Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome.

Abstract:

:During protein synthesis, ribosomes become stalled on polyproline-containing sequences, unless they are rescued in archaea and eukaryotes by the initiation factor 5A (a/eIF-5A) and in bacteria by the homologous protein EF-P. While a structure of EF-P bound to the 70S ribosome exists, structural insight into eIF-5A on the 80S ribosome has been lacking. Here we present a cryo-electron microscopy reconstruction of eIF-5A bound to the yeast 80S ribosome at 3.9 Å resolution. The structure reveals that the unique and functionally essential post-translational hypusine modification reaches toward the peptidyltransferase center of the ribosome, where the hypusine moiety contacts A76 of the CCA-end of the P-site tRNA. These findings would support a model whereby eIF-5A stimulates peptide bond formation on polyproline-stalled ribosomes by stabilizing and orienting the CCA-end of the P-tRNA, rather than by directly contributing to the catalysis.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Schmidt C,Becker T,Heuer A,Braunger K,Shanmuganathan V,Pech M,Berninghausen O,Wilson DN,Beckmann R

doi

10.1093/nar/gkv1517

subject

Has Abstract

pub_date

2016-02-29 00:00:00

pages

1944-51

issue

4

eissn

0305-1048

issn

1362-4962

pii

gkv1517

journal_volume

44

pub_type

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