A heat-sensitive cellular function located in the nucleolus.
Striking nucleolar lesions occur in cultured cells after exposure to supranormal temperatures. These lesions appear at 42 degrees C and consist of a loss of the granular ribonucleoprotein (RNP) component and intranucleolar chromatin, and a disappearance of the nucleolar reticulum. The material remaining in the morphologically homogeneous nucleolus is a large amount of closely packed fibrillar RNP. The lesions remain identical as temperature increases to 45 degrees C. These alterations are reversible when the cells are returned to 37 degrees C and are associated with the reappearance of an exaggerated amount of intranucleolar chromatin and granular RNP. High-resolution radioautography indicates that after thermic shock nucleolar RNA synthesis is inhibited whereas extranucleolar sites are preserved: it also suggests that the granular RNP is reconverted to fibrillar RNP probably by simple unraveling. The results prove the existence of heat-sensitive cellular functions in the nucleolus which deal with the DNA-dependent RNA synthesis. The precise site of action is assumed to involve hydrogen bonds, resulting in configurational changes in nucleolar RNP and affecting the stability of the DNA molecule. The subsequent events in nucleolar RNA synthesis are discussed in light of the morphologic and biochemical effects of actinomycin D on the nucleolus.
D000818:Animals; D001345:Autoradiography; D002466:Cell Nucleolus / Q000502:physiology*; D006224:Cricetinae; D046508:Culture Techniques; D004247:DNA / Q000378:metabolism; D004721:Endoplasmic Reticulum; D006651:Histocytochemistry; D006358:Hot Temperature; D008854:Microscopy, Electron; D009698:Nucleoproteins / Q000378:metabolism; D012313:RNA / Q000096:biosynthesis; D014316:Tritium; D014529:Uridine / Q000378:metabolism
D009698:Nucleoproteins; D014316:Tritium; D012313:RNA; D004247:DNA; D014529:Uridine