Roles of Aminoacyl tRNA synthetases in mRNA regulation
Aminoacyl tRNA synthetases (aaRSs) are a well-studied family of enzymes with a canonical role in charging tRNA with specific amino acid. Yet, these proteins appear to exert non-canonical roles, including post-transcriptional regulation. We performed a comprehensive analysis of mRNAs bound by almost all S. cerevisiae cytosolic aaRSs. Interestingly, we revealed that aaRSs preferential association with target mRNA that contains structure and modification mimicry of their cognate tRNAs. Point mutations that disassemble the anticodon mimic or the modification sites decrease aaRSs binding and affect the target mRNA translation. Together, our results reveal a novel post-transcriptional regulatory mechanism that exploits structure and modification mimicry to control mRNA translation according to tRNA charging demands
