Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

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
Stable URL: http://www.jstor.org/stable/3059230
Page Count: 6
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Preview not available

Abstract

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.

Page Thumbnails

  • Thumbnail: Page 
9515
    9515
  • Thumbnail: Page 
9516
    9516
  • Thumbnail: Page 
9517
    9517
  • Thumbnail: Page 
9518
    9518
  • Thumbnail: Page 
9519
    9519
  • Thumbnail: Page 
9520
    9520