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Immediate response of the DnaK molecular chaperone system to heat shock
Author(s) -
Siegenthaler Rahel K.,
Grimshaw John P.A.,
Christen Philipp
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00190-5
Subject(s) - chaperone (clinical) , heat shock protein , hsp70 , heat shock , escherichia coli , biophysics , biology , microbiology and biotechnology , escherichia coli proteins , chemistry , biochemistry , gene , medicine , pathology
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.