Abstract
The endogenous DNA-dependent RNA polymerase activity of rat ascites nucleoli was characterized in situ and compared with the activity assayed in whole nuclei and extranucleolar chromatin. Optimal activity of the nucleolar polymerase required Mg 2+ and low salt concentrations (0.08–0.10 M NaCl or 0.04 M (NH 4) 2SO 4). High salt (0.3–0.5 M NaCl or 0.3–0.4 M (NH 4) 2SO 4) inhibited the nucleolar polymerase activity but was stimulatory in whole nuclei and extranucleolar chromatin. The response of the nucleolar RNA polymerase to salt has some similarities to the bacterial polymerase system and suggests an enzyme pool not associated with the DNA template in nucleoli.
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