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Related Experiment Videos

Rous sarcoma virus integrase protein: mapping functions for catalysis and substrate binding

F D Bushman1, B Wang

  • 1Infectious Disease Laboratory, Salk Institute, La Jolla, California 92037.

Journal of Virology
|April 1, 1994
PubMed
Summary

Rous sarcoma virus integrase function is modular. Key activities for DNA strand transfer reside outside the N-terminal zinc-binding domain, unlike previously thought for retroviral integrases.

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Retroviruses like Rous sarcoma virus (RSV) integrate their DNA into host genomes using integrase enzymes.
  • Understanding integrase function is crucial for retroviral replication and potential therapeutic strategies.

Purpose of the Study:

  • To investigate the functional organization of Rous sarcoma virus (RSV) integrase.
  • To determine the roles of specific domains, including the HHCC motif, in RSV integrase activity.

Main Methods:

  • Construction and in vitro activity assays of deletion mutant RSV integrase derivatives.
  • Analysis of specific cleavage, DNA strand transfer, and disintegration reactions.

Main Results:

  • Deletion of the N-terminal HHCC zinc-binding motif or the C-terminal domain impaired cleavage and strand transfer.

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  • Mutants retaining the central domain could perform disintegration, suggesting catalysis occurs there.
  • Strand transfer activity was restored in N-terminal deletion mutants via peptide fusion, retaining substrate specificity.

    • Conclusions:

    • RSV integrase exhibits a modular organization, with catalytic and substrate recognition functions primarily located outside the N-terminal HHCC domain.
    • This modularity is conserved across retroviral integrases, including human immunodeficiency virus integrase.
    • Restoration of function via peptide fusion offers new insights into integrase mechanisms.