In most organisms, the synthesis of heat shock proteins is a transient physiological change in the cell exposed to supra-optimal temperatures. The physiological response to heat shock is particularly dependent on the cell type and on the capacity of the organisms to respond to environmental alterations. In this study the mycelial growth and synthesis of heat shock proteins of two Pisolithus isolates (RV82 and RS24) and one Paxillus involutus isolate to supra-optimal temperatures was evaluated. Mycelial growth was evaluated under sublethal, lethal and heat shock temperature conditions with appropriate growth medium on Petri plates. Proteins in the mycelium of the isolates were marked using radioactive amino acid (³H-leucine) and the radioactivity was quantified in scintillation solution. Synthesis of heat shock proteins (HSPs) were evaluated by polyacrylamide gels (SDS-PAGE and 2D-PAGE). The two Pisolithus isolates RS24 and RV82 were more tolerant to high temperatures than P. involutus. The Pisolithus isolates differed regarding the synthesis of stress proteins since high and low molecular mass proteins were synthesized. In response to the heat shock, the RV82 isolate synthesized putative heat shock proteins of the groups HSP70, HSP28, HSP26 and sHSPs (15-18 kDa), while the RS24 isolate synthesized putative heat shock proteins of the groups HSP86, HSP60, HSP55, HSP35 and sHSPs (12-18 kDa). The low heat tolerance of the P. involutus isolate was attributed to its incapacity of synthesizing HSPs. Our results suggest that the induction of the thermotolerance mechanism differs among ectomicorrhizal fungi isolates.
heat stress; heat shock proteins; HSPs; Pisolithus sp.; Paxillus involutus
