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Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC

Nature Structural & Molecular Biology volume 24, pages 611–619 (2017)Cite this article

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Abstract

Chaperones, which assist protein folding are essential components of every living cell. The yeast ribosome-associated complex (RAC) is a chaperone that is highly conserved in eukaryotic cells. The RAC consists of the J protein Zuo1 and the unconventional Hsp70 homolog Ssz1. The RAC heterodimer stimulates the ATPase activity of the ribosome-bound Hsp70 homolog Ssb, which interacts with nascent polypeptide chains to facilitate de novo protein folding. In addition, the RAC–Ssb system is required to maintain the fidelity of protein translation. Recent work reveals important details of the unique structures of RAC and Ssb and identifies how the chaperones interact with the ribosome. The new findings start to uncover how the exceptional chaperone triad cooperates in protein folding and maintenance of translational fidelity and its connection to extraribosomal functions.

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Figure 1: Structures of the Hsp70 homologs Ssz1 and Ssb.
Figure 2: Structure-based models of the RAC heterodimer and of its interaction with the ribosome.
Figure 3: Ssb interacts with the ribosome via the C terminus of SBDα.
Figure 4: In vivo functions of the yeast RAC–Ssb system.
Figure 5: The mammalian ribosome-associated complex (mRAC).

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Acknowledgements

This work was supported by the Deutsche Forschungsgemeinschaft (DFG) through FOR967 (to I.S. and S.R.), GRK1188, SFB1036 and the Leibniz program (to I.S.), SFB 746 (to S.R.), and RO 1028/5-1 (to S.R.), and by the Excellence Initiative of the German federal and state governments [BIOSS-2] (to S.R). I.S. is an investigator of the Cluster of Excellence: CellNetworks. We thank C. Conz, F. Weyer, K. Lapouge, and G. Valentin Gese for careful reading and suggestions on the manuscript.

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  1. Institute of Biochemistry and Molecular Biology, ZBMZ, Medical Faculty, University of Freiburg, Freiburg, Germany

    Ying Zhang & Sabine Rospert

  2. BIOSS Centre for Biological Signaling Studies, University of Freiburg, Freiburg, Germany

    Ying Zhang & Sabine Rospert

  3. Heidelberg University Biochemistry Center (BZH), Heidelberg, Germany

    Irmgard Sinning

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  1. Ying Zhang
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  2. Irmgard Sinning
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Correspondence to Sabine Rospert.

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Zhang, Y., Sinning, I. & Rospert, S. Two chaperones locked in an embrace: structure and function of the ribosome-associated complex RAC. Nat Struct Mol Biol 24, 611–619 (2017). https://doi.org/10.1038/nsmb.3435

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