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J Virol. 1983 July; 47(1): 249-252

Characterization of RNase H activity associated with reverse transcriptase in simian foamy virus type 1.

ABSTRACT

Spumavirinae or foamy viruses have been shown to have a characteristic RNA-dependent DNA polymerase activity. We demonstrate here the existence of an RNase H activity that copurifies with the 81-kilodalton monomeric polypeptide, which carries the RNA-dependent DNA polymerase activity of simian foamy virus type 1. RNase H degrades RNA hybrid substrates; however, it does not solubilize single-stranded RNAs. Inactivation assays with heat, high levels of bivalent cations, ethidium bromide, and sodium fluoride suggest that the RNase H catalytic site could be topologically independent from the DNA polymerase catalytic site.

This article has been cited by other articles:

• Baldwin, D. N., Linial, M. L. (1999). Proteolytic Activity, the Carboxy Terminus of Gag, and the Primer Binding Site Are Not Required for Pol Incorporation into Foamy Virus Particles. J. Virol. 73: 6387-6393 [Abstract] [Full Text]