Immediate response of the DnaK molecular chaperone system to heat shock

The familiar heat shock response in cells comprises the enhanced expression of molecular chaperones. In recent experiments with the Hsp70 system of Escherichia coli, the co-chaperone GrpE has been found to undergo a reversible thermal transition in the physiological temperature range. Here, we tested whether this thermal transition is of functional significance in the complete DnaK/DnaJ/GrpE chaperone system. We found that a mere increase in temperature resulted in a higher fraction of fluorescence-labeled peptides being sequestered by DnaK. This direct adaptation of the DnaK/DnaJ/GrpE chaperone system to heat shock conditions may serve to bridge the time lag of enhanced chaperone expression.