Asymmetric Arginine Dimethylation of Ribosomal Protein S2: Regulation of Translation
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چکیده
The subcellular localization of cytoplasmic mRNAs plays a significant role in controlling translation. In response to stress, eukaryotic cells quickly sequester “house-keeping” mRNAs to stress granules (SGs) in order to allow preferential translation of mRNAs that encode molecular chaperones and repair enzymes. SGs form when translation initiation is stalled: either the ternary complex becomes unavailable, or ribosomal recruitment is inhibited. In addition to mRNA, SGs contain 40S subunits, various translation initiation factors, and other RNA-binding proteins. Recently, it was shown that SGs contain RNA-binding proteins with asymmetrical dimethylarginines (ADMA). While this post-translation modification is associated with changes in protein activity and localization, when asymmetric arginine dimethylation occurs during stress and the functionality of ADMA in the context of SG assembly are questions that remain unanswered.
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