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Iron-sulfur clusters are involved in post-translational arginylation
Verna Van1, Janae B Brown1, Corin R O'Shea2
1Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD, 21250, USA.
Nature Communications
|January 28, 2023
Summary
Eukaryotic arginyl-tRNA transferases (ATE1s) bind a novel [Fe-S] cluster, essential for their activity and linked to stress response. This oxygen-sensitive cluster may mediate oxidative stress sensing in the N-degron pathway.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- Arginylation is a crucial post-translational modification regulating protein stability and half-life in eukaryotes.
- Arginyl-tRNA transferases (ATE1s) catalyze arginylation but their structure, mechanism, and regulation remain poorly understood.
Purpose of the Study:
- To investigate the structure, mechanism, and regulation of arginyl-tRNA transferases (ATE1s).
- To identify novel regulatory mechanisms controlling ATE1 activity and its role in cellular processes.
Main Methods:
- Biochemical characterization of the [Fe-S] cluster in ATE1.
- In vitro and in vivo assays to assess arginylation activity.
- Analysis of the yeast stress response.
Main Results:
- A previously undiscovered [Fe-S] cluster conserved across evolution was identified in ATE1s.
- The presence of the [Fe-S] cluster is directly linked to ATE1's arginylation activity.
- The oxygen-sensitive nature of the ATE1 [Fe-S] cluster suggests a role in oxidative stress sensing.
Conclusions:
- A cluster-based regulatory paradigm for ATE1 function is proposed.
- The ATE1 [Fe-S] cluster is critical for enzyme activity and links arginylation to the yeast stress response.
- This finding provides a potential molecular mechanism for oxidative stress detection via the N-degron pathway.
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