Reverse transcriptase-associated RNase H. Part IV. Pyrophosphate does not inhibit RNase H activity of AMV DNA polymerase

Arun Srivastava, Mukund J. Modak

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)892-899
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume91
Issue number3
DOIs
StatePublished - Dec 14 1979
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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