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Iron-sulfur clusters are involved in post-translational arginylation

Author

Listed:
  • 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
    University of Miami Miller School of Medicine)

  • Aaron T. Smith

    (University of Maryland, Baltimore County)

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.

Suggested Citation

  • 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 & Aaron T. Smith, 2023. "Iron-sulfur clusters are involved in post-translational arginylation," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36158-z
    DOI: 10.1038/s41467-023-36158-z
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    References listed on IDEAS

    as
    1. Rong-Gui Hu & Jun Sheng & Xin Qi & Zhenming Xu & Terry T. Takahashi & Alexander Varshavsky, 2005. "The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators," Nature, Nature, vol. 437(7061), pages 981-986, October.
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    Cited by:

    1. Thilini Abeywansha & Wei Huang & Xuan Ye & Allison Nawrocki & Xin Lan & Eckhard Jankowsky & Derek J. Taylor & Yi Zhang, 2023. "The structural basis of tRNA recognition by arginyl-tRNA-protein transferase," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Hongxia Chen & Xi Zhao & Wei Yang & Qi Zhang & Rongjiao Hao & Siao Jiang & Huihui Han & Zuyin Yu & Shuang Xing & Changjiang Feng & Qianqian Wang & Hao Lu & Yuanfeng Li & Cheng Quan & Yiming Lu & Gangq, 2023. "RNA N6-methyladenosine modification-based biomarkers for absorbed ionizing radiation dose estimation," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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