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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Rajyaguru P,She M,Parker Rdoi
10.1016/j.molcel.2011.11.026subject
Has Abstractpub_date
2012-01-27 00:00:00pages
244-54issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(11)00986-5journal_volume
45pub_type
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