Immediate response of the DnaK molecular chaperone system to heat shock

FEBS Letters

Christen, Philipp¹  Siegenthaler, Rahel K.¹  Grimshaw, John P.A.¹ 

[1] Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland

关键词: Molecular chaperone;    Hsp70;    DnaK;    Heat shock response;    GrpE;    Thermosensor;    a-NR;    acrylodan-labeled peptide NR (NRLLLTG);    a-p4;    acrylodan-labeled peptide p4 (CALLQSRLLS);    Hsp70;    70-kDa heat shock protein;   

DOI  :  10.1016/S0014-5793(04)00190-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown