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Papers In Press, published online ahead of print January 10, 2007
Biology Dept., Institute of Microbiology, University of Halle, Halle 06120
Corresponding Author: t.brueser{at}mikrobiologie.uni-halle.de
The Tat system from Escherichia coli transports folded proteins with N-terminal twin-arginine signal peptides across the cytoplasmic membrane. The influence of general chaperones on Tat substrate targeting has not been clarified so far. Here we show that the chaperones SlyD and DnaK bind to a broad range of different Tat signal sequences in vitro and in vivo. Initially, SlyD and GroEL were purified from DnaK-deficient extracts by their affinity to various Tat signal sequences. Of these, only SlyD bound Tat signal sequences also in the presence of DnaK. SlyD and DnaK also co-purified with Tat substrate precursors, demonstrating the binding to Tat signal sequences in vivo. Deletion of dnaK completely abolished Tat-dependent translocation of CueO, but not of DmsA, YcdB, or HiPIP, indicating that DnaK has an essential role specifically for CueO. DnaK was not required for stability of the CueO precursor and thus served in some essential step after folding. A CueO signal sequence fusion to HiPIP was Tat-dependently transported without the need of DnaK, indicating that the mature domain of CueO is responsible for the DnaK-dependence. The overall results suggest that SlyD and DnaK are in the set of chaperones which can serve as general Tat signal binding proteins. DnaK has additional functions which are indispensable for the targeting of CueO.
J. Biol. Chem, 10.1074/jbc.M608235200
Submitted on August 28, 2006
Revised on January 5, 2007
Accepted on January 10, 2007
DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone
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