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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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Bibliographic Details
Main Authors: Zhang, Ying (Author) , Valentín Gesé, Genís (Author) , Conz, Charlotte (Author) , Lapouge, Karine (Author) , Kopp, Jürgen (Author) , Wölfle, Tina (Author) , Rospert, Sabine (Author) , Sinning, Irmgard (Author)
Format: Article (Journal)
Language:English
Published: [2020]
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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Summary: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.
Item Description:Gesehen am 17.04.2020
Physical Description:Online Resource
ISSN:2041-1723
DOI:10.1038/s41467-020-15313-w

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