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Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain

Cotranslational chaperones assist in de novo folding of nascent polypeptides in all organisms. In yeast, the heterodimeric ribosome-associated complex (RAC) forms a unique chaperone triad with the Hsp70 homologue Ssb. We report the X-ray structure of full length Ssb in the ATP-bound open conformatio...

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Hauptverfasser: Gumiero, Andrea (VerfasserIn) , Conz, Charlotte (VerfasserIn) , Valentín Gesé, Genís (VerfasserIn) , Zhang, Ying (VerfasserIn) , Weyer, Felix Alexander (VerfasserIn) , Lapouge, Karine (VerfasserIn) , Kappes, Julia (VerfasserIn) , von Plehwe, Ulrike (VerfasserIn) , Schermann, Géza (VerfasserIn) , Fitzke, Edith (VerfasserIn) , Wölfle, Tina (VerfasserIn) , Fischer, Tamás (VerfasserIn) , Rospert, Sabine (VerfasserIn) , Sinning, Irmgard (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 24 Nov 2016
In: Nature Communications
Year: 2016, Jahrgang: 7
ISSN:20411723
DOI:10.1038/ncomms13563
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/ncomms13563
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/ncomms13563
Volltext
Verfasserangaben:Andrea Gumiero, Charlotte Conz, Genís Valentín Gesé, Ying Zhang, Felix Alexander Weyer, Karine Lapouge, Julia Kappes, Ulrike von Plehwe, Géza Schermann, Edith Fitzke, Tina Wölfle, Tamás Fischer, Sabine Rospert and Irmgard Sinning
Beschreibung
Zusammenfassung:Cotranslational chaperones assist in de novo folding of nascent polypeptides in all organisms. In yeast, the heterodimeric ribosome-associated complex (RAC) forms a unique chaperone triad with the Hsp70 homologue Ssb. We report the X-ray structure of full length Ssb in the ATP-bound open conformation at 2.6 Å resolution and identify a positively charged region in the α-helical lid domain (SBDα), which is present in all members of the Ssb-subfamily of Hsp70s. Mutational analysis demonstrates that this region is strictly required for ribosome binding. Crosslinking shows that Ssb binds close to the tunnel exit via contacts with both, ribosomal proteins and rRNA, and that specific contacts can be correlated with switching between the open (ATP-bound) and closed (ADP-bound) conformation. Taken together, our data reveal how Ssb dynamics on the ribosome allows for the efficient interaction with nascent chains upon RAC-mediated activation of ATP hydrolysis.
Beschreibung:Gesehen am 27.08.2020
Beschreibung:Online Resource
ISSN:20411723
DOI:10.1038/ncomms13563

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