Cycloheximide and heat shock induce new polypeptide synthesis in Neurospora crassa.
Treatment of Neurospora crassa with 0.1 microgram of cycloheximide per ml, a concentration which inhibited protein synthesis by about 70%, resulted in the greatly enhanced synthesis of at least three polypeptide bands with estimated molecular weights of 88,000, 30,000, and 28,000. A temperature shift from 25 to 37 degrees C resulted in the appearance of a single new polypeptide band of 70,000 daltons, the same size as the major heat shock-induced proteins observed in species of Drosophila and Dictyostelium. Synthesis of the cycloheximide-stimulated polypeptide bands was on cytoplasmic ribosomes rather than on mitochondrial ribosomes, as incorporation of isotope into the polypeptide bands was inhibited by 1.0 microgram of cycloheximide per ml but not by 1 mg of chloramphenicol per ml. In a mutant with cycloheximide-resistant ribosomes, 0.1 microgram of cycloheximide per ml failed to alter the pattern of protein synthesis from that of the controls. It is suggested that the new synthesis of the polypeptide bands reflects specific mechanisms of adaptation to different kinds of environmental stress, including inhibition of protein synthesis and temperature increases.
D002701:Chloramphenicol / Q000494:pharmacology; D002940:Circadian Rhythm; D003513:Cycloheximide / Q000494:pharmacology*; D004351:Drug Resistance; D006360:Heat-Shock Proteins; D008970:Molecular Weight; D009491:Neurospora / Q000502:physiology*; D009492:Neurospora crassa / Q000502:physiology*; D014176:Protein Biosynthesis; D012270:Ribosomes / Q000502:physiology
D006360:Heat-Shock Proteins; D002701:Chloramphenicol; D003513:Cycloheximide