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Nucleic Acids Research, 1978, Vol. 5, No. 9 3325-3336
© 1978


Articles

Inhibition of mammalian RNA polymerase by 5,6-dichlororibofuranosylbenzimidazole (DRB) and DRB triphosphate

Christine Dreyer and Peter Hausen*

Max-Planck-Institut für Virusforschung, Abteilung für Zellbiologie 74 Tubingen, GFR

Received July 4, 1978.

DRB triphosphate inhibits activity of isolated RNA polymerase B, and, to a lesser extent, that of polymerase A. The same holds true for transcription in isolated nuclei. It does not act as an initiation inhibitor. In all cases, high concentrations of DRB triphosphate are required. Cells do not phosphorylate DRB to a measurable extent. hn RNA resistant to DRB is initiated with both ATP and GTP in the presence of the drug. These experiments render the hypothesis unlikely that DRB triphosphate in the cell specifically interferes with the initiation reaction of polymerase B.


*with the technical assistance of Karin Herrmann and Ursula Rössler


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