Visualization by cryo-electron microscopy of genomic RNA that binds to the protein capsid inside bacteriophage MS2

J Mol Biol. 2003 Sep 12;332(2):415-22. doi: 10.1016/s0022-2836(03)00846-5.


The icosahedrally symmetrized structure of bacteriophage MS2 as determined by cryo-electron microscopy (EM) reveals the presence of genomic RNA that attaches to coat-protein dimers. Earlier X-ray diffraction studies revealed similar interactions between the unique operator hairpin of the MS2 genomic RNA and the coat-protein dimer. This observation leads us to conclude that not only the operator, but also many other RNA sequences in the genome of MS2, are able to bind to the coat-protein dimer. A substantial number of potential coat-protein-dimer binding sites are present in the genome of MS2 that can account for the observed RNA densities in the EM map. Moreover, it appears that these stem-loop structures are able to bind in a similar fashion to the coat protein dimer as the wild-type operator hairpin. The EM map also shows additional density between the potential operator-binding sites, linking the RNA stem-loops together to form an icosahedral network around the 3 and 5-fold axes. This RNA network is bound to the inside of the MS2 capsid and probably influences both capsid stability and formation, supporting the idea that capsid formation and RNA packaging are intimately linked to each other.

MeSH terms

  • Capsid Proteins / metabolism*
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Levivirus / chemistry*
  • Levivirus / isolation & purification
  • Models, Molecular
  • Nucleic Acid Conformation
  • RNA, Viral / chemistry*
  • RNA, Viral / metabolism


  • Capsid Proteins
  • RNA, Viral