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
关联
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arginineMethylationPromotesTranslationRepressionActivityOf.pdf | 2019-12-05 | 公开 | 下载 |