The cellular response to stress includes synthesis of specific stress
proteins in the presence of a generalized suppression of protein synth
esis. The response occurs in intact animals, individually stressed org
ans of intact animals, donor organs upon removal, regardless of preser
vation methods, and cells in culture. The molecular biology of stress
protein induction is not understood. While stress proteins are benefic
ial, overall suppression of protein synthesis, if prolonged, is harmfu
l. Since altered energy metabolism is integral to stress induction, we
examined the mitochondria to determine if they could provide a possib
le molecular mechanism for initiating the response. Rat myoblasts were
incubated at varying temperatures for up to 120 min in [S-35]methioni
ne. Proteins were separated electrophoretically and newly synthesized
proteins visualized autoradiographically. Isolated mitochondria from r
esting rat myoblasts were then stressed, label incorporation determine
d, and newly synthesized protein was visualized. Stress sharply suppre
ssed protein synthesis in mitochondria but autoradiograms of stressed
mitochondria showed that a single stress protein of 18 kDa was synthes
ized. Mitochondria independently respond to stress and synthesize a st
ress protein from their own DNA. This protein may provide an intermedi
ary pathway that links stressful conditions in the environment to the
overall response observed in the cell. (C) 1996 Academic Press, Inc.