All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Diffusive dynamics of bacterial proteome as a proxy of cell death

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F23%3A00566839" target="_blank" >RIV/61388955:_____/23:00566839 - isvavai.cz</a>

  • Result on the web

    <a href="https://hdl.handle.net/11104/0338111" target="_blank" >https://hdl.handle.net/11104/0338111</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acscentsci.2c01078" target="_blank" >10.1021/acscentsci.2c01078</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Diffusive dynamics of bacterial proteome as a proxy of cell death

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    ACS Central Science

  • ISSN

    2374-7943

  • e-ISSN

    2374-7951

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    93-102

  • UT code for WoS article

    000914868100001

  • EID of the result in the Scopus database

    2-s2.0-85147138801