Iron-sulfur clusters are involved in post-translational arginylation

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

doi:10.1038/s41467-023-36158-z

Iron-sulfur clusters are involved in post-translational arginylation

Journal Article · Fri Jan 27 23:00:00 EST 2023 · Nature Communications

DOI:https://doi.org/10.1038/s41467-023-36158-z· OSTI ID:2423911

Van, Verna ^[1]; ^[1]; ^[2]; Rosenbach, Hannah ^[3]; Mohamed, Ijaz ^[1]; ^[1]; Bui, Toan S. ^[1]; Szalai, Veronika A. ^[4]; ^[5]; ^[3]; Zhang, Fangliang ^[2]; ^[1]

Univ. of Maryland Baltimore County (UMBC), Baltimore, MD (United States)
Univ. of Miami, FL (United States)
Heinrich-Heine-Universität Düsseldorf (Germany)
National Inst. of Standards and Technology (NIST), Gaithersburg, MD (United States)
Reed College, Portland, OR (United States)

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.

View Accepted Manuscript (DOE)

Research Organization:: SLAC National Accelerator Laboratory, Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Institutes of Health (NIH); German Research Foundation (DFG)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 2423911

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 14; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
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Iron-sulfur clusters are involved in post-translational arginylation

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