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Nucleic Acids Research, 1995, Vol. 23, No. 14 2621-2625
© 1995

MOLECULAR BIOLOGY

Mutational analysis of the reverse transcriptase and ribonuclease H domains of the human foamy virus

Donat Kögel, Mordechal Aboud1 and Rolf M. Flügel*

Abteilung Retrovirale Genexpression, Angewandte Tumorivologie, Deutsches Krebsorschungszentrum 69009 Heidelberg, Germany 1Department of Microbiology and Immunology, Ben-Gurion University of the Negev Beer-Sheva, Israel

*To whom correspondence should be addressed

Received April 25, 1995. Accepted June 14, 1995.

Human foamy or spuma virus (HFV) codes for a distinct set of pol gene products. To determine the minimalrequirements for the HFV enzymatic activities, defined residues of the reverse transcriptase (RT) and ribonuclease H (RNase H) domain of the HFV pol gene were mutated by site-specific PCR mutagenesls. The mutant gene products were bacterially expressed, purified by Ni2+ chelate affinity chromatography and characterised by Western blotting. The enzymatic activities of the individual recombinant HFV pol mutant proteins were characterised by in situ RT, RNase H and RNase H* assays. Two substitution mutants reached RT activity levels higher than that of the intact recombinant HFV RT-RH-Hls. When the catalytically essential D508 was substituted by A508, 5% of RNase H activity was retained while ONA polymerase activity increased 2-fold. A deletion of 11 amlno acid residues In the hinge region completely abolished DNA polymerase while RNase H activity decreased 2-fold. A deletion mutant In the C-termlnal RH domain showed no RNase H but retained RNase H* activity indicating that the activities are genetically separable. The combined data reveal that the HFV DNA polymerase and RNase H activities are interdependent.


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D. N. Baldwin and M. L. Linial
Proteolytic Activity, the Carboxy Terminus of Gag, and the Primer Binding Site Are Not Required for Pol Incorporation into Foamy Virus Particles
J. Virol., August 1, 1999; 73(8): 6387 - 6393.
[Abstract] [Full Text]


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