Characterizing the interactome of human Arginyl-tRNA Synthethase
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ABSTRACT: Prior work revealed nuclear-localized aminoacyl-tRNA synthetases (aaRSs) that checked newly synthesized tRNAs for charging before export to the cytoplasm. To reveal other functions, we sought to identify nuclear proteins that interact with arginyl-tRNA synthetase (ArgRS) in the nucleus. Serine/Arginine Repetitive Matrix Protein 2 (SRRM2), which is stored with RNA splicing apparatus components in nuclear speckle condensates, was found as a consistent interaction partner that co localized with SRRM2 ArgRS in nuclear speckles. Dynamic photo-bleaching experiments showed that, consistent with condensate properties, SRRM2 has a fluctuating appearance in speckles. Knock down of ArgRS impeded SRRM2 speckle trafficking and, coincidently, altered splicing processing of pre-mRNA transcripts. Among the altered spliced variants, those of tRNA synthetase family members were prominent. Thus, nuclear ArgRS shapes the dynamics of a protein in class of nuclear condensates. Also, the work expands the repertoire of nuclear tRNA synthetase roles to include regulation of RNA splicing, including of aaRS family member transcripts.
INSTRUMENT(S): Q Exactive
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Permanent Cell Line Cell, Cell Culture
SUBMITTER: Haissi Cui
LAB HEAD: Paul Schimmel
PROVIDER: PXD015692 | Pride | 2023-04-14
REPOSITORIES: Pride
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