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Mutations in the RNase H Domain of HIV-1 Reverse Transcriptase Affect the Initiation of DNA Synthesis and the Specificity of RNase H Cleavage in vivo
John G. Julias, Mary Jane McWilliams, Stefan G. Sarafianos, Edward Arnold and Stephen H. Hughes
Proceedings of the National Academy of Sciences of the United States of America
Vol. 99, No. 14 (Jul. 9, 2002), pp. 9515-9520
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3059230
Page Count: 6
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Retroviral reverse transcriptases contain a DNA polymerase activity that can copy an RNA or DNA template and an RNase H activity that degrades the viral RNA genome during reverse transcription. RNase H makes both specific and nonspecific cleavages; specific cleavages are used to generate and remove the polypurine tract primer used for plus-strand DNA synthesis and to remove the tRNA primer used for minus-strand DNA synthesis. We generated mutations in an HIV-1-based vector to change amino acids in the RNase H domain that contact either the RNA and DNA strands. Some of these mutations affected the initiation of DNA synthesis, demonstrating an interdependence of the polymerase and RNase H activities of HIV-1 reverse transcription during viral DNA synthesis. The ends of the linear DNA form of the HIV-1 genome are defined by the specific RNase H cleavages that remove the plus- and minus-strand primers; these ends can be joined to form two-long-terminal repeat circles. Analysis of two-long-terminal repeat circle junctions showed that mutations in the RNase H domain affect the specificity of RNase H cleavage.
Proceedings of the National Academy of Sciences of the United States of America © 2002 National Academy of Sciences