Internal initiation of translation from the human rhinovirus-2 internal ribosome entry site requires the binding of Unr to two distinct sites on the 5′ untranslated region

2007/10/18 by Emma Anderson, Emma C. Anderson, Sarah L. Hunt +1 · 17 citations
Medicine · Biochemistry, Genetics and Molecular Biology · #Viral Infections and Immunology Research #RNA and protein synthesis mechanisms #Viral gastroenteritis research and epidemiology

paper · doi:10.1099/vir.0.82463-0

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.

Citations

• All five cold-shock domains of unr (upstream of N- ras) are required for stimulation of human rhinovirus RNA translation

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