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A simple, RNA-mediated allosteric switch controls the pathway to formation of a T=3 viral capsid

Stockley, PG, Rolfsson, O, Thompson, GS, Basnak, G, Francese, S, Stonehouse, NJ, Homans, SW, Ashcroft, AE (2007) A simple, RNA-mediated allosteric switch controls the pathway to formation of a T=3 viral capsid. Journal of Molecular Biology, 369 . pp. 541-552. ISSN 0022-2836. (doi:10.1016/j.jmb.2007.03.020) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1016/j.jmb.2007.03.020

Abstract

Using mass spectrometry we have detected both assembly intermediates and the final product, the T = 3 viral capsid, during reassembly of the RNA bacteriophage MS2. Assembly is only efficient when both types of quasiequivalent coat protein dimer seen in the final capsid are present in solution. NMR experiments confirm that interconversion of these conformers is allosterically regulated by sequence-specific binding of a short RNA stem-loop. Isotope pulse-chase experiments confirm that all intermediates observed are competent for further coat protein addition, i.e., they are all on the pathway to capsid formation, and that the unit of capsid growth is a coat protein dimer. The major intermediate species are dominated by stoichiometries derived from formation of the particle threefold axis, implying that there is a defined pathway toward the T=3 shell. These results provide the first experimental evidence for a detailed mechanistic explanation of the regulation of quasiequivalent capsid assembly. They suggest a direct role for the encapsidated RNA in assembly in vivo, which is consistent with the structure

Item Type: Article
DOI/Identification number: 10.1016/j.jmb.2007.03.020
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: G. Thompson
Date Deposited: 23 Jan 2019 17:38 UTC
Last Modified: 30 May 2019 08:47 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/71817 (The current URI for this page, for reference purposes)
Thompson, GS: https://orcid.org/0000-0001-9399-7636
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