Abstract
Heat shocks or cold shocks were found to induce characteristic changes in the pattern of protein synthesis in Tetrahymena pyriformis as analysed on sodium dodecyl sulphate (SDS)-polyacrylamide gels. Within 10 min the temperature shift-up induces increased incorporation of [ 35S]methionine into 4–5 protein bands, whereas incorporation into other bands is reduced, The heat-induced proteins appear to be metabolically stable, and no change in protein turnover could be detected at the elevated temperature. The protein induction is not observed when RNA synthesis is inhibited by actinomycin D. The temperature shift-down induces a different pattern of protein synthesis and there is no evidence of a common molecular mechanism underlying synchrony induction with heat shocks and cold shocks.
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