Skip to main content
U.S. flag

An official website of the United States government

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.

Iron-sulfur clusters are involved in post-translational arginylation

Published

Author(s)

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

Abstract

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.
Citation
Nature Communications

Keywords

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

Citation

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], https://doi.org/10.1038/s41467-023-36158-z, https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=932333 (Accessed December 14, 2024)

Issues

If you have any questions about this publication or are having problems accessing it, please contact reflib@nist.gov.

Created January 28, 2023, Updated May 17, 2023