gram-negative bacteria and thus holds great potential for the expression of recombinant proteins in Escherichia coil. Nevertheless, this promise has been hampered by the low translocation efficiency. In this study, we demonstrate that the co-expression of DmsD, a system specific cytoplasmic chaperone similar to TorD, in conjunction with the DmsA signal peptide can enhance the translocation of the GFP fusion protein by 28.2%. We further show the presence of cross-activity between DmsD and TorD for the DmsA and TorA leader-fusions. The co-expression of DmsD and TorD enhances the translocation of ssTorA-GFP fusion and ssDmsA-GFP fusion by 28.6% and 46.6%, respectively. It was also observed that the co-expression of DmsD led to a reduction in the formation of GFP inclusion bodies, whereas the co-expression of TorD primarily led to a reduction in proteolysis by the Clp system. It is concluded that DmsD and TorD enhance protein translocation via the Tat pathway by providing activity against protein aggregation and/or proteolysis. (C) 2010 Taiwan Institute of Chemical Engineers. Published by Elsevier B.V. All rights reserved.
URI: http://hdl.handle.net/11455/41157
ISSN: 1876-1070
文章連結: http://dx.doi.org/10.1016/j.jtice.2010.01.004
Appears in Collections:化學工程學系所

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