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Related Experiment Videos

Functional interactions between SV40 T antigen and other replication proteins at the replication fork

Y Murakami1, J Hurwitz

  • 1Department of Molecular Biology, Memorial Sloan-Kettering Cancer Center, New York, New York 10021.

The Journal of Biological Chemistry
|May 25, 1993
PubMed
Summary

Simian virus 40 T antigen interacts with DNA replication machinery, slowing unwinding. Leading strand synthesis rate is limited by T antigen

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • SV40 DNA replication involves complex protein interactions at the replication fork.
  • Understanding these interactions is crucial for elucidating viral DNA replication mechanisms.

Purpose of the Study:

  • To investigate the functional interactions of SV40 T antigen with key replication proteins.
  • To determine the roles of these proteins in DNA unwinding and primer synthesis.

Main Methods:

  • Utilized purified components supporting SV40 DNA replication in vitro.
  • Examined protein association dynamics using dilution experiments.
  • Measured DNA unwinding and primer synthesis rates.

Main Results:

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  • SV40 T antigen remained associated with the replication fork, while pol alpha-primase dissociated during primer synthesis.
  • T antigen unwound DNA at 200 bp/min, a rate inhibited by pol alpha-primase, HSSB, and primase.
  • Leading strand synthesis by pol delta holoenzyme occurred at ~200 nt/min, limited by T antigen's unwinding rate.

    • Conclusions:

    • Pol alpha-primase interacts with T antigen and HSSB during unwinding, slowing T antigen movement.
    • SV40 DNA replication rate is limited by the DNA unwinding step catalyzed by T antigen.