Počet záznamů: 1
Sequestration of Proteins in Stress Granules Relies on the In-Cell but Not the In Vitro Folding Stability
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SYSNO ASEP 0548178 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Sequestration of Proteins in Stress Granules Relies on the In-Cell but Not the In Vitro Folding Stability Tvůrce(i) Samanta, N. (DE)
Ribeiro, S. S. (DE)
Becker, M. (DE)
Laborie, E. (FR)
Pollak, R. (DE)
Timr, Štěpán (UFCH-W)
Sterpone, F. (FR)
Ebbinghaus, S.G. (DE)Zdroj.dok. Journal of the American Chemical Society. - : American Chemical Society - ISSN 0002-7863
Roč. 143, č. 47 (2021), s. 19909-19918Poč.str. 10 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova Stress granules ; In Vitro Folding Stability ; heat stress Vědní obor RIV CF - Fyzikální chemie a teoretická chemie Obor OECD Physical chemistry Způsob publikování Open access Institucionální podpora UFCH-W - RVO:61388955 UT WOS 000750622600027 EID SCOPUS 85119911776 DOI 10.1021/jacs.1c09589 Anotace 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. Pracoviště Ústav fyzikální chemie J.Heyrovského Kontakt Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Rok sběru 2022 Elektronická adresa http://hdl.handle.net/11104/0324283
Počet záznamů: 1