Sodium pyrophosphate, a known inhibitor of DNA polymerases, strongly inhibits DNA synthesis directed by various synthetic and natural template-primers and catalysed by reverse transcriptases from AMV and RLV, but has no effect on the reverse transcriptase-associated ribonuclease H activity. The synthesis of both actinomycin D sensitive and insensitive DNA under the direction of 70 S AMV RNA or globin mRNA with high or low concentrations of substrate triphosphates is inhibited by the addition of pyrophosphate but under none of these conditions, could RNase H activity be suppressed by inclusion of pyrophosphate. These studies further establish that the site for RNase H function is distinct from the substrate binding site and that the target for pyrophosphate action is not the RNase H (template binding site).
|Number of pages
|Biochemical and Biophysical Research Communications
|Published - Dec 14 1979
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology