Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits

Lee, K., Sharma, R., Shrestha, O. K., Bingman, C. A., Craig, E. A. (November 2016) Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits. Nat Struct Mol Biol, 23 (11). pp. 1003-1010. ISSN 1545-9993 (Print)1545-9985 (Linking)

URL: https://www.ncbi.nlm.nih.gov/pubmed/27669034
DOI: 10.1038/nsmb.3299


Ribosome-associated J protein-Hsp70 chaperones promote nascent-polypeptide folding and normal translational fidelity. The J protein Zuo1 is known to span the ribosomal subunits, but understanding of its function is limited. Here we present new structural and cross-linking data allowing more precise positioning of Saccharomyces cerevisiae Zuo1 near the 60S polypeptide-exit site and suggesting interactions of Zuo1 with the ribosomal protein eL31 and 25S rRNA helix 24. The junction between the 60S-interacting and subunit-spanning helices is a hinge that positions Zuo1 on the 40S yet accommodates subunit rotation. Interaction between the Zuo1 C terminus and 40S occurs via 18S rRNA expansion segment 12 (ES12) of helix 44, which originates at the decoding site. Deletions in either ES12 or the Zuo1 C terminus alter readthrough of stop codons and -1 frameshifting. Our study offers insight into how this cotranslational chaperone system may monitor decoding-site activity and nascent-polypeptide transit, thereby coordinating protein translation and folding.

Item Type: Paper
Subjects: organs, tissues, organelles, cell types and functions > organelles, types and functions > ribosome
structural biology
Investigative techniques and equipment > x ray crystallography
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: November 2016
Date Deposited: 01 Dec 2016 16:06
Last Modified: 01 Dec 2016 16:06
PMCID: PMC5097012
Related URLs:
URI: https://repository.cshl.edu/id/eprint/33914

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