Specific inhibition of DNA polymerase associated RNase H by DNA

Mukund Modak, S. L. Marcus

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The RNase H activity associated with several RNA-directed DNA polymerases is inhibited by the addition of DNA, in contrast to RNase H activity from enzymes devoid of polymerizing activity. Kinetic investigations of the inhibitory effect of DNA, using purified Rauscher leukemia virus DNA polymerase as a test enzyme, revealed that the addition of DNA to an ongoing RNase H reaction causes an immediate cessation of RNase H activity. Concomitant initiation of DNA synthesis directed by inhibitory DNA can occur, provided that appropriate substrate and primer is available. Thus, in addition to providing a simple test for the distinction between polymerase-associated and polymerase-independent RNase H activity, this study strongly supports the concepts that RNase H activity expressed by several mammalian oncoviral reverse trancriptases is an integral part of that molecule, and that the catalytic site of RNase H activity is also involved in template-primer binding.

Original languageEnglish (US)
Pages (from-to)243-246
Number of pages4
JournalJournal of Virology
Volume22
Issue number1
StatePublished - Jan 1 1977
Externally publishedYes

Fingerprint

Ribonuclease H
DNA-directed DNA polymerase
DNA-Directed DNA Polymerase
DNA
RNA-directed DNA polymerase
Rauscher Virus
enzymes
leukemia
active sites
polymerization
RNA-Directed DNA Polymerase
Enzymes
testing
triplex DNA
kinetics
viruses
Catalytic Domain
synthesis

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

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Specific inhibition of DNA polymerase associated RNase H by DNA. / Modak, Mukund; Marcus, S. L.

In: Journal of Virology, Vol. 22, No. 1, 01.01.1977, p. 243-246.

Research output: Contribution to journalArticle

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