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Diffusive dynamics of bacterial proteome as a proxy of cell death
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SYSNO ASEP 0566839 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Diffusive dynamics of bacterial proteome as a proxy of cell death Author(s) Di Barri, D. (FR)
Timr, Štěpán (UFCH-W)
Guiral, M. (FR)
Giudici-Orticoni, M.-T. (FR)
Seydel, T. (FR)
Beck, Ch. (FR)
Petrillo, C. (IT)
Derreumaux, P. (FR)
Melchionna, S. (IT)
Sterpone, F. (FR)
Peters, J. (FR)
Paciaroni, A. (IT)Source Title ACS Central Science. - : American Chemical Society - ISSN 2374-7943
Roč. 9, č. 1 (2023), s. 93-102Number of pages 10 s. Language eng - English Country US - United States Keywords Bacteria ; Diffusion ; Transport properties Subject RIV CF - Physical ; Theoretical Chemistry OECD category Physical chemistry Method of publishing Open access Institutional support UFCH-W - RVO:61388955 UT WOS 000914868100001 EID SCOPUS 85147138801 DOI 10.1021/acscentsci.2c01078 Annotation Temperature variations have a big impact on bacterial metabolism and death, yet an exhaustive molecular picture of these processes is still missing. For instance, whether thermal death is determined by the deterioration of the whole or a specific part of the proteome is hotly debated. Here, by monitoring the proteome dynamics of E. coli, we clearly show that only a minor fraction of the proteome unfolds at the cell death. First, we prove that the dynamical state of the E. coli proteome is an excellent proxy for temperature-dependent bacterial metabolism and death. The proteome diffusive dynamics peaks at about the bacterial optimal growth temperature, then a dramatic dynamical slowdown is observed that starts just below the cell’s death temperature. Next, we show that this slowdown is caused by the unfolding of just a small fraction of proteins that establish an entangling interprotein network, dominated by hydrophobic interactions, across the cytoplasm. Finally, the deduced progress of the proteome unfolding and its diffusive dynamics are both key to correctly reproduce the E. coli growth rate. Workplace J. Heyrovsky Institute of Physical Chemistry Contact Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Year of Publishing 2024 Electronic address https://hdl.handle.net/11104/0338111
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