The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb
The ribosome-associated complex (RAC), which contains the Hsp40 protein Zuo1 and the non-canonical Hsp70 protein Ssz1 forms a chaperone triad with the fungal-specific Hsp70 protein Ssb. Here the authors combine X-ray crystallography, crosslinking and biochemical experiments and present the structure...
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| Main Authors: | , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
[2020]
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| In: |
Nature Communications
Year: 2020, Volume: 11 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-020-15313-w |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/s41467-020-15313-w Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/s41467-020-15313-w 
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| Author Notes: | Ying Zhang, Genís Valentín Gesé, Charlotte Conz, Karine Lapouge, Jürgen Kopp, Tina Wölfle, Sabine Rospert, Irmgard Sinning |
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| 520 | |a The ribosome-associated complex (RAC), which contains the Hsp40 protein Zuo1 and the non-canonical Hsp70 protein Ssz1 forms a chaperone triad with the fungal-specific Hsp70 protein Ssb. Here the authors combine X-ray crystallography, crosslinking and biochemical experiments and present the structure of the Zuo1 N-terminus bound to Ssz1 and demonstrate that Ssz1 is an active chaperone for nascent chains. | ||
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