Summary information and primary citation
- PDB-id
-
2hua;
DSSR-derived features in text and
JSON formats
- Class
- RNA
- Method
- NMR
- Summary
- Solution structure of csfv ires domain iia
- Reference
-
Locker N, Easton LE, Lukavsky PJ (2007): "HCV and
CSFV IRES domain II mediate eIF2 release during 80S
ribosome assembly." Embo J.,
26, 795-805. doi: 10.1038/sj.emboj.7601549.
- Abstract
- Internal ribosome entry site (IRES) RNAs from the
hepatitis C virus (HCV) and classical swine fever virus
(CSFV) coordinate cap-independent assembly of eukaryotic
48S initiation complexes, consisting of the 40S ribosomal
subunit, eukaryotic initiation factor (eIF) 3 and the
eIF2/GTP/Met-tRNA(i)(Met) ternary complex. Here, we report
that these IRESes also play a functional role during 80S
ribosome assembly downstream of 48S complex formation, in
promoting eIF5-induced GTP hydrolysis and eIF2/GDP release
from the initiation complex. We show that this function is
encoded in their independently folded IRES domain II and
that it depends both on its characteristic bent
conformation and two conserved RNA motifs, an apical
hairpin loop and a loop E. Our data suggest a general mode
of subunit joining in HCV and HCV-like IRESes.
