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


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.

SUBMITTER: Poornima G 

PROVIDER: S-EPMC6693564 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature

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

Poornima Gopalakrishna G   Mythili Ravishankar R   Nag Priyabrata P   Parbin Sabnam S   Verma Praveen Kumar PK   Hussain Tanweer T   Rajyaguru Purusharth I PI  

RNA biology 20190612 9


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 s  ...[more]

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