Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase
Abstract
:1. Introduction
2. Results
2.1. Intracellular Measurements of Arginylation Using an Arginylation Sensor Plasmid
2.2. Intracellular Arginylation Depends on the Physiological State of the Cell but Does Not Compete with Active Translation
2.3. ATE1 Can Interact with the Long and Short RARS, but Overexpression of RARS Does Not Facilitate Arginylation
2.4. The ATE1–RARS Interaction Is tRNA-Independent
2.5. Displacement of the Long RARS from the MSC Increases Intracellular Arginylation
2.6. Displacement of RARS from the MSC Increases the Cytosolic Fraction of ATE1
3. Discussion
4. Materials and Methods
4.1. Materials
4.2. Total Protein Analysis and Cell Fractionation
4.3. Cell Treatments for Arginylation Sensor Measurements, Translation Inhibition and the Puromycylation Assay
4.4. Immunoprecipitation
4.5. Western Blotting
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Avcilar-Kucukgoze, I.; MacTaggart, B.; Kashina, A. Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase. Int. J. Mol. Sci. 2022, 23, 10160. https://doi.org/10.3390/ijms231710160
Avcilar-Kucukgoze I, MacTaggart B, Kashina A. Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase. International Journal of Molecular Sciences. 2022; 23(17):10160. https://doi.org/10.3390/ijms231710160
Chicago/Turabian StyleAvcilar-Kucukgoze, Irem, Brittany MacTaggart, and Anna Kashina. 2022. "Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase" International Journal of Molecular Sciences 23, no. 17: 10160. https://doi.org/10.3390/ijms231710160