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Related Experiment Videos

Mutations in HIV reverse transcriptase which alter RNase H activity and decrease strand transfer efficiency are

C E Cameron1, M Ghosh, S F Le Grice

  • 1Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 24, 1997
PubMed
Summary
This summary is machine-generated.

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Deleting amino acids from HIV reverse transcriptase (RT) p51 subunit affects DNA stability and RNase H activity. Specific deletions impair DNA strand transfer, suggesting a role for RT-nucleocapsid protein complexes in viral DNA synthesis.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Virology

Background:

  • Structural studies indicate the p51 carboxyl terminus of HIV reverse transcriptase (RT) is crucial for RNase H activity.
  • Understanding RT structure-function relationships is key to developing antiviral therapies.

Purpose of the Study:

  • To investigate the impact of p51 carboxyl-terminal deletions on HIV RT activity.
  • To analyze the effects of these deletions on DNA polymerase, RNase H, and DNA strand transfer functions.
  • To explore the interaction between RT and nucleocapsid protein (NC).

Main Methods:

  • Purification of mutant HIV RT heterodimers with progressive deletions (5, 9, 13 amino acids) at the p51 carboxyl terminus.
  • Assays for RNA-dependent DNA polymerase activity, RNase H activity (using a labeled RNA/DNA hybrid), and DNA strand transfer.

Related Experiment Videos

  • Investigation of suppression of strand transfer defects by different forms of HIV nucleocapsid protein (NC).

    • Main Results:

    • Progressive deletions in the p51 terminus decreased the stability of the RT-DNA complex.
    • A 13-amino acid deletion (Delta13) significantly altered RNase H activity, increasing hydrolysis product length and shifting the spatial relationship between polymerase and RNase H active sites.
    • The Delta13 mutant showed impaired DNA strand transfer, which could be rescued by the 71-amino acid form of HIV NC.

    Conclusions:

    • The p51 carboxyl terminus plays a critical role in maintaining the stability and function of the RT-DNA complex.
    • Specific deletions in p51 disrupt the coordinated action of polymerase and RNase H activities, impacting proviral DNA synthesis.
    • Results suggest a specific interaction between HIV RT and NC, highlighting its importance in viral DNA synthesis.