Heat and nutritional shock-induced proteins of the fungus Achlya are different and under independent transcriptional control

Abstract

When the temperature of exponentially growing cells of the coenocytic fungus Achlya klebsiana strain 1969 was suddenly elevated from 24 to 37 °C (thermal stress), synthesis of at least 12 preexisting proteins (heat-shock proteins, HSPs) was vigorously induced while synthesis of most other cell proteins declined transiently. After 2–3 h of thermal stress, the cells recovered and resumed normal protein synthesis. If the cells were first starved of nutrients (nutritional stress) before the temperature was raised to 37 °C, the same 12 HSPs were induced, but synthesis of both heat-shock-inducible and nonheat-shock proteins declined to trace levels after 4 h of thermal stress. Molecular weights (MW) of the HSPs were approximately 96 000a, 96 000b, 85 000, 72 000, 70 000, 69 000a, 69 000b, 68 000, 60 000, 52 000, 26 000a, and 26 000b, and they had similar isoelectric points (5.8–6.2). Nutritionally stressed cells showed an induced synthesis of some 28 proteins (nutritional stress proteins, NSPs), when they were not heat shocked, and an induced synthesis of 20 NSPs when heat shocked. In the presence of glutamine, nutritionally stressed cells induced the synthesis of 15 NSPs when they were not heat shocked and 17 NSPs when they were heat shocked. The NSPs and HSPs were electrophoretically different proteins. Glutamine did not affect the induction pattern of the HSPs, but it arrested reproductive development of starving cells while altering the pattern of NSP synthesis. Since actinomycin D inhibited the induced synthesis of HSPs and some NSPs, they may be under transcriptional control. In vitro translation of poly(A)+ RNAs from heat-shocked cells showed that these cells were rich in HSP mRNAs and poor in NSP mRNAs. We speculate that NSPs, but not HSPs, may play a role in reproductive development and sporulation in this fungus.