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Reverse transcriptase: correlation of zinc content with activity.

B J Poiesz, G Seal, L A Loeb

    Proceedings of the National Academy of Sciences of the United States of America
    |December 1, 1974
    PubMed
    Summary
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    Avian myeloblastosis virus DNA polymerase requires zinc for activity. This zinc metalloenzyme can be selectively inhibited by chelators, offering potential therapeutic strategies against oncogenic viruses.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Virology

    Background:

    • DNA polymerase is crucial for viral replication.
    • Previous studies suggested avian myeloblastosis virus (AMV) DNA polymerase contains zinc.
    • The precise role of zinc in AMV DNA polymerase activity remained unclear.

    Purpose of the Study:

    • To investigate the obligatory zinc requirement for AMV DNA polymerase activity.
    • To determine if AMV DNA polymerase is a zinc metalloenzyme.
    • To explore selective inhibition of viral DNA polymerases.

    Main Methods:

    • Using radioactive zinc (65Zn) to trace enzyme-bound zinc.
    • Employing isoelectric focusing to localize zinc and polymerase activity.
    • Inactivating the enzyme with the chelator 1,10-phenanthroline.

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  • Assessing the restoration of activity by adding Zn(2+).

    • Main Results:

    • Enzyme-bound zinc was found to be exchangeable with 65Zn.
    • Radioactive zinc was coincident with polymerase activity after isoelectric focusing.
    • Chelation with 1,10-phenanthroline inactivated the enzyme and removed zinc.
    • Inactivation was reversible upon addition of Zn(2+).
    • AMV DNA polymerase showed faster inactivation by 1,10-phenanthroline compared to bacterial and animal polymerases.

    Conclusions:

    • Avian myeloblastosis virus DNA polymerase is a zinc metalloenzyme.
    • The enzyme's activity is strictly dependent on zinc.
    • Selective inactivation of viral DNA polymerases using metal chelators is feasible.