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Updated: Jan 24, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
Published on: June 30, 2013
RGG-motif self-association regulates eIF4G-binding translation repressor protein Scd6
Gopalakrishna Poornima1, Ravishankar Mythili1,2, Priyabrata Nag3
1a Department of Biochemistry, Indian Institute of Science , Bangalore , India.
Abstract:
Regulation of mRNA translation plays a key role in the control of gene expression. Scd6, a conserved RGG-motif containing protein represses translation by binding to translation initiation factor eIF4G1. Here we report that Scd6 binds itself in RGG-motif dependent manner and self-association regulates its repression activity. Scd6 self-interaction competes with eIF4G1 binding and methylation of Scd6 RGG-motif by Hmt1 negatively affects self-association. Results pertaining to Sbp1 indicate that self-association could be a general feature of RGG-motif containing translation repressor proteins. Taken together, our study reveals a mechanism of regulation of eIF4G-binding RGG-motif translation repressors.
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