Translational control of protein synthesis in response to heat shock in D. melanogaster cells.

In response to elevated temperature, Drosophila cells synthesize a small set of proteins known as the heat-shock proteins, while synthesis of most other proteins ceases. In vitro translation has been used to demonstrate that the messenger RNAs encoding the normal (25 degrees) spectrum of proteins are not broken down or irreversibly inactivated in response to the temperature change. During the heat shock only the heat-shock mRNAs plus a small number of preexisting mRNAs are translated, while most other messages are stored and can be reactivated upon return of the cells to their normal temperature. After recovery from heat shock, cells translate both the normal mRNA and the remaining heat-shock mRNA. The translational control operating in intact cells has been reproduced in cell-free translation systems directed by purified mRNA from normal and heat-shocked cells. Lysates prepared from heat-shocked Drosophila cells preferentially translated the heat-shock messages, while the lysate made from normally growing Drosophila cells indiscriminately translated both normal and heat-shock messages. Therefore there must be stable alterations in the translational components of heat-shocked cells which are capable of causing selective translation of the heat-shock messages. In addition there must be information encoded in the heat-shock messages that allows their selection.