Anderson, Emma C., Hunt, Sarah L. and Jackson, Richard J. (2007) Internal initiation of translation from the human rhinovirus-2 IRES requires the binding of Unr to two distinct sites on the 5' UTR. Journal of General Virology, Vol.88 (No.11). pp. 3043-3052. doi:10.1099/vir.0.82463-0 ISSN 0022-1317.

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Abstract

Internal initiation of translation from the human rhinovirus-2 (HRV-2) internal ribosome entry site (IRES) is dependent upon host cell trans-acting factors. The multiple cold shock domain protein Unr and the polypyrimidine, tract-binding protein have been identified as synergistic activators of HRV-2 IRES-driven translation. In order to investigate the mechanism by which Unr acts in this process, we have mapped the binding sites of Unr to two distinct secondary structure domains of the HRV-2 IRES, and have identified specific nucleotides that are involved in the binding of Unr to the IRES. The data suggest that Unr acts as an RNA chaperone to maintain a complex tertiary IRES structure required for translational competency.

Item Type:	Journal Article
Subjects:	Q Science > Q Science (General)
Divisions:	Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title:	Journal of General Virology
Publisher:	Society for General Microbiology
ISSN:	0022-1317
Official Date:	November 2007
Dates:	Date Event November 2007 Published
Volume:	Vol.88
Number:	No.11
Page Range:	pp. 3043-3052
DOI:	10.1099/vir.0.82463-0
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access

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