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The three-dimensional structure of genomic RNA in bacteriophage MS2: implications for assembly.
The structures of recombinant MS2 capsids reveal clear density for bound RNA beneath the coat protein binding sites on the inner surface of the T=3 MS2 Capsid, and show that a short extension of the minimal assembly initiation sequence that promotes an increase in the efficiency of assembly, interacts with the protein capsid forming a network of bound RNA. Expand
A tiling approach to virus capsid assembly explaining a structural puzzle in virology.
  • R. Twarock
  • Biology, Medicine
  • Journal of theoretical biology
  • 21 February 2004
A novel approach for the description of the protein stoichiometry of viral capsids, that is the protein shells protecting the viral genome, is introduced based on tiling theory. This approachExpand
Affine extensions of the icosahedral group with applications to the three-dimensional organisation of simple viruses
This approach complements Caspar-Klug theory and provides details on virus structure that have not been accessible with previous methods, implying that icosahedral symmetry is more important for virus architecture than previously appreciated. Expand
Direct Evidence for Packaging Signal-Mediated Assembly of Bacteriophage MS2
Using cross-linking coupled to matrix-assisted laser desorption/ionization mass spectrometry and CLIP-Seq sequencing, we determined the peptide and oligonucleotide sequences at the interfaces betweenExpand
All-atom normal-mode analysis reveals an RNA-induced allostery in a bacteriophage coat protein.
  • E. Dykeman, R. Twarock
  • Chemistry, Medicine
  • Physical review. E, Statistical, nonlinear, and…
  • 10 March 2010
The results suggest that asymmetric contacts between the A -duplex RNA phosphodiester backbone of the stem loop with the EF loop in one coat protein subunit results in an increased dynamic behavior of its FG loop. Expand
Dynamic allostery controls coat protein conformer switching during MS2 phage assembly.
The vibrational modes of both TR-bound and RNA-free coat protein dimers using an all-atom normal-mode analysis suggest that asymmetric contacts between the A-duplex RNA phosphodiester backbone and the EF-loop in one coat protein subunit result in the FG-loop of that subunit becoming more dynamic, whilst the equivalent loop on the other monomer decreases its mobility. Expand
Simple rules for efficient assembly predict the layout of a packaged viral RNA.
It is shown that the organization of the viral genomes within the capsids provides intriguing insights into the highly cooperative nature of the assembly process of ssRNA viruses in vivo. Expand
The HBV RNA pre-genome encodes specific motifs that mediate interactions with the viral core protein that promote nucleocapsid assembly
Using RNA SELEX and bioinformatics, multiple regions in the pre-genomic RNA with high affinity for core protein dimers are identified that trigger sequence-specific assembly of virus-like particles (VLPs) at much higher fidelity and yield than in the absence of RNA. Expand
Structural constraints on the three-dimensional geometry of simple viruses: case studies of a new predictive tool.
This new concept in virus biology provides for the first time predictive information on the structural constraints on coat protein and genome topography, and reveals a previously unrecognized structural interdependence of the shapes and sizes of different viral components. Expand
Degenerate RNA packaging signals in the genome of Satellite Tobacco Necrosis Virus: implications for the assembly of a T=1 capsid.
Using a recombinant, T=1 Satellite Tobacco Necrosis Virus (STNV)-like particle expressed in Escherichia coli, conditions for in vitro disassembly and reassembly of the viral capsid are established and results are consistent with an assembly mechanism based on kinetically driven folding of the RNA. Expand