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

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 Fischer, Sabine Rospert () and Irmgard Sinning ()
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Andrea Gumiero: Heidelberg University Biochemistry Center (BZH)
Charlotte Conz: Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, 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
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
Tina Wölfle: Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
Tamás Fischer: Heidelberg University Biochemistry Center (BZH)
Sabine Rospert: Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
Irmgard Sinning: Heidelberg University Biochemistry Center (BZH)

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms13563

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