Pyrophosphate analogues in pyrophosphorolysis reaction catalyzed by DNA polymerases

Abstract

It is demonstrated here that rat liver DNA polymerase β catalyzes the pyrophosphorolysis reaction with pyrophosphate (PP i) and its analogues. The substrate specificity of the PP i-binding site of several DNA polymerases was investigated. It was discovered that the ability of DNA polymerases to utilize PP i analogues instead of PP i 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 PP i-binding site of DNA polymerases.