Internal initiation of translation from the human rhinovirus-2 IRES requires the binding of Unr to two distinct sites on the 5' UTR
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. ISSN 0022-1317Full text not available from this repository.
Official URL: http://dx.doi.org/10.1099/vir.0.82463-0
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 > Life Sciences (2010- )|
|Journal or Publication Title:||Journal of General Virology|
|Publisher:||Society for General Microbiology|
|Official Date:||November 2007|
|Page Range:||pp. 3043-3052|
|Access rights to Published version:||Restricted or Subscription Access|
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