DnaK Chaperone Takes Part in Folding but Not in Refolding of Thermal Inactivated Proteins in Bacillus subtilis

The role of the DnaKJE and Trigger Factor (TF) chaperones in folding and refolding of proteins in Bacillus subtilis is studied. Bacterial luciferases of Photobacterium leiognathi and Photorhabdus luminescens as protein substrates have been used. It is shown that DnaKJE takes part in folding but not in refolding of the thermal inactivated proteins. It is shown that TF takes part in the synthesis of thermolabile P. leiognathi luciferase, but significantly decreases the level of synthesis of thermostable P. luminescens luciferase.