The beta hairpin structure within ribosomal protein S5 mediates interplay between domains II and IV and regulates HCV IRES function.

ABSTRACT: Translation initiation in Hepatitis C Virus (HCV) is mediated by Internal Ribosome Entry Site (IRES), which is independent of cap-structure and uses a limited number of canonical initiation factors. During translation initiation IRES-40S complex formation depends on high affinity interaction of IRES with ribosomal proteins. Earlier, it has been shown that ribosomal protein S5 (RPS5) interacts with HCV IRES. Here, we have extensively characterized the HCV IRES-RPS5 interaction and demonstrated its role in IRES function. Computational modelling and RNA-protein interaction studies demonstrated that the beta hairpin structure within RPS5 is critically required for the binding with domains II and IV. Mutations disrupting IRES-RPS5 interaction drastically reduced the 80S complex formation and th

SUBMITTER: Bhat P 

PROVIDER: S-EPMC4357715 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature