'Stress-proteins' are induced in Tetrahymena pyriformis by histidinol but not in mammalian (L-929) cells.

This study compares the influence of histidinol, a reversible inhibitor of growth and protein synthesis, on patterns of proteins synthesis in Tetrahymena pyriformis and cultured mouse L cells. In Tetrahymena, histidinol (10 mM) reduced total cell protein synthesis by over 60%. Analysis of individual protein bands by SDS-PAGE showed that at least 17 bands became less prominent, while 13 polypeptides became more prominent, during exposure to histidinol. These effects were rapidly reversed by addition of equivalent concentrations of histidine. Actinomycin D (actD) prevented the enhancement of most of the histidinol-'stimulated' bands, suggesting control at the transcriptional level. The majority of the histidinol-'stimulated' polypeptides appeared to be the same as corresponding heat-shock polypeptides, although some polypeptides were 'stimulated' by histidinol and not by heat shock, while others were 'stimulated' by heat shock and not by histidinol. 'Stimulation', both by histidinol and by heat shock, may reflect selective retention rather than induced synthesis of some or all of the relevant polypeptides. In contrast to Tetrahymena, cultured mouse L cells did not alter their normal polypeptide pattern under the influence of histidinol, under conditions in which total protein synthesis was depressed to a similar degree. It is possible that 'stress' proteins might be formed or retained in order to mediate adaptive responses of free-living cells to environmental changes.