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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| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article (Journal) |
| Language: | English |
| Published: |
2013
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| 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 |
| 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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| 520 | |a 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. | ||
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