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Phage phi29 DNA replication organizer membrane protein p16.7 contains a coiled coil and a dimeric,

Daniel Muñoz-Espín1, Mauricio G Mateu, Laurentino Villar

  • 1Instituto de Biología Molecular "Eladio Viñuela", Centro de Biología Molecular "Severo Ochoa", Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain.

The Journal of Biological Chemistry
|September 17, 2004
PubMed

Insights

The Bacillus subtilis phage p16.7 protein

Area of Science:

  • Molecular Biology
  • Virology
  • Structural Biology

Background:

  • Bacillus subtilis phage p16.7 is a membrane protein
  • It is involved in prokaryotic DNA replication
  • p16.7 has an N-terminal transmembrane domain for membrane localization

Purpose of the Study:

  • Characterize the dimerization and DNA-binding domains of p16.7
  • Investigate the functional significance of different p16.7 domains
  • Explore evolutionary relationships of p16.7 domains

Main Methods:

  • Protein expression and purification of p16.7 variants
  • Dimerization assays
  • DNA binding studies
  • Sequence analysis
  • Spectroscopic analyses

Main Results:

  • The N-terminal half of p16.7A forms a dimeric coiled coil
  • The C-terminal domain (p16.7C) is the primary dimerization domain
  • p16.7C binds to DNA and the phage varphi29 terminal protein
  • p16.7C shows evolutionary relation to eukaryotic homeodomains

Conclusions:

  • The C-terminal domain (p16.7C) is the functional unit of p16.7
  • p16.7C mediates dimerization, DNA binding, and terminal protein interaction
  • p16.7C's homology to homeodomains suggests a conserved DNA-binding mechanism

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