HEAT-SHOCK GENE-EXPRESSION IN MURINE ERYTHROID-CELLS

The effect of the heat-shock stress factor on protein synthesis in Rauscher virus-transformed murine erythroblasts with blocked hemoglobin synthesis was studied. The most pronounced heat-shock protein (HSP) synthesis was observed at 43 and 45-degrees-C. Under conditions of heat shock the cells examined demonstrated enhanced (or new) synthesis of HSP with relative mol. mass of approximately 70-80 kD, approximately 50 kD and approximately 15-25 kD. No stable induction of 90 kD heat-shock protein was observed. The characteristic feature of transflormed erythroblasts was a sufficiently stable appearance of low-molecular HSP with mol. mass from 14 kD to 25 kD, among which there were proteins with relative mol. mass corresponding to that of globin chains.