PMID:15044009

Citation	Siegenthaler, RK, Grimshaw, JP and Christen, P (2004) Immediate response of the DnaK molecular chaperone system to heat shock. FEBS Lett. 562:105-10
Abstract	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.
Links	PubMed Online version:10.1016/S0014-5793(04)00190-5
Keywords	2-Naphthylamine/analogs & derivatives; 2-Naphthylamine/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Fluorescent Dyes/metabolism; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/metabolism; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/metabolism; Hot Temperature; Macromolecular Substances; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Peptides/metabolism
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