Iron-sulfur clusters are involved in post-translational arginylation

Verna Van, Janae B. Brown, Corin R. O’Shea, Hannah Rosenbach, Ijaz Mohamed, Nna-Emeka Ejimogu, Toan S. Bui, Veronika A. Szalai, Kelly N. Chacón, Ingrid Span, Fangliang Zhang and Aaron T. Smith ()
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Verna Van: University of Maryland, Baltimore County
Janae B. Brown: University of Maryland, Baltimore County
Corin R. O’Shea: University of Miami, Miller School of Medicine
Hannah Rosenbach: Heinrich-Heine-Universität Düsseldorf
Ijaz Mohamed: University of Maryland, Baltimore County
Nna-Emeka Ejimogu: University of Maryland, Baltimore County
Toan S. Bui: University of Maryland, Baltimore County
Veronika A. Szalai: National Institute of Standards and Technology
Kelly N. Chacón: Reed College
Ingrid Span: Heinrich-Heine-Universität Düsseldorf
Fangliang Zhang: University of Miami, Miller School of Medicine
Aaron T. Smith: University of Maryland, Baltimore County

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract Eukaryotic arginylation is an essential post-translational modification that modulates protein stability and regulates protein half-life. Arginylation is catalyzed by a family of enzymes known as the arginyl-tRNA transferases (ATE1s), which are conserved across the eukaryotic domain. Despite their conservation and importance, little is known regarding the structure, mechanism, and regulation of ATE1s. In this work, we show that ATE1s bind a previously undiscovered [Fe-S] cluster that is conserved across evolution. We characterize the nature of this [Fe-S] cluster and find that the presence of the [Fe-S] cluster in ATE1 is linked to its arginylation activity, both in vitro and in vivo, and the initiation of the yeast stress response. Importantly, the ATE1 [Fe-S] cluster is oxygen-sensitive, which could be a molecular mechanism of the N-degron pathway to sense oxidative stress. Taken together, our data provide the framework of a cluster-based paradigm of ATE1 regulatory control.

Date: 2023
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DOI: 10.1038/s41467-023-36158-z

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