The present study was to investigate the regulation of heat shock(HS) response and the role of HSP70 by monitoring HSP70 synthesis in Drosophila melanogaster tissues. When the salivary glands dissected from third instar larvae were heat-shocked at 37...
The present study was to investigate the regulation of heat shock(HS) response and the role of HSP70 by monitoring HSP70 synthesis in Drosophila melanogaster tissues. When the salivary glands dissected from third instar larvae were heat-shocked at 37℃ in the medium containing canavanine instead of arginine, transcription of HSP genes continued and canvanine-substituted HSP70 was accumulated in vast qualities. But if the synthesis of normal (arginine-incorporated) HSP70 was permitted, a specific quantity of functional HSP must accumulate before transcription of HSP genes was repressed. Also, in the case of actinomycin D treatment, HSPs must have accumulated before normal protein synthesis was restored. The HSP70 showed a binding capacity to RNA, however, analog substitution eliminated the binding potential of HSP70 to RNA. When the labeled salivary glands were chased at 24℃, the binding capacity to RNA was eliminated. In conclusion, it seemed that the level of HSPs synthesis was self-controlled posttranscriptionally and that HSP70 was bound to nuclear RNA during the HS or the initial part of recovery.