tRNAArg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation.

Irem Avcilar-Kucukgoze, Howard Gamper, Christine Polte, Zoya Ignatova, Ralph Kraetzner, Michael Shtutman, Ya-Ming Hou, Dawei W Dong, Anna Kashina

Cell chemical biology 2020 Jul 16

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Arginyltransferase ATE1 mediates posttranslational arginylation and plays key roles in multiple physiological processes. ATE1 utilizes arginyl (Arg)-tRNAArg as the donor of Arg, putting this reaction into a direct competition with the protein synthesis machinery. Here, we address the question of ATE1- Arg-tRNAArg specificity as a potential mechanism enabling this competition in vivo. Using in vitro arginylation assays and Ate1 knockout models, we find that, in addition to full-length tRNA, ATE1 is also able to utilize short tRNAArg fragments that bear structural resemblance to tRNA-derived fragments (tRF), a recently discovered class of small regulatory non-coding RNAs with global emerging biological role. Ate1 knockout cells show a decrease in tRFArg generation and a significant increase in the ratio of tRNAArg:tRFArg compared with wild type, suggesting a functional link between tRFArg and arginylation. We propose that generation of physiologically important tRFs can serve as a switch between translation and protein arginylation. Copyright © 2020 Elsevier Ltd. All rights reserved.

Citation

Irem Avcilar-Kucukgoze, Howard Gamper, Christine Polte, Zoya Ignatova, Ralph Kraetzner, Michael Shtutman, Ya-Ming Hou, Dawei W Dong, Anna Kashina. tRNAArg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation. Cell chemical biology. 2020 Jul 16;27(7):839-849.e4