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| Verfasst von: | Morán Luengo, Tania [VerfasserIn]  |
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| | Kityk, Roman [VerfasserIn] |
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| | Mayer, Matthias P. [VerfasserIn] |
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| | Rüdiger, Stefan G.D. [VerfasserIn] |
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| Titel: | Hsp90 breaks the deadlock of the Hsp70 chaperone system |
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| Verf.angabe: | Tania Morán Luengo, Roman Kityk, Matthias P. Mayer, Stefan G. D. Rüdiger |
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| E-Jahr: | 2018 |
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| Jahr: | [3 May 2018] |
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| Umfang: | 17 S. |
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| Illustrationen: | Illustrationen |
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| Fussnoten: | Published: April 26, 2018 ; Gesehen am 22.07.2019 |
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| Titel Quelle: | Enthalten in: Molecular cell |
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| Ort Quelle: | [Cambridge, Mass.] : Cell Press, 1997 |
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| Jahr Quelle: | 2018 |
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| Band/Heft Quelle: | 70 (2018,3) Seite 545-552, e1-e9 |
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| ISSN Quelle: | 1097-4164 |
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| Abstract: | Summary - Protein folding in the cell requires ATP-driven chaperone machines such as the conserved Hsp70 and Hsp90. It is enigmatic how these machines fold proteins. Here, we show that Hsp90 takes a key role in protein folding by breaking an Hsp70-inflicted folding block, empowering protein clients to fold on their own. At physiological concentrations, Hsp70 stalls productive folding by binding hydrophobic, core-forming segments. Hsp90 breaks this deadlock and restarts folding. Remarkably, neither Hsp70 nor Hsp90 alters the folding rate despite ensuring high folding yields. In fact, ATP-dependent chaperoning is restricted to the early folding phase. Thus, the Hsp70-Hsp90 cascade does not fold proteins, but instead prepares them for spontaneous, productive folding. This stop-start mechanism is conserved from bacteria to man, assigning also a general function to bacterial Hsp90, HtpG. We speculate that the decreasing hydrophobicity along the Hsp70-Hsp90 cascade may be crucial for enabling spontaneous folding. |
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| DOI: | doi:10.1016/j.molcel.2018.03.028 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1016/j.molcel.2018.03.028 |
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| | Volltext: http://www.sciencedirect.com/science/article/pii/S1097276518302314 |
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| | DOI: https://doi.org/10.1016/j.molcel.2018.03.028 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | DnaK |
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| | Hsp70 |
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| | Hsp90 |
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| | HtpG |
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| | luciferase |
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| | molecular chaperones |
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| | protein folding |
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| | protein quality control |
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| | proteostasis |
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| | steroid hormone receptor |
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| K10plus-PPN: | 1669528758 |
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| Verknüpfungen: | → Zeitschrift |
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Hsp90 breaks the deadlock of the Hsp70 chaperone system / Morán Luengo, Tania [VerfasserIn]; [3 May 2018] (Online-Ressource)
