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Decoding the Role of the Global Proteome Dynamics for Cellular Thermal Stability
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SYSNO ASEP 0583573 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Decoding the Role of the Global Proteome Dynamics for Cellular Thermal Stability Author(s) Caviglia, B. (FR)
Di Bari, D. (IT)
Timr, Štěpán (UFCH-W)
Guiral, M. (FR)
Giudici-Orticoni, M.-T. (FR)
Petrillo, C. (IT)
Peters, J. (FR)
Sterpone, F. (FR)
Paciaroni, A. (IT)Source Title Journal of Physical Chemistry Letters. - : American Chemical Society - ISSN 1948-7185
Roč. 15, č. 5 (2024), s. 1435-1441Number of pages 7 s. Language eng - English Country US - United States Keywords neutron-scattering ; proteins ; temperature ; adaptation ; diffusion ; viscosity ; extinctions ; evolution ; powder ; limits Subject RIV CF - Physical ; Theoretical Chemistry OECD category Physical chemistry Method of publishing Limited access Institutional support UFCH-W - RVO:61388955 UT WOS 001158986700001 EID SCOPUS 85184665864 DOI 10.1021/acs.jpclett.3c03351 Annotation Molecular mechanisms underlying the thermal response of cells remain elusive. On the basis of the recent result that the short-time diffusive dynamics of the Escherichia coli proteome is an excellent indicator of temperature-dependent bacterial metabolism and death, we used neutron scattering (NS) spectroscopy and molecular dynamics (MD) simulations to investigate the sub-nanosecond proteome mobility in psychro-, meso-, and hyperthermophilic bacteria over a wide temperature range. The magnitude of thermal fluctuations, measured by atomic mean square displacements, is similar among all studied bacteria at their respective thermal cell death. Global roto-translational motions turn out to be the main factor distinguishing the bacterial dynamical properties. We ascribe this behavior to the difference in the average proteome net charge, which becomes less negative for increasing bacterial thermal stability. We propose that the chemical-physical properties of the cytoplasm and the global dynamics of the resulting proteome are fine-tuned by evolution to uphold optimal thermal stability conditions. Workplace J. Heyrovsky Institute of Physical Chemistry Contact Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Year of Publishing 2025 Electronic address https://hdl.handle.net/11104/0351578
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