Number of the records: 1  

Diffusive dynamics of bacterial proteome as a proxy of cell death

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    SYSNO ASEP0566839
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleDiffusive 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 TitleACS Central Science. - : American Chemical Society - ISSN 2374-7943
    Roč. 9, č. 1 (2023), s. 93-102
    Number of pages10 s.
    Languageeng - English
    CountryUS - United States
    KeywordsBacteria ; Diffusion ; Transport properties
    Subject RIVCF - Physical ; Theoretical Chemistry
    OECD categoryPhysical chemistry
    Method of publishingOpen access
    Institutional supportUFCH-W - RVO:61388955
    UT WOS000914868100001
    EID SCOPUS85147138801
    DOI10.1021/acscentsci.2c01078
    AnnotationTemperature 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.
    WorkplaceJ. Heyrovsky Institute of Physical Chemistry
    ContactMichaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196
    Year of Publishing2024
    Electronic addresshttps://hdl.handle.net/11104/0338111
Number of the records: 1  

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