Article

 

Arginine methylation promotes translation repression activity of eIF4G-binding protein, Scd6. 公开 Deposited

https://scholar.colorado.edu/concern/articles/v692t6855
Abstract
  • Regulation of translation plays a critical role in determining mRNA fate. A new role was recently reported for a subset of RGG-motif proteins in repressing translation initiation by binding eIF4G1. However the signaling mechanism(s) that leads to spatial and temporal regulation of repression activity of RGG-motif proteins remains unknown. Here we report the role of arginine methylation in regulation of repression activity of Scd6, a conserved RGG-motif protein. We demonstrate that Scd6 gets arginine methylated at its RGG-motif and Hmt1 plays an important role in its methylation. We identify specific methylated arginine residues in the Scd6 RGG-motif in vivo We provide evidence that methylation augments Scd6 repression activity. Arginine methylation defective (AMD) mutant of Scd6 rescues the growth defect caused by overexpression of Scd6, a feature of translation repressors in general. Live-cell imaging of the AMD mutant revealed that it is defective in inducing formation of stress granules. Live-cell imaging and pull-down results indicate that it fails to bind eIF4G1 efficiently. Consistent with these results, a strain lacking Hmt1 is also defective in Scd6-eIF4G1 interaction. Our results establish that arginine methylation augments Scd6 repression activity by promoting eIF4G1-binding. We propose that arginine methylation of translation repressors with RGG-motif could be a general modulator of their repression activity.
Creator
Date Issued
  • 2016-11-02
Academic Affiliation
Journal Title
Journal Issue/Number
  • 19
Journal Volume
  • 44
File Extent
  • 9358-9368
Subject
Publisher
最新修改
  • 2019-12-05
Identifier
  • PubMed ID: 27613419
Resource Type
权利声明
DOI
ISSN
  • 1362-4962
Language

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