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Sequestration of Proteins in Stress Granules Relies on the In-Cell but Not the In Vitro Folding Stability

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F21%3A00548178" target="_blank" >RIV/61388955:_____/21:00548178 - isvavai.cz</a>

  • Result on the web

    <a href="http://hdl.handle.net/11104/0324283" target="_blank" >http://hdl.handle.net/11104/0324283</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/jacs.1c09589" target="_blank" >10.1021/jacs.1c09589</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Sequestration of Proteins in Stress Granules Relies on the In-Cell but Not the In Vitro Folding Stability

  • Original language description

    Stress granules (SGs) are among the most studied membraneless organelles that form upon heat stress (HS) to sequester unfolded, misfolded, or aggregated protein, supporting protein quality control (PQC) clearance. The folding states that are primarily associated with SGs, as well as the function of the phase separated environment in adjusting the energy landscapes, remain unknown. Here, we investigate the association of superoxide dismutase 1 (SOD1) proteins with different folding stabilities and aggregation propensities with condensates in cells, in vitro and by simulation. We find that irrespective of aggregation the folding stability determines the association of SOD1 with SGs in cells. In vitro and in silico experiments however suggest that the increased flexibility of the unfolded state constitutes only a minor driving force to associate with the dynamic biomolecular network of the condensate. Specific protein–protein interactions in the cytoplasm in comparison to SGs determine the partitioning of folding states between the respective phases during HS.

  • 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

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of the American Chemical Society

  • ISSN

    0002-7863

  • e-ISSN

    1520-5126

  • Volume of the periodical

    143

  • Issue of the periodical within the volume

    47

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    19909-19918

  • UT code for WoS article

    000750622600027

  • EID of the result in the Scopus database

    2-s2.0-85119911776