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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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