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Halogenation of tyrosine perturbs large-scale protein self-organization

Author

Listed:
  • Huan Sun

    (Beijing Institute of Technology
    Technical University of Berlin)

  • Haiyang Jia

    (Beijing Institute of Technology
    Max Planck Institute of Biochemistry)

  • Olivia Kendall

    (Technical University of Berlin
    University of Edinburgh)

  • Jovan Dragelj

    (Technical University of Berlin)

  • Vladimir Kubyshkin

    (University of Manitoba)

  • Tobias Baumann

    (Technical University of Berlin)

  • Maria-Andrea Mroginski

    (Technical University of Berlin)

  • Petra Schwille

    (Max Planck Institute of Biochemistry)

  • Nediljko Budisa

    (Technical University of Berlin
    University of Manitoba)

Abstract

Protein halogenation is a common non-enzymatic post-translational modification contributing to aging, oxidative stress-related diseases and cancer. Here, we report a genetically encodable halogenation of tyrosine residues in a reconstituted prokaryotic filamentous cell-division protein (FtsZ) as a platform to elucidate the implications of halogenation that can be extrapolated to living systems of much higher complexity. We show how single halogenations can fine-tune protein structures and dynamics of FtsZ with subtle perturbations collectively amplified by the process of FtsZ self-organization. Based on experiments and theories, we have gained valuable insights into the mechanism of halogen influence. The bending of FtsZ structures occurs by affecting surface charges and internal domain distances and is reflected in the decline of GTPase activities by reducing GTP binding energy during polymerization. Our results point to a better understanding of the physiological and pathological effects of protein halogenation and may contribute to the development of potential diagnostic tools.

Suggested Citation

  • Huan Sun & Haiyang Jia & Olivia Kendall & Jovan Dragelj & Vladimir Kubyshkin & Tobias Baumann & Maria-Andrea Mroginski & Petra Schwille & Nediljko Budisa, 2022. "Halogenation of tyrosine perturbs large-scale protein self-organization," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32535-2
    DOI: 10.1038/s41467-022-32535-2
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    References listed on IDEAS

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    1. Jason W. Chin, 2017. "Expanding and reprogramming the genetic code," Nature, Nature, vol. 550(7674), pages 53-60, October.
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