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Nucleic Acids Research, 1974, Vol. 1, No. 11 1549-1560
© 1974

Articles

Inhibition of poly(A) polymerase by rifamycin derivatives

Samson T. Jacob and Kathleen M. Rose

Department of Pharmacology, Milton S.Hershey Medical Center, Pennsylvania State University College of Medicine Hershey, Pennsylvania 17033, USA

Received September 11, 1974. The effect of several rifamycin derivatives on poly(A) synthesis in vitro was tested using purified rat liver mitochondrial poly(A) polymeraseassayed with an exogenous primer. When used at a concentration of 300 yg/ml, derivatives AF/013, PR/19, AF/AETP, M/88 and AF/ABDP completely inhibitedactivity corresponding to 50 ug of enzyme protein. Under similar conditions, derivatives DMAO and AF/MO failed to inhibit enzyme activity. Studies with PR/19 showed that the drug interacted directly with the enzyme molecule and did not affect the enzyme-primer complex formation. The inhibition by the drug could be reversed by increasing the substrate(ATP) concentration. It is concluded that some rifamycin derivatives can specifically inhibit template-independent nucleotlde chain elongationre actions.


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