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.
Dual interaction of the Hsp70 J protein co-chaperone Zuotin with the 40S and 60S subunits of the ribosome
Kanghyun Lee,Ruchika Sharma,O. K. Shrestha,C. Bingman,E. Craig
Published 2016 in Nature Structural &Molecular Biology
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- Publication year
2016
- Venue
Nature Structural &Molecular Biology
- Publication date
2016-09-07
- Fields of study
Biology, Medicine
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- Source metadata
Semantic Scholar, PubMed
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