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The RNA bacteriophages represent ideal model systems in which to probe the detailed assembly pathway for the formation of a T = 3 quasi-equivalent capsid. For MS2, the assembly reaction can be probed in vitro using acid disassembled coat protein subunits and a short (19 nt) RNA stem-loop that acts as the translational operator of the replicase gene and leads to sequence-specific sequestration and packaging of the cognate phage RNA in vivo. Reassembly reactions can be initiated by mixing these components at neutral pH. The molecular basis of the sequence-specific RNA–protein interaction is now well understood. Recent NMR studies on the protein demonstrate extensive mobility in the loops of the polypeptide that alter their conformations to form the quasi-equivalent conformers of the final capsid. It seems reasonable to assume that RNA binding results in reduction of this flexibility. However, mass spectrometry suggests that these RNA–protein complexes may only provide one type of quasi-equivalent capsid building block competent to form five-fold axes but not the full shell. Work with longer RNAs suggests that the RNA may actively template the assembly pathway providing a partial explanation of how conformers are selected in the growing shell.
Author(s): Stockley PG, Ashcroft AE, Francese S, Thompson GS, Ranson NA, Smith AM, Homans SW, Stonehouse NJ
Publication type: Article
Publication status: Published
Journal: Computational and Mathematical Methods in Medicine
Year: 2005
Volume: 6
Issue: 2
Pages: 119-125
ISSN (print): 1748-670X
ISSN (electronic): 1748-6718
Publisher: Hindawi Publishing Corporation
URL: http://dx.doi.org/10.1080/10273660500149869
DOI: 10.1080/10273660500149869
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