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RGG-motif self-association regulates eIF4G-binding translation repressor protein Scd6

Version 3 2019-10-09, 07:55
Version 2 2019-06-12, 08:38
Version 1 2019-06-03, 12:56
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posted on 2019-10-09, 07:55 authored by Gopalakrishna Poornima, Ravishankar Mythili, Priyabrata Nag, Sabnam Parbin, Praveen Kumar Verma, Tanweer Hussain, Purusharth I Rajyaguru

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.

Funding

This work was supported by Wellcome Trust/DBT India Alliance [IA/I/12/2/500625], Department of Biotechnology [BT/PR13267/BRB/10/1444/2015] and DBT-IISc partnership in PIR lab. TH was supported by Wellcome Trust/DBT India Alliance [IA/I/17/2/503313] and IISc start-up funds [R(IV)090/1076/2017-4252].

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