Reformation of nucleoli after ethione-induced fragmentation in the absence of significant protein synthesis.
The rat liver nucleolus, after fragmentation induced by ethionine treatment, has been found to undergo complete reformation by adenine in the presence of a dose of cycloheximide sufficient to cause inhibition of protein synthesis by 90-95%. In contrast, actinomycin D given along with adenine was followed by the appearance of a small compact mass containing only the fibrillar component with no evident granules. This structure resembled pseudonucleoli seen in the anucleolate mutant of Xenopus laevis or in certain early stages of amphibian oocytes. Actinomycin D administered 2 hr after adenine induced a segregation of the fibrillar and granular components of nucleoli similar to that induced in the normal nucleolus. The implications of these findings in relation to nucleolar organization are briefly discussed.
D000225:Adenine / Q000494:pharmacology; D000818:Animals; D002247:Carbon Isotopes; D002466:Cell Nucleolus / Q000187:drug effects / Q000378:metabolism*; D003513:Cycloheximide / Q000494:pharmacology; D003609:Dactinomycin / Q000494:pharmacology; D005001:Ethionine / Q000494:pharmacology; D005260:Female; D008099:Liver / Q000166:cytology* / Q000187:drug effects; D008854:Microscopy, Electron; D014176:Protein Biosynthesis; D012313:RNA / Q000096:biosynthesis*; D051381:Rats; D013997:Time Factors
D002247:Carbon Isotopes; D003609:Dactinomycin; D012313:RNA; D003513:Cycloheximide; D000225:Adenine; D005001:Ethionine