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Dissecting the fine details of assembly of a T=3 capsid

Stockley, PG, Ashcroft, AE, Francese, S, Thompson, GS, Ranson, NA, Smith, AM, Homans, SW, Stonehouse, NJ (2005) Dissecting the fine details of assembly of a T=3 capsid. Journal of Theoretical Medicine, 6 . pp. 119-125. ISSN 1027-3662. (doi:10.1080/10273660500149869) (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) (KAR id:71819)

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.
Official URL:
http://dx.doi.org/10.1080/10273660500149869

Abstract

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.

Item Type: Article
DOI/Identification number: 10.1080/10273660500149869
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Gary Thompson
Date Deposited: 23 Jan 2019 17:43 UTC
Last Modified: 16 Nov 2021 10:26 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/71819 (The current URI for this page, for reference purposes)

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