Abstract
Chromatin of isolated nuclei from regenerating rat hepatocytes, 24 hr after partial hepatectomy, appeared mainly in the dispersed form. Exogenous ribonuclease (RNase) digestion of purified nuclei induced a marked condensation of extranucleolar chromatin, a quantitative reduction of ribonucleoprotein (RNP) perichromatin fibrils, and a solubilization of the heterogeneous nuclear (hn) RNA and of the small-molecular-weight (smw) RNAs contained in the RNP fibrils. Incubation of purified nuclei at 37°C for 30 min, when endogenous RNase was active, also caused a marked condensation of chromatin, but only a slight solubilization of rapidly labeled hnRNA without affecting the smwRNAs in the RNP fibrils. Both control and enzyme-treated nuclei presented the same quantity of RNA polymerase II molecules and the same transcriptional activity.
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