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).
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Dec 14 1979|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology