Display Settings:

Format

Send to:

Choose Destination
Mol Cell. 2012 Jan 27;45(2):244-54. doi: 10.1016/j.molcel.2011.11.026.

Scd6 targets eIF4G to repress translation: RGG motif proteins as a class of eIF4G-binding proteins.

Author information

  • 1Department of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona 85721, USA.

Abstract

The formation of mRNPs controls the interaction of the translation and degradation machinery with individual mRNAs. The yeast Scd6 protein and its orthologs regulate translation and mRNA degradation in yeast, C. elegans, D. melanogaster, and humans by an unknown mechanism. We demonstrate that Scd6 represses translation by binding the eIF4G subunit of eIF4F in a manner dependent on its RGG domain, thereby forming an mRNP repressed for translation initiation. Strikingly, several other RGG domain-containing proteins in yeast copurify with eIF4E/G and we demonstrate that two such proteins, Npl3 and Sbp1, also directly bind eIF4G and repress translation in a manner dependent on their RGG motifs. These observations identify the mechanism of Scd6 function through its RGG motif and indicate that eIF4G plays an important role as a scaffolding protein for the recruitment of translation repressors.

Copyright © 2012 Elsevier Inc. All rights reserved.

PMID:
22284680
[PubMed - indexed for MEDLINE]
PMCID:
PMC3277450
Free PMC Article

Images from this publication.See all images (6)Free text

Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Write to the Help Desk