Oligomeric structures of the phage phi29 histone-like protein p6

J Mol Biol. 1999 Sep 24;292(3):581-8. doi: 10.1006/jmbi.1999.3078.


Protein p6 of Bacillus subtilis phage phi29 has been described as a histone-like protein, playing a role in genome organization and compaction, on the basis of its high intracellular abundance, its pleiotropic effect, and its ability to bind and highly compact the whole phi29 DNA in vitro. Protein p6 forms large multimeric nucleoprotein complexes in which a right-handed superhelical DNA wraps toroidally around the protein core. Analytical ultracentrifugation analysis, at the concentration estimated in vivo (at least 1 mM), showed that protein p6 self-associates into elongated oligomers, suggesting that, in the absence of DNA, the protein could form a scaffold for DNA binding. In this work we have studied the structure of these oligomers by transmission electron microscopy and image processing. The results show that protein p6 aggregates into crooked-shaped oligomers, compatible with a helical structure. The oligomers could interact head-to-tail to form doughnut-shaped structures or they could grow into right-handed double-helical filaments by a nucleation-dependent polymerization process. The dimensions of the crooked-shaped structures are in agreement with that of the DNA in the nucleoprotein complex previously described. We propose that the crooked-shaped structures could act as a scaffold imposing the right-handed path followed by the DNA, and thus it could be considered a non-transient DNA chaperone.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacillus Phages / chemistry*
  • Bacillus subtilis / virology*
  • Cross-Linking Reagents / chemistry
  • DNA, Superhelical / chemistry
  • DNA, Viral / chemistry
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / ultrastructure
  • Glutaral / chemistry
  • Image Processing, Computer-Assisted
  • Microscopy, Electron
  • Nucleoproteins / chemistry
  • Protein Conformation
  • Ultracentrifugation
  • Viral Proteins / chemistry*
  • Viral Proteins / ultrastructure


  • Cross-Linking Reagents
  • DNA, Superhelical
  • DNA, Viral
  • DNA-Binding Proteins
  • Nucleoproteins
  • Viral Proteins
  • viral protein p6
  • Glutaral