How cells work with "Lego® bricks"
Scientists from Saarland University, RPTU Kaiserslautern-Landau, VIB-VUB Brussels and cooperating institutions have discovered that important enzymes in our cells, so-called peroxiredoxins, can be combined more flexibly than previously assumed. The discovery shows how cells can create molecular diversity and fine-tune stress responses.
Peroxiredoxins have protective and regulatory functions by controlling the levels of peroxides such as hydrogen peroxide. For more than 20 years, researchers assumed that these enzymes form complexes of ten identical protein units arranged in a donut-like structure. However, the study now published shows that cells can instead mix two versions of the enzyme together to form hybrid protein complexes.
By combining two building blocks with different properties, cells can form many different protein complexes and thus generate a wide variety of molecular structures and functions from just two building blocks. Using biochemical and imaging methods, the researchers were able to determine that this mixing takes place in organisms ranging from yeasts and humans to plants and parasites.
The researchers emphasize that this "molecular Lego®" strategy could help cells to fine-tune stress responses and signaling pathways. Understanding how these mixed complexes work could provide new insights into how cells adapt to living with oxygen and how diseases develop in which the oxidative balance in the cell is disturbed, including ageing, cancer and metabolic disorders.
The study:
"Heterooligomerization drives structural plasticity of eukaryotic peroxiredoxins", has been published in the journal "Nature Chemical Biology". The DOI is:
https://doi.org/10.1038/s41589-026-02157-6
Scientific contacts:
Marcel Deponte
Comparative Biochemistry
Department of Chemistry
RPTU Kaiserslautern-Landau
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Bruce Morgan
Institute of Biochemistry
Center for Human and Molecular Biology (ZHMB)
Saarland University
E bruce.morgan[at]uni-saarland.de
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Joris Messens
VIB-VUB Center for Structural Biology
Brussels
Peroxiredoxin heteroassemblies are distributed over a negative contrast electron microscopy grid. A heterodecamer stands out sharply and illustrates the structural diversity of cellular antioxidant enzymes. Figure: Joris Messens
