Cytoplasmic fluidity and the cold life: proteome stability is decoupled from viability in psychrophiles
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F25%3A00642143" target="_blank" >RIV/61388955:_____/25:00642143 - isvavai.cz</a>
Result on the web
<a href="https://hdl.handle.net/11104/0372063" target="_blank" >https://hdl.handle.net/11104/0372063</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-025-65270-5" target="_blank" >10.1038/s41467-025-65270-5</a>
Alternative languages
Result language
angličtina
Original language name
Cytoplasmic fluidity and the cold life: proteome stability is decoupled from viability in psychrophiles
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Communications
ISSN
2041-1723
e-ISSN
2041-1723
Volume of the periodical
16
Issue of the periodical within the volume
NOV 2025
Country of publishing house
GB - UNITED KINGDOM
Number of pages
13
Pages from-to
10345
UT code for WoS article
001624438000016
EID of the result in the Scopus database
2-s2.0-105022738312