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Structural characterization of a eukaryotic chaperone: the ribosome-associated complex

The eukaryotic ribosome-associated complex (RAC) chaperone is poorly understood. Structural analyses now provide insight into the catalytic inactivity and possible functions of the Ssz1 subunit and reveal that RAC interacts with the ribosome via the Zuo1 subunit. RAC crouches over the ribosomal exit...

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Bibliographic Details
Main Authors: Leidig, Christoph (Author) , Bange, Gert (Author) , Kopp, Jürgen (Author) , Amlacher, Stefan (Author) , Aravind, Ajay (Author) , Wickles, Stephan (Author) , Witte, Gregor (Author) , Hurt, Ed (Author) , Beckmann, Roland (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: 2013
In: Nature structural & molecular biology
Year: 2013, Volume: 20, Issue: 1, Pages: 23-28
ISSN:1545-9985
DOI:10.1038/nsmb.2447
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb.2447
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb.2447
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Author Notes:Christoph Leidig, Gert Bange, Jürgen Kopp, Stefan Amlacher, Ajay Aravind, Stephan Wickles, Gregor Witte, Ed Hurt, Roland Beckmann & Irmgard Sinning
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Summary:The eukaryotic ribosome-associated complex (RAC) chaperone is poorly understood. Structural analyses now provide insight into the catalytic inactivity and possible functions of the Ssz1 subunit and reveal that RAC interacts with the ribosome via the Zuo1 subunit. RAC crouches over the ribosomal exit tunnel, where its conformation may be controlled by the ribosomal expansion segment ES27.
Item Description:Gesehen am 17.01.2022
Published online 2 December 2012
Ergänzende Informationen sind im Online-Artikel verfügbar
Physical Description:Online Resource
ISSN:1545-9985
DOI:10.1038/nsmb.2447

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