Pyrophosphate analogues in pyrophosphorolysis reaction catalyzed by DNA polymerases.

T Rozovskaya, N Tarussova, S Minassian, A Atrazhev, M Kukhanova, A Krayevsky, Z Chidgeavadze, R Beabealashvilli

Index: FEBS Lett. 247(2) , 289-92, (1989)

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Abstract

It is demonstrated here that rat liver DNA polymerase beta catalyzes the pyrophosphorolysis reaction with pyrophosphate (PPi) and its analogues. The substrate specificity of the PPi-binding site of several DNA polymerases was investigated. It was discovered that the ability of DNA polymerases to utilize PPi analogues instead of PPi in the pyrophosphorolysis reaction was markedly restricted. Only imidodiphosphate and methylenediphosphonate were demonstrated as participating in this process. Oxodiphosphonate and phosphonoformate inhibited DNA synthesis, but probably not via the interaction with the PPi-binding site of DNA polymerases.