Halogenation of tyrosine perturbs large-scale protein self-organization

Huan Sun, Haiyang Jia (), Olivia Kendall, Jovan Dragelj, Vladimir Kubyshkin, Tobias Baumann, Maria-Andrea Mroginski (), Petra Schwille () and Nediljko Budisa ()
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Huan Sun: Beijing Institute of Technology
Haiyang Jia: Beijing Institute of Technology
Olivia Kendall: Technical University of Berlin
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

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-32535-2

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