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Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain

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  • Andrea Gumiero

    (Heidelberg University Biochemistry Center (BZH)
    Present address: Istituto Poligrafico e Zecca dello Stato S.p.A., Via Salaria, I–712–00138 Roma, Italy)

  • Charlotte Conz

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signaling Studies, University of Freiburg)

  • Genís Valentín Gesé

    (Heidelberg University Biochemistry Center (BZH))

  • Ying Zhang

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signaling Studies, University of Freiburg)

  • Felix Alexander Weyer

    (Heidelberg University Biochemistry Center (BZH))

  • Karine Lapouge

    (Heidelberg University Biochemistry Center (BZH))

  • Julia Kappes

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg)

  • Ulrike von Plehwe

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg)

  • Géza Schermann

    (Heidelberg University Biochemistry Center (BZH))

  • Edith Fitzke

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signaling Studies, University of Freiburg)

  • Tina Wölfle

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signaling Studies, University of Freiburg)

  • Tamás Fischer

    (Heidelberg University Biochemistry Center (BZH)
    Present address: The John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, Australia)

  • Sabine Rospert

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signaling Studies, University of Freiburg)

  • Irmgard Sinning

    (Heidelberg University Biochemistry Center (BZH))

Abstract

Cotranslational chaperones assist in de novo folding of nascent polypeptides in all organisms. In yeast, the heterodimeric ribosome-associated complex (RAC) forms a unique chaperone triad with the Hsp70 homologue Ssb. We report the X-ray structure of full length Ssb in the ATP-bound open conformation at 2.6 Å resolution and identify a positively charged region in the α-helical lid domain (SBDα), which is present in all members of the Ssb-subfamily of Hsp70s. Mutational analysis demonstrates that this region is strictly required for ribosome binding. Crosslinking shows that Ssb binds close to the tunnel exit via contacts with both, ribosomal proteins and rRNA, and that specific contacts can be correlated with switching between the open (ATP-bound) and closed (ADP-bound) conformation. Taken together, our data reveal how Ssb dynamics on the ribosome allows for the efficient interaction with nascent chains upon RAC-mediated activation of ATP hydrolysis.

Suggested Citation

  • Andrea Gumiero & Charlotte Conz & Genís Valentín Gesé & Ying Zhang & Felix Alexander Weyer & Karine Lapouge & Julia Kappes & Ulrike von Plehwe & Géza Schermann & Edith Fitzke & Tina Wölfle & Tamás Fis, 2016. "Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain," Nature Communications, Nature, vol. 7(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13563
    DOI: 10.1038/ncomms13563
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    Cited by:

    1. Yan Chen & Bin Tsai & Ningning Li & Ning Gao, 2022. "Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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