Arginine methylation augments Sbp1 function in translation repression and decapping.

ABSTRACT: The fate of messenger RNA in cytoplasm plays a crucial role in various cellular processes. However, the mechanisms that decide whether mRNA will be translated, degraded or stored remain unclear. Single stranded nucleic acid binding protein (Sbp1), an Arginine-Glycine-Glycine (RGG-motif) protein, is known to promote transition of mRNA into a repressed state by binding eukaryotic translation initiation factor 4G1 (eIF4G1) and to promote mRNA decapping, perhaps by modulation of Dcp1/2 activity. Sbp1 is known to be methylated on arginine residues in RGG-motif; however, the functional relevance of this modification in vivo remains unknown. Here, we report that Sbp1 is arginine-methylated in an hnRNP methyl transferase (Hmt1)-dependent manner and that methylation is enhanced upon glucose depriva

SUBMITTER: Bhatter N 

PROVIDER: S-EPMC6916386 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature