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Bacteriophage T4 gp2 interferes with cell viability and with bacteriophage lambda Red recombination

K Appasani1, D S Thaler, E B Goldberg

  • 1Department of Molecular Biology and Microbiology, Tufts University Medical School, Boston, Massachusetts 02111-1800, USA.

Journal of Bacteriology
|February 11, 1999
PubMed
Summary

T4 phage protein gp2 kills bacteria by binding to double-stranded DNA termini. This binding protects phage DNA from degradation by exonuclease V, as shown by inhibited Red-mediated recombination.

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Area of Science:

  • Molecular Biology
  • Virology
  • Bacteriology

Background:

  • The T4 phage head protein gp2 is crucial for phage assembly and protects injected DNA from host exonucleases.
  • gp2 is a basic protein incorporated into the phage head, shielding DNA termini during infection.

Purpose of the Study:

  • To investigate the mechanism by which T4 gp2 protects phage DNA.
  • To elucidate the role of gp2 in bacterial cell death and recombination processes.

Main Methods:

  • Expressing recombinant gp2 in bacterial cells.
  • Comparing the effects of gp2 expression on Red-mediated and Int-mediated recombination pathways.
  • Analyzing bacterial survival rates post-gp2 expression.

Main Results:

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  • Recombinant gp2 expression leads to rapid bacterial cell death.
  • Red-mediated recombination, which requires double-stranded DNA termini, is significantly inhibited by gp2.
  • Int-mediated recombination, which does not require termini, is less affected by gp2.

Conclusions:

  • T4 gp2 kills bacteria by binding to double-stranded DNA termini.
  • This binding mechanism is likely responsible for protecting injected phage DNA from exonuclease V degradation.
  • gp2's action on DNA termini is analogous to Mu Gam protein's function.