[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 transformed 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.