Objective
Bacteria export numerous proteins across the plasma membrane and this process has been heavily exploited for protein production on an industrial scale. However, the standard 'general secretory pathway' transports proteins in an unfolded state and is inapplicable for the export of the majority of cytosolic and heterologous proteins because of their tendency to fold prematurely. Recent studies, primarily by this partnership, have revealed the operation of a novel bacterial protein export system that recognises signal pepetides bearing twin-arginine motifs (RR-SIGNAL PEPTIDES) and which has the remarkable ability to export large, fully-folded proteins. Critically, RR-signal pepetides direct the export of several heterologous proteins and this application is aimed at the exploitation of this twin-arginine translocation (Tat) system to export active, high value-added proteins from Escherichia coli and Bacillus subtilis. We propose to engineer RR-signal peptides capable of directing highly specific and efficient export in these organisms, and to produce super-exporting stains capable of exporting heterolohous proteins on a commercial scale.
Fields of science
Call for proposal
Data not availableFunding Scheme
CSC - Cost-sharing contractsCoordinator
9712 CP GRONINGEN
Netherlands