Cytoplasmic fluidity and the cold life: proteome stability is decoupled from viability in psychrophiles

Beatrice Caviglia, Stepan Timr, Marianne Guiral, Marie-Thérèse Giudici-Orticoni, Tilo Seydel, Christian Beck, Judith Peters (), Fabio Sterpone () and Alessandro Paciaroni ()
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Beatrice Caviglia: University of Perugia, Department of Physics and Geology
Stepan Timr: Czech Academy of Sciences, J. Heyrovsky Institute of Physical Chemistry
Marianne Guiral: BIP, CNRS, Aix-Marseille Université, Laboratoire de Bioénergétique et Ingénierie des Protéines
Marie-Thérèse Giudici-Orticoni: BIP, CNRS, Aix-Marseille Université, Laboratoire de Bioénergétique et Ingénierie des Protéines
Tilo Seydel: Institut Laue-Langevin
Christian Beck: Institut Laue-Langevin
Judith Peters: Institut Laue-Langevin
Fabio Sterpone: Laboratoire de Biochimie Théorique, Université Paris Cité, CNRS
Alessandro Paciaroni: University of Perugia, Department of Physics and Geology

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: Abstract Protein diffusion, critical for cellular metabolism, occurs in the highly crowded cytoplasm. Understanding how this dynamics changes when organisms are adapted to different thermal niches is a fundamental challenge in microbiology and biophysics. In Escherichia coli, protein diffusion undergoes a pronounced slowdown at temperatures near cellular death, coinciding with the early stages of unfolding. To determine whether this phenomenon is universal, we investigated psychrophilic and hyperthermophilic bacteria. In both species, a marked diffusion slowdown takes place at the onset of proteome melting. However, while the dynamic arrest is associated with the thermal death point for the hyperthermophilic proteome, the psychrophilic proteome maintains substantial mobility well beyond the cellular inactivation. The decoupling between metabolic viability and proteome dynamics and stability suggests that the functional processes of psychrophilic bacteria are temperature sensitive. This finding echoes the behavior of psychrophilic enzymes, manifesting a large temperature gap between optimal activity and unfolding. Protein diffusion is optimized to maintain functional fluidity at the organism’s working conditions, but its temperature dependence is controlled by the proteome folded state. Our findings redefine the relationship between cytoplasmic dynamics, proteome stability, and bacterial survival in cold environments.

Date: 2025
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DOI: 10.1038/s41467-025-65270-5

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