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Iron-sulfur clusters are involved in post-translational arginylation



Verna Van, Janae Brown, Corin R. O’Shea, Hannah Rosenbach, Ijaz Mohamed, Nna-Emeka Ejimogu, Toan Bui, Veronika Szalai, Kelly Chacón, Ingrid Span, Aaron T. Smith


Eukaryotic arginylation is an essential post-translational modification that both modulates protein stability and regulates protein half-life through the N-degron pathway. Arginylation is catalyzed by a family of enzymes known as the arginyl-tRNA transferases (ATE1s), which are conserved across the eukaryotic domain. Despite its conservation and importance, little is known regarding the structure, mechanism, and regulation of ATE1s. In this work, we have discovered that ATE1s bind a previously unknown [Fe-S] cluster that is conserved across evolution. We have extensively characterized the nature of this [Fe-S] cluster, and we show that the presence of the [Fe-S] cluster is linked to alterations in arginylation efficacy. Finally, we demonstrate that the ATE1 [Fe-S] cluster is oxygen sensitive, which could be a molecular mechanism of the N-degron pathway to sense oxidative stress. Thus, our data provide the framework of a cluster-based paradigm of ATE1 regulatory control.
Nature Communications


iron sulfur cluster, arginylation, arginine transferase, N-degron pathway


Van, V. , Brown, J. , O’Shea, C. , Rosenbach, H. , Mohamed, I. , Ejimogu, N. , Bui, T. , Szalai, V. , Chacón, K. , Span, I. and Smith, A. (2023), Iron-sulfur clusters are involved in post-translational arginylation, Nature Communications, [online],, (Accessed July 12, 2024)


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Created January 28, 2023, Updated May 17, 2023