Prompt heat-shock and heat-shifted proteins associated with the nuclear matrix-intermediate filament scaffold in Drosophila melanogaster cells.

Elevated temperatures induced the synthesis of several new proteins in Drosophila melanogaster cells. Besides the conventional heat shock (HS) proteins, another set of temperature-induced proteins has been found. These latter resemble the prompt HS proteins of mammalian cells. The prompt HS proteins of Drosophila differ from the well-known conventional HS proteins in the following properties: (1) synthesis of the prompt HS proteins is insensitive to the transcription inhibitor actinomycin D, which blocks the appearance of conventional HS proteins; (2) induction of the prompt HS proteins requires a significantly higher temperature than conventional HS proteins; (3) prompt HS proteins associate strictly with the nuclear matrix-intermediate filament complex (NM-IF), while the conventional HS proteins are found in all subcellular fractions; (4) prompt HS proteins of Drosophila are induced by high temperature alone while the conventional HS proteins are also produced by a variety of stress conditions. Resinless-section electron micrographs show an altered nuclear matrix morphology in heat-shocked cells. The nuclear matrix fibers are altered in spatial distribution and have much additional electron-dense material. This added material probably reflects the soluble proteins shifted into the nuclear matrix at high temperature. The prompt HS proteins can be distinguished clearly from heat-shifted proteins by several criteria. Also, the prompt HS proteins are distinct from the heat-insensitive viral proteins of a persistent virus (HPS-1).